Skip to main content
Top
Published in:
Cover of the book

2015 | OriginalPaper | Chapter

Sialic Acid Receptors of Viruses

Authors : Mikhail Matrosovich, Georg Herrler, Hans Dieter Klenk

Published in: SialoGlyco Chemistry and Biology II

Publisher: Springer International Publishing

Activate our intelligent search to find suitable subject content or patents.

search-config
loading …

Abstract

Sialic acid linked to glycoproteins and gangliosides is used by many viruses as a receptor for cell entry. These viruses include important human and animal pathogens, such as influenza, parainfluenza, mumps, corona, noro, rota, and DNA tumor viruses. Attachment to sialic acid is mediated by receptor binding proteins that are constituents of viral envelopes or exposed at the surface of non-enveloped viruses. Some of these viruses are also equipped with a neuraminidase or a sialyl-O-acetyl-esterase. These receptor-destroying enzymes promote virus release from infected cells and neutralize sialic acid-containing soluble proteins interfering with cell surface binding of the virus. Variations in the receptor specificity are important determinants for host range, tissue tropism, pathogenicity, and transmissibility of these viruses.

Dont have a licence yet? Then find out more about our products and how to get one now:

Springer Professional "Wirtschaft+Technik"

Online-Abonnement

Mit Springer Professional "Wirtschaft+Technik" erhalten Sie Zugriff auf:

  • über 102.000 Bücher
  • über 537 Zeitschriften

aus folgenden Fachgebieten:

  • Automobil + Motoren
  • Bauwesen + Immobilien
  • Business IT + Informatik
  • Elektrotechnik + Elektronik
  • Energie + Nachhaltigkeit
  • Finance + Banking
  • Management + Führung
  • Marketing + Vertrieb
  • Maschinenbau + Werkstoffe
  • Versicherung + Risiko

Jetzt Wissensvorsprung sichern!

Springer Professional "Technik"

Online-Abonnement

Mit Springer Professional "Technik" erhalten Sie Zugriff auf:

  • über 67.000 Bücher
  • über 390 Zeitschriften

aus folgenden Fachgebieten:

  • Automobil + Motoren
  • Bauwesen + Immobilien
  • Business IT + Informatik
  • Elektrotechnik + Elektronik
  • Energie + Nachhaltigkeit
  • Maschinenbau + Werkstoffe




 

Jetzt Wissensvorsprung sichern!

Literature
1.
go back to reference Hirst GK (1941) The agglutination of red cells by allantoic fluid of chick embryos infected with influenza virus. Science 94:22–23 Hirst GK (1941) The agglutination of red cells by allantoic fluid of chick embryos infected with influenza virus. Science 94:22–23
2.
go back to reference McClelland L, Hare R (1941) The adsorption of influenza virus by red cells and a new in vitro method of measuring antibodies for influenza virus. Can J Public Health 32:530–538 McClelland L, Hare R (1941) The adsorption of influenza virus by red cells and a new in vitro method of measuring antibodies for influenza virus. Can J Public Health 32:530–538
3.
go back to reference Burnet FM, Stone JD (1947) The receptor-destroying enzyme of V. cholerae. Aust J Exp Biol Med Sci 25:227–233 Burnet FM, Stone JD (1947) The receptor-destroying enzyme of V. cholerae. Aust J Exp Biol Med Sci 25:227–233
4.
go back to reference Gottschalk A, Lind PE (1949) Product of interaction between influenza virus enzyme and ovomucin. Nature 164:232 Gottschalk A, Lind PE (1949) Product of interaction between influenza virus enzyme and ovomucin. Nature 164:232
5.
go back to reference Klenk E, Faillard H, Lempfrid H (1955) Über die enzymatische Wirkung von Influenza Virus. Z physiol Chem 301:235–246 Klenk E, Faillard H, Lempfrid H (1955) Über die enzymatische Wirkung von Influenza Virus. Z physiol Chem 301:235–246
6.
go back to reference de Groot RJ (2006) Structure, function and evolution of the hemagglutinin-esterase proteins of corona- and toroviruses. Glycoconj J 23:59–72 de Groot RJ (2006) Structure, function and evolution of the hemagglutinin-esterase proteins of corona- and toroviruses. Glycoconj J 23:59–72
7.
go back to reference Lehmann F, Tiralongo E, Tiralongo J (2006) Sialic acid-specific lectins: occurrence, specificity and function. Cell Mol Life Sci 63:1331–1354 Lehmann F, Tiralongo E, Tiralongo J (2006) Sialic acid-specific lectins: occurrence, specificity and function. Cell Mol Life Sci 63:1331–1354
8.
go back to reference Neu U, Stehle T, Atwood WJ (2009) The Polyomaviridae: contributions of virus structure to our understanding of virus receptors and infectious entry. Virology 384:389–399 Neu U, Stehle T, Atwood WJ (2009) The Polyomaviridae: contributions of virus structure to our understanding of virus receptors and infectious entry. Virology 384:389–399
9.
go back to reference Olofsson S, Bergstrom T (2005) Glycoconjugate glycans as viral receptors. Ann Med 37:154–172 Olofsson S, Bergstrom T (2005) Glycoconjugate glycans as viral receptors. Ann Med 37:154–172
10.
go back to reference Taube S, Jiang M, Wobus CE (2010) Glycosphingolipids as receptors for non-enveloped viruses. Viruses 2:1011–1049 Taube S, Jiang M, Wobus CE (2010) Glycosphingolipids as receptors for non-enveloped viruses. Viruses 2:1011–1049
11.
go back to reference McCauley JW, Hongo S, Kaverin NV, Kochs G, Lamb RA, Matrosovich MN, Perez DR, Palese P, Presti RM, Rimstadt E et al. (2011) Orthomyxoviridae. In: King AMQ, Adams MJ, Carstens EB, Lefkowitz EJ (eds) Virus taxonomy. Elsevier, Oxford, pp 749–762 McCauley JW, Hongo S, Kaverin NV, Kochs G, Lamb RA, Matrosovich MN, Perez DR, Palese P, Presti RM, Rimstadt E et al. (2011) Orthomyxoviridae. In: King AMQ, Adams MJ, Carstens EB, Lefkowitz EJ (eds) Virus taxonomy. Elsevier, Oxford, pp 749–762
12.
go back to reference Palese P, Shaw ML (2007) Orthomyxoviridae: the viruses and their replication. In: Knipe DM, Howley PM (eds) Fields virology. Lippincott, Williams and Wilkins, Philadelphia, pp 1647–1689 Palese P, Shaw ML (2007) Orthomyxoviridae: the viruses and their replication. In: Knipe DM, Howley PM (eds) Fields virology. Lippincott, Williams and Wilkins, Philadelphia, pp 1647–1689
13.
go back to reference Tong S, Li Y, Rivailler P, Conrardy C, Castillo DA, Chen LM, Recuenco S, Ellison JA, Davis CT, York IA et al. (2012) A distinct lineage of influenza A virus from bats. Proc Natl Acad Sci U S A 109:4269–4274 Tong S, Li Y, Rivailler P, Conrardy C, Castillo DA, Chen LM, Recuenco S, Ellison JA, Davis CT, York IA et al. (2012) A distinct lineage of influenza A virus from bats. Proc Natl Acad Sci U S A 109:4269–4274
14.
go back to reference Klenk HD (2011) Influenza virology. In: von Itzstein M (ed) Influenza virus sialidase – a drug discovery target. Springer, Basel, pp 1–29 Klenk HD (2011) Influenza virology. In: von Itzstein M (ed) Influenza virus sialidase – a drug discovery target. Springer, Basel, pp 1–29
15.
go back to reference Gamblin SJ, Skehel JJ (2010) Influenza hemagglutinin and neuraminidase membrane glycoproteins. J Biol Chem 285:28403–28409 Gamblin SJ, Skehel JJ (2010) Influenza hemagglutinin and neuraminidase membrane glycoproteins. J Biol Chem 285:28403–28409
16.
go back to reference Skehel JJ, Wiley DC (2000) Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin. Annu Rev Biochem 69:531–569 Skehel JJ, Wiley DC (2000) Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin. Annu Rev Biochem 69:531–569
17.
go back to reference Matrosovich MN, Klenk H-D, Kawaoka Y (2006) Receptor specificity, host range and pathogenicity of influenza viruses. In: Kawaoka Y (ed) Influenza virology: current topics. Caister Academic, Wymondham, pp 95–137 Matrosovich MN, Klenk H-D, Kawaoka Y (2006) Receptor specificity, host range and pathogenicity of influenza viruses. In: Kawaoka Y (ed) Influenza virology: current topics. Caister Academic, Wymondham, pp 95–137
18.
go back to reference Connor RJ, Kawaoka Y, Webster RG, Paulson JC (1994) Receptor specificity in human, avian, and equine H2 and H3 influenza virus isolates. Virology 205:17–23 Connor RJ, Kawaoka Y, Webster RG, Paulson JC (1994) Receptor specificity in human, avian, and equine H2 and H3 influenza virus isolates. Virology 205:17–23
19.
go back to reference Matrosovich M, Tuzikov A, Bovin N, Gambarian A, Klimov A, Cox N, Castrucci M, Donatelli I, Kawaoka Y (2000) Alterations of receptor-binding properties of H1, H2 and H3 avian influenza virus hemagglutinins upon introduction into mammals. J Virol 74:8502–8512 Matrosovich M, Tuzikov A, Bovin N, Gambarian A, Klimov A, Cox N, Castrucci M, Donatelli I, Kawaoka Y (2000) Alterations of receptor-binding properties of H1, H2 and H3 avian influenza virus hemagglutinins upon introduction into mammals. J Virol 74:8502–8512
20.
go back to reference Rogers GN, Paulson JC (1983) Receptor determinants of human and animal influenza virus isolates: differences in receptor specificity of the H3 hemagglutinin based on species of origin. Virology 127:361–373 Rogers GN, Paulson JC (1983) Receptor determinants of human and animal influenza virus isolates: differences in receptor specificity of the H3 hemagglutinin based on species of origin. Virology 127:361–373
21.
go back to reference Baum LG, Paulson JC (1990) Sialyloligosaccharides of the respiratory epithelium in the selection of human influenza virus receptor specificity. Acta Histochem Suppl 40:35–38 Baum LG, Paulson JC (1990) Sialyloligosaccharides of the respiratory epithelium in the selection of human influenza virus receptor specificity. Acta Histochem Suppl 40:35–38
22.
go back to reference Gambaryan A, Webster R, Matrosovich M (2002) Differences between influenza virus receptors on target cells of duck and chicken. Arch Virol 147:1197–1208 Gambaryan A, Webster R, Matrosovich M (2002) Differences between influenza virus receptors on target cells of duck and chicken. Arch Virol 147:1197–1208
23.
go back to reference Ito T, Couceiro JN, Kelm S, Baum LG, Krauss S, Castrucci MR, Donatelli I, Kida H, Paulson JC, Webster RG et al. (1998) Molecular basis for the generation in pigs of influenza A viruses with pandemic potential. J Virol 72:7367–7373 Ito T, Couceiro JN, Kelm S, Baum LG, Krauss S, Castrucci MR, Donatelli I, Kida H, Paulson JC, Webster RG et al. (1998) Molecular basis for the generation in pigs of influenza A viruses with pandemic potential. J Virol 72:7367–7373
24.
go back to reference Kuchipudi SV, Nelli R, White GA, Bain M, Chang KC, Dunham S (2009) Differences in influenza virus receptors in chickens and ducks: implications for interspecies transmission. J Mol Genet Med 3:143–151 Kuchipudi SV, Nelli R, White GA, Bain M, Chang KC, Dunham S (2009) Differences in influenza virus receptors in chickens and ducks: implications for interspecies transmission. J Mol Genet Med 3:143–151
25.
go back to reference Pillai SP, Lee CW (2010) Species and age related differences in the type and distribution of influenza virus receptors in different tissues of chickens, ducks and turkeys. Virol J 7:5 Pillai SP, Lee CW (2010) Species and age related differences in the type and distribution of influenza virus receptors in different tissues of chickens, ducks and turkeys. Virol J 7:5
26.
go back to reference Shinya K, Ebina M, Yamada S, Ono M, Kasai N, Kawaoka Y (2006) Avian flu: influenza virus receptors in the human airway. Nature 440:435–436 Shinya K, Ebina M, Yamada S, Ono M, Kasai N, Kawaoka Y (2006) Avian flu: influenza virus receptors in the human airway. Nature 440:435–436
27.
go back to reference Matrosovich M, Stech J, Klenk HD (2009) Influenza receptors, polymerase and host range. Rev Sci Tech 28:203–217 Matrosovich M, Stech J, Klenk HD (2009) Influenza receptors, polymerase and host range. Rev Sci Tech 28:203–217
28.
go back to reference Matrosovich MN, Gambarian AS, Klenk HD (2008) Receptor specificity of influenza viruses and its alteration during interspecies transmission. In: Klenk HD, Matrosovich MN, Stech J (eds) Avian Influenza. Karger, Basel, pp 134–155 Matrosovich MN, Gambarian AS, Klenk HD (2008) Receptor specificity of influenza viruses and its alteration during interspecies transmission. In: Klenk HD, Matrosovich MN, Stech J (eds) Avian Influenza. Karger, Basel, pp 134–155
29.
go back to reference Gambaryan A, Tuzikov A, Pazynina G, Bovin N, Balish A, Klimov A (2006) Evolution of the receptor binding phenotype of influenza A (H5) viruses. Virology 344:432–438 Gambaryan A, Tuzikov A, Pazynina G, Bovin N, Balish A, Klimov A (2006) Evolution of the receptor binding phenotype of influenza A (H5) viruses. Virology 344:432–438
30.
go back to reference Matrosovich M, Zhou N, Kawaoka Y, Webster R (1999) The surface glycoproteins of H5 influenza viruses isolated from humans, chickens, and wild aquatic birds have distinguishable properties. J Virol 73:1146–1155 Matrosovich M, Zhou N, Kawaoka Y, Webster R (1999) The surface glycoproteins of H5 influenza viruses isolated from humans, chickens, and wild aquatic birds have distinguishable properties. J Virol 73:1146–1155
31.
go back to reference Stevens J, Blixt O, Tumpey TM, Taubenberger JK, Paulson JC, Wilson IA (2006) Structure and receptor specificity of the hemagglutinin from an H5N1 influenza virus. Science 312:404–410 Stevens J, Blixt O, Tumpey TM, Taubenberger JK, Paulson JC, Wilson IA (2006) Structure and receptor specificity of the hemagglutinin from an H5N1 influenza virus. Science 312:404–410
32.
go back to reference Matrosovich MN, Matrosovich TY, Gray T, Roberts NA, Klenk HD (2004) Human and avian influenza viruses target different cell types in cultures of human airway epithelium. Proc Natl Acad Sci U S A 101:4620–4624 Matrosovich MN, Matrosovich TY, Gray T, Roberts NA, Klenk HD (2004) Human and avian influenza viruses target different cell types in cultures of human airway epithelium. Proc Natl Acad Sci U S A 101:4620–4624
33.
go back to reference Nicholls JM, Chan MC, Chan WY, Wong HK, Cheung CY, Kwong DL, Wong MP, Chui WH, Poon LL, Tsao SW et al. (2007) Tropism of avian influenza A (H5N1) in the upper and lower respiratory tract. Nat Med 13:147–149 Nicholls JM, Chan MC, Chan WY, Wong HK, Cheung CY, Kwong DL, Wong MP, Chui WH, Poon LL, Tsao SW et al. (2007) Tropism of avian influenza A (H5N1) in the upper and lower respiratory tract. Nat Med 13:147–149
34.
go back to reference van Riel D, Munster VJ, de Wit E, Rimmelzwaan GF, Fouchier RA, Osterhaus AD, Kuiken T (2006) H5N1 virus attachment to lower respiratory tract. Science 312:399 van Riel D, Munster VJ, de Wit E, Rimmelzwaan GF, Fouchier RA, Osterhaus AD, Kuiken T (2006) H5N1 virus attachment to lower respiratory tract. Science 312:399
35.
go back to reference van Riel D, Munster VJ, de Wit E, Rimmelzwaan GF, Fouchier RA, Osterhaus AD, Kuiken T (2007) Human and avian influenza viruses target different cells in the lower respiratory tract of humans and other mammals. Am J Pathol 171:1215–1223 van Riel D, Munster VJ, de Wit E, Rimmelzwaan GF, Fouchier RA, Osterhaus AD, Kuiken T (2007) Human and avian influenza viruses target different cells in the lower respiratory tract of humans and other mammals. Am J Pathol 171:1215–1223
37.
go back to reference Herfst S, Schrauwen EJ, Linster M, Chutinimitkul S, de Wit E, Munster VJ, Sorrell EM, Bestebroer TM, Burke DF, Smith DJ et al. (2012) Airborne transmission of influenza A/H5N1 virus between ferrets. Science 336:1534–1541 Herfst S, Schrauwen EJ, Linster M, Chutinimitkul S, de Wit E, Munster VJ, Sorrell EM, Bestebroer TM, Burke DF, Smith DJ et al. (2012) Airborne transmission of influenza A/H5N1 virus between ferrets. Science 336:1534–1541
38.
go back to reference Imai M, Watanabe T, Hatta M, Das SC, Ozawa M, Shinya K, Zhong G, Hanson A, Katsura H, Watanabe S et al. (2012) Experimental adaptation of an influenza H5 HA confers respiratory droplet transmission to a reassortant H5 HA/H1N1 virus in ferrets. Nature 486:420–428 Imai M, Watanabe T, Hatta M, Das SC, Ozawa M, Shinya K, Zhong G, Hanson A, Katsura H, Watanabe S et al. (2012) Experimental adaptation of an influenza H5 HA confers respiratory droplet transmission to a reassortant H5 HA/H1N1 virus in ferrets. Nature 486:420–428
39.
go back to reference Scholtissek C, Hinshaw VS, Olsen CW (1998) Influenza in pigs and their role as the intermediate host. In: Nicholson KG, Webster RG, Hay A (eds) Textbook of influenza. Blackwell Science, London, pp 137–145 Scholtissek C, Hinshaw VS, Olsen CW (1998) Influenza in pigs and their role as the intermediate host. In: Nicholson KG, Webster RG, Hay A (eds) Textbook of influenza. Blackwell Science, London, pp 137–145
40.
go back to reference Gambaryan AS, Karasin AI, Tuzikov AB, Chinarev AA, Pazynina GV, Bovin NV, Matrosovich MN, Olsen CW, Klimov AI (2005) Receptor-binding properties of swine influenza viruses isolated and propagated in MDCK cells. Virus Res 114:15–22 Gambaryan AS, Karasin AI, Tuzikov AB, Chinarev AA, Pazynina GV, Bovin NV, Matrosovich MN, Olsen CW, Klimov AI (2005) Receptor-binding properties of swine influenza viruses isolated and propagated in MDCK cells. Virus Res 114:15–22
41.
go back to reference Van Poucke SG, Nicholls JM, Nauwynck HJ, Van Reeth K (2010) Replication of avian, human and swine influenza viruses in porcine respiratory explants and association with sialic acid distribution. Virol J 7:38 Van Poucke SG, Nicholls JM, Nauwynck HJ, Van Reeth K (2010) Replication of avian, human and swine influenza viruses in porcine respiratory explants and association with sialic acid distribution. Virol J 7:38
42.
go back to reference Bradley KC, Jones CA, Tompkins SM, Tripp RA, Russell RJ, Gramer MR, Heimburg-Molinaro J, Smith DF, Cummings RD, Steinhauer DA (2011) Comparison of the receptor binding properties of contemporary swine isolates and early human pandemic H1N1 isolates (Novel 2009 H1N1). Virology 413:169–182 Bradley KC, Jones CA, Tompkins SM, Tripp RA, Russell RJ, Gramer MR, Heimburg-Molinaro J, Smith DF, Cummings RD, Steinhauer DA (2011) Comparison of the receptor binding properties of contemporary swine isolates and early human pandemic H1N1 isolates (Novel 2009 H1N1). Virology 413:169–182
43.
go back to reference Chen LM, Rivailler P, Hossain J, Carney P, Balish A, Perry I, Davis CT, Garten R, Shu B, Xu X et al. (2011) Receptor specificity of subtype H1 influenza A viruses isolated from swine and humans in the United States. Virology 412:401–410 Chen LM, Rivailler P, Hossain J, Carney P, Balish A, Perry I, Davis CT, Garten R, Shu B, Xu X et al. (2011) Receptor specificity of subtype H1 influenza A viruses isolated from swine and humans in the United States. Virology 412:401–410
44.
go back to reference Maines TR, Jayaraman A, Belser JA, Wadford DA, Pappas C, Zeng H, Gustin KM, Pearce MB, Viswanathan K, Shriver ZH et al. (2009) Transmission and pathogenesis of swine-origin 2009 A(H1N1) influenza viruses in ferrets and mice. Science 325:484–487 Maines TR, Jayaraman A, Belser JA, Wadford DA, Pappas C, Zeng H, Gustin KM, Pearce MB, Viswanathan K, Shriver ZH et al. (2009) Transmission and pathogenesis of swine-origin 2009 A(H1N1) influenza viruses in ferrets and mice. Science 325:484–487
46.
go back to reference Childs RA, Palma AS, Wharton S, Matrosovich T, Liu Y, Chai W, Campanero-Rhodes MA, Zhang Y, Eickmann M, Kiso M et al. (2009) Receptor-binding specificity of pandemic influenza A (H1N1) 2009 virus determined by carbohydrate microarray. Nat Biotechnol 27:797–799 Childs RA, Palma AS, Wharton S, Matrosovich T, Liu Y, Chai W, Campanero-Rhodes MA, Zhang Y, Eickmann M, Kiso M et al. (2009) Receptor-binding specificity of pandemic influenza A (H1N1) 2009 virus determined by carbohydrate microarray. Nat Biotechnol 27:797–799
47.
go back to reference Kilander A, Rykkvin R, Dudman SG, Hungnes O (2010) Observed association between the HA1 mutation D222G in the 2009 pandemic influenza A(H1N1) virus and severe clinical outcome, Norway 2009–2010. Euro Surveill 15(9):pii=19498 Kilander A, Rykkvin R, Dudman SG, Hungnes O (2010) Observed association between the HA1 mutation D222G in the 2009 pandemic influenza A(H1N1) virus and severe clinical outcome, Norway 2009–2010. Euro Surveill 15(9):pii=19498
48.
go back to reference Puzelli S, Facchini M, De Marco MA, Palmieri A, Spagnolo D, Boros S, Corcioli F, Trotta D, Bagnarelli P, Azzi A, Cassone A, Rezza G, Pompa MG, Oleari F, Donatelli I, the Influnet Surveillance Group for Pandemic A(H1N1) 2009 Influenza Virus in Italy (2010) Molecular surveillance of pandemic influenza A(H1N1) viruses circulating in Italy from May 2009 to February 2010: association between haemagglutinin mutations and clinical outcome. Euro Surveill 15(43):pii=19696 Puzelli S, Facchini M, De Marco MA, Palmieri A, Spagnolo D, Boros S, Corcioli F, Trotta D, Bagnarelli P, Azzi A, Cassone A, Rezza G, Pompa MG, Oleari F, Donatelli I, the Influnet Surveillance Group for Pandemic A(H1N1) 2009 Influenza Virus in Italy (2010) Molecular surveillance of pandemic influenza A(H1N1) viruses circulating in Italy from May 2009 to February 2010: association between haemagglutinin mutations and clinical outcome. Euro Surveill 15(43):pii=19696
49.
go back to reference Liu Y, Childs RA, Matrosovich T, Wharton S, Palma AS, Chai W, Daniels R, Gregory V, Uhlendorff J, Kiso M et al. (2010) Altered receptor specificity and cell tropism of D222G hemagglutinin mutants isolated from fatal cases of pandemic A(H1N1) 2009 influenza virus. J Virol 84:12069–12074 Liu Y, Childs RA, Matrosovich T, Wharton S, Palma AS, Chai W, Daniels R, Gregory V, Uhlendorff J, Kiso M et al. (2010) Altered receptor specificity and cell tropism of D222G hemagglutinin mutants isolated from fatal cases of pandemic A(H1N1) 2009 influenza virus. J Virol 84:12069–12074
50.
go back to reference Chutinimitkul S, Herfst S, Steel J, Lowen AC, Ye J, van Riel D, Schrauwen EJ, Bestebroer TM, Koel B, Burke DF et al. (2010) Virulence-associated substitution D222G in the hemagglutinin of 2009 pandemic influenza A(H1N1) virus affects receptor binding. J Virol 84:11802–11813 Chutinimitkul S, Herfst S, Steel J, Lowen AC, Ye J, van Riel D, Schrauwen EJ, Bestebroer TM, Koel B, Burke DF et al. (2010) Virulence-associated substitution D222G in the hemagglutinin of 2009 pandemic influenza A(H1N1) virus affects receptor binding. J Virol 84:11802–11813
51.
go back to reference Matrosovich MN, Gambaryan AS, Teneberg S, Piskarev VE, Yamnikova SS, Lvov DK, Robertson JS, Karlsson KA (1997) Avian influenza A viruses differ from human viruses by recognition of sialyloligosaccharides and gangliosides and by a higher conservation of the HA receptor-binding site. Virology 233:224–234 Matrosovich MN, Gambaryan AS, Teneberg S, Piskarev VE, Yamnikova SS, Lvov DK, Robertson JS, Karlsson KA (1997) Avian influenza A viruses differ from human viruses by recognition of sialyloligosaccharides and gangliosides and by a higher conservation of the HA receptor-binding site. Virology 233:224–234
52.
go back to reference Nicholls JM, Chan RW, Russell RJ, Air GM, Peiris JS (2008) Evolving complexities of influenza virus and its receptors. Trends Microbiol 16:149–157 Nicholls JM, Chan RW, Russell RJ, Air GM, Peiris JS (2008) Evolving complexities of influenza virus and its receptors. Trends Microbiol 16:149–157
53.
go back to reference Varghese JN, Laver WG, Colman PM (1983) Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 A resolution. Nature 303:35–40 Varghese JN, Laver WG, Colman PM (1983) Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 A resolution. Nature 303:35–40
54.
go back to reference Blok J, Air GM (1982) Block deletions in the neuraminidase genes from some influenza A viruses of the N1 subtype. Virology 118:229–234 Blok J, Air GM (1982) Block deletions in the neuraminidase genes from some influenza A viruses of the N1 subtype. Virology 118:229–234
55.
go back to reference Matrosovich MN, Matrosovich TY, Gray T, Roberts NA, Klenk HD (2004) Neuraminidase is important for the initiation of influenza virus infection in human airway epithelium. J Virol 78:12665–12667 Matrosovich MN, Matrosovich TY, Gray T, Roberts NA, Klenk HD (2004) Neuraminidase is important for the initiation of influenza virus infection in human airway epithelium. J Virol 78:12665–12667
56.
go back to reference Palese P, Tobita K, Ueda M, Compans RW (1974) Characterization of temperature sensitive influenza virus mutants defective in neuraminidase. Virology 61:397–410 Palese P, Tobita K, Ueda M, Compans RW (1974) Characterization of temperature sensitive influenza virus mutants defective in neuraminidase. Virology 61:397–410
57.
go back to reference Banks J, Speidel ES, Moore E, Plowright L, Piccirillo A, Capua I, Cordioli P, Fioretti A, Alexander DJ (2001) Changes in the haemagglutinin and the neuraminidase genes prior to the emergence of highly pathogenic H7N1 avian influenza viruses in Italy. Arch Virol 146:963–973 Banks J, Speidel ES, Moore E, Plowright L, Piccirillo A, Capua I, Cordioli P, Fioretti A, Alexander DJ (2001) Changes in the haemagglutinin and the neuraminidase genes prior to the emergence of highly pathogenic H7N1 avian influenza viruses in Italy. Arch Virol 146:963–973
58.
go back to reference Kaverin NV, Gambaryan AS, Bovin NV, Rudneva IA, Shilov AA, Khodova OM, Varich NL, Sinitsin BV, Makarova NV, Kropotkina EA (1998) Postreassortment changes in influenza A virus hemagglutinin restoring HA-NA functional match. Virology 244:315–321 Kaverin NV, Gambaryan AS, Bovin NV, Rudneva IA, Shilov AA, Khodova OM, Varich NL, Sinitsin BV, Makarova NV, Kropotkina EA (1998) Postreassortment changes in influenza A virus hemagglutinin restoring HA-NA functional match. Virology 244:315–321
59.
go back to reference Mitnaul LJ, Matrosovich MN, Castrucci MR, Tuzikov AB, Bovin NV, Kobasa D, Kawaoka Y (2000) Balanced hemagglutinin and neuraminidase activities are critical for efficient replication of influenza A virus. J Virol 74:6015–6020 Mitnaul LJ, Matrosovich MN, Castrucci MR, Tuzikov AB, Bovin NV, Kobasa D, Kawaoka Y (2000) Balanced hemagglutinin and neuraminidase activities are critical for efficient replication of influenza A virus. J Virol 74:6015–6020
60.
go back to reference Wagner R, Matrosovich M, Klenk HD (2002) Functional balance between haemagglutinin and neuraminidase in influenza virus infections. Rev Med Virol 12:159–166 Wagner R, Matrosovich M, Klenk HD (2002) Functional balance between haemagglutinin and neuraminidase in influenza virus infections. Rev Med Virol 12:159–166
61.
go back to reference Wagner R, Wolff T, Herwig A, Pleschka S, Klenk HD (2000) Interdependence of hemagglutinin glycosylation and neuraminidase as regulators of influenza virus growth: a study by reverse genetics. J Virol 74:6316–6323 Wagner R, Wolff T, Herwig A, Pleschka S, Klenk HD (2000) Interdependence of hemagglutinin glycosylation and neuraminidase as regulators of influenza virus growth: a study by reverse genetics. J Virol 74:6316–6323
62.
go back to reference Hausmann J, Kretzschmar E, Garten W, Klenk HD (1995) N1 neuraminidase of influenza virus A/FPV/Rostock/34 has haemadsorbing activity. J Gen Virol 76(Pt 7):1719–1728 Hausmann J, Kretzschmar E, Garten W, Klenk HD (1995) N1 neuraminidase of influenza virus A/FPV/Rostock/34 has haemadsorbing activity. J Gen Virol 76(Pt 7):1719–1728
63.
go back to reference Kobasa D, Rodgers ME, Wells K, Kawaoka Y (1997) Neuraminidase hemadsorption activity, conserved in avian influenza A viruses, does not influence viral replication in ducks. J Virol 71:6706–6713 Kobasa D, Rodgers ME, Wells K, Kawaoka Y (1997) Neuraminidase hemadsorption activity, conserved in avian influenza A viruses, does not influence viral replication in ducks. J Virol 71:6706–6713
64.
go back to reference Laver WG, Colman PM, Webster RG, Hinshaw VS, Air GM (1984) Influenza virus neuraminidase with hemagglutinin activity. Virology 137:314–323 Laver WG, Colman PM, Webster RG, Hinshaw VS, Air GM (1984) Influenza virus neuraminidase with hemagglutinin activity. Virology 137:314–323
65.
go back to reference Varghese JN, Colman PM, van Donkelaar A, Blick TJ, Sahasrabudhe A, McKimm-Breschkin JL (1997) Structural evidence for a second sialic acid binding site in avian influenza virus neuraminidases. Proc Natl Acad Sci U S A 94:11808–11812 Varghese JN, Colman PM, van Donkelaar A, Blick TJ, Sahasrabudhe A, McKimm-Breschkin JL (1997) Structural evidence for a second sialic acid binding site in avian influenza virus neuraminidases. Proc Natl Acad Sci U S A 94:11808–11812
66.
go back to reference Uhlendorff J, Matrosovich T, Klenk HD, Matrosovich M (2009) Functional significance of the hemadsorption activity of influenza virus neuraminidase and its alteration in pandemic viruses. Arch Virol 154:945–957 Uhlendorff J, Matrosovich T, Klenk HD, Matrosovich M (2009) Functional significance of the hemadsorption activity of influenza virus neuraminidase and its alteration in pandemic viruses. Arch Virol 154:945–957
67.
go back to reference Herrler G, Hausmann J, Klenk HD (1995) Sialic acid as receptor determinant of ortho- and paramyxoviruses. In: Rosenberg A (ed) Biology of the Sialic acids. Plenum, New York, pp 315–336 Herrler G, Hausmann J, Klenk HD (1995) Sialic acid as receptor determinant of ortho- and paramyxoviruses. In: Rosenberg A (ed) Biology of the Sialic acids. Plenum, New York, pp 315–336
68.
go back to reference Herrler G, Klenk HD (1991) Structure and function of the HEF glycoprotein of influenza C virus. Adv Virus Res 40:213–234 Herrler G, Klenk HD (1991) Structure and function of the HEF glycoprotein of influenza C virus. Adv Virus Res 40:213–234
69.
go back to reference Rosenthal PB, Zhang X, Formanowski F, Fitz W, Wong CH, Meier-Ewert H, Skehel JJ, Wiley DC (1998) Structure of the haemagglutinin-esterase-fusion glycoprotein of influenza C virus. Nature 396:92–96 Rosenthal PB, Zhang X, Formanowski F, Fitz W, Wong CH, Meier-Ewert H, Skehel JJ, Wiley DC (1998) Structure of the haemagglutinin-esterase-fusion glycoprotein of influenza C virus. Nature 396:92–96
70.
go back to reference Herrler G, Rott R, Klenk HD, Muller HP, Shukla AK, Schauer R (1985) The receptor-destroying enzyme of influenza C virus is neuraminate-O-acetylesterase. EMBO J 4:1503–1506 Herrler G, Rott R, Klenk HD, Muller HP, Shukla AK, Schauer R (1985) The receptor-destroying enzyme of influenza C virus is neuraminate-O-acetylesterase. EMBO J 4:1503–1506
71.
go back to reference Herrler G, Multhaup G, Beyreuther K, Klenk HD (1988) Serine 71 of the glycoprotein HEF is located at the active site of the acetylesterase of influenza C virus. Arch Virol 102:269–274 Herrler G, Multhaup G, Beyreuther K, Klenk HD (1988) Serine 71 of the glycoprotein HEF is located at the active site of the acetylesterase of influenza C virus. Arch Virol 102:269–274
72.
go back to reference Pleschka S, Klenk HD, Herrler G (1995) The catalytic triad of the influenza C virus glycoprotein HEF esterase: characterization by site-directed mutagenesis and functional analysis. J Gen Virol 76:2529–2537 Pleschka S, Klenk HD, Herrler G (1995) The catalytic triad of the influenza C virus glycoprotein HEF esterase: characterization by site-directed mutagenesis and functional analysis. J Gen Virol 76:2529–2537
73.
go back to reference Vlasak R, Muster T, Lauro AM, Powers JC, Palese P (1989) Influenza C virus esterase: analysis of catalytic site, inhibition, and possible function. J Virol 63:2056–2062 Vlasak R, Muster T, Lauro AM, Powers JC, Palese P (1989) Influenza C virus esterase: analysis of catalytic site, inhibition, and possible function. J Virol 63:2056–2062
74.
go back to reference Hofling K, Klenk HD, Herrler G (1997) Inactivation of inhibitors by the receptor-destroying enzyme of influenza C virus. J Gen Virol 78:567–570 Hofling K, Klenk HD, Herrler G (1997) Inactivation of inhibitors by the receptor-destroying enzyme of influenza C virus. J Gen Virol 78:567–570
75.
go back to reference Hofling K, Brossmer R, Klenk H, Herrler G (1996) Transfer of an esterase-resistant receptor analog to the surface of influenza C virions results in reduced infectivity due to aggregate formation. Virology 218:127–133 Hofling K, Brossmer R, Klenk H, Herrler G (1996) Transfer of an esterase-resistant receptor analog to the surface of influenza C virions results in reduced infectivity due to aggregate formation. Virology 218:127–133
76.
go back to reference Herrler G, Gross HJ, Brossmer R (1995) A synthetic sialic acid analog that is resistant to the receptor-destroying enzyme can be used by influenza C virus as a receptor determinant for infection of cells. Biochem Biophys Res Commun 216:821–827 Herrler G, Gross HJ, Brossmer R (1995) A synthetic sialic acid analog that is resistant to the receptor-destroying enzyme can be used by influenza C virus as a receptor determinant for infection of cells. Biochem Biophys Res Commun 216:821–827
77.
go back to reference Herrler G, Gross HJ, Imhof A, Brossmer R, Milks G, Paulson JC (1992) A synthetic sialic acid analogue is recognized by influenza C virus as a receptor determinant but is resistant to the receptor-destroying enzyme. J Biol Chem 267:12501–12505 Herrler G, Gross HJ, Imhof A, Brossmer R, Milks G, Paulson JC (1992) A synthetic sialic acid analogue is recognized by influenza C virus as a receptor determinant but is resistant to the receptor-destroying enzyme. J Biol Chem 267:12501–12505
78.
go back to reference Rogers GN, Herrler G, Paulson JC, Klenk HD (1986) Influenza C virus uses 9-O-acetyl-N-acetylneuraminic acid as a high affinity receptor determinant for attachment to cells. J Biol Chem 261:5947–5951 Rogers GN, Herrler G, Paulson JC, Klenk HD (1986) Influenza C virus uses 9-O-acetyl-N-acetylneuraminic acid as a high affinity receptor determinant for attachment to cells. J Biol Chem 261:5947–5951
79.
go back to reference Herrler G, Klenk HD (1987) The surface receptor is a major determinant of the cell tropism of influenza C virus. Virology 159:102–108 Herrler G, Klenk HD (1987) The surface receptor is a major determinant of the cell tropism of influenza C virus. Virology 159:102–108
80.
go back to reference Zimmer G, Klenk HD, Herrler G (1995) Identification of a 40-kDa cell surface sialoglycoprotein with the characteristics of a major influenza C virus receptor in a Madin–Darby canine kidney cell line. J Biol Chem 270:17815–17822 Zimmer G, Klenk HD, Herrler G (1995) Identification of a 40-kDa cell surface sialoglycoprotein with the characteristics of a major influenza C virus receptor in a Madin–Darby canine kidney cell line. J Biol Chem 270:17815–17822
81.
go back to reference Zimmer G, Lottspeich F, Maisner A, Klenk HD, Herrler G (1997) Molecular characterization of gp40, a mucin-type glycoprotein from the apical plasma membrane of Madin–Darby canine kidney cells (type I). Biochem J 326:99–108 Zimmer G, Lottspeich F, Maisner A, Klenk HD, Herrler G (1997) Molecular characterization of gp40, a mucin-type glycoprotein from the apical plasma membrane of Madin–Darby canine kidney cells (type I). Biochem J 326:99–108
82.
go back to reference Marschall M, Herrler G, Boswald C, Foerst G, Meier-Ewert H (1994) Persistent influenza C virus possesses distinct functional properties due to a modified HEF glycoprotein. J Gen Virol 75:2189–2196 Marschall M, Herrler G, Boswald C, Foerst G, Meier-Ewert H (1994) Persistent influenza C virus possesses distinct functional properties due to a modified HEF glycoprotein. J Gen Virol 75:2189–2196
83.
go back to reference Matsuzaki M, Sugawara K, Adachi K, Hongo S, Nishimura H, Kitame F, Nakamura K (1992) Location of neutralizing epitopes on the hemagglutinin-esterase protein of influenza C virus. Virology 189:79–87 Matsuzaki M, Sugawara K, Adachi K, Hongo S, Nishimura H, Kitame F, Nakamura K (1992) Location of neutralizing epitopes on the hemagglutinin-esterase protein of influenza C virus. Virology 189:79–87
84.
go back to reference Szepanski S, Gross HJ, Brossmer R, Klenk HD, Herrler G (1992) A single point mutation of the influenza C virus glycoprotein (HEF) changes the viral receptor-binding activity. Virology 188:85–92 Szepanski S, Gross HJ, Brossmer R, Klenk HD, Herrler G (1992) A single point mutation of the influenza C virus glycoprotein (HEF) changes the viral receptor-binding activity. Virology 188:85–92
85.
go back to reference Umetsu Y, Sugawara K, Nishimura H, Hongo S, Matsuzaki M, Kitame F, Nakamura K (1992) Selection of antigenically distinct variants of influenza C viruses by the host cell. Virology 189:740–744 Umetsu Y, Sugawara K, Nishimura H, Hongo S, Matsuzaki M, Kitame F, Nakamura K (1992) Selection of antigenically distinct variants of influenza C viruses by the host cell. Virology 189:740–744
86.
go back to reference Falk K, Namork E, Rimstad E, Mjaaland S, Dannevig BH (1997) Characterization of infectious salmon anemia virus, an orthomyxo-like virus isolated from Atlantic salmon (Salmo salar L.). J Virol 71:9016–9023 Falk K, Namork E, Rimstad E, Mjaaland S, Dannevig BH (1997) Characterization of infectious salmon anemia virus, an orthomyxo-like virus isolated from Atlantic salmon (Salmo salar L.). J Virol 71:9016–9023
87.
go back to reference Kristiansen M, Froystad MK, Rishovd AL, Gjoen T (2002) Characterization of the receptor-destroying enzyme activity from infectious salmon anaemia virus. J Gen Virol 83:2693–2697 Kristiansen M, Froystad MK, Rishovd AL, Gjoen T (2002) Characterization of the receptor-destroying enzyme activity from infectious salmon anaemia virus. J Gen Virol 83:2693–2697
88.
go back to reference Hellebo A, Vilas U, Falk K, Vlasak R (2004) Infectious salmon anemia virus specifically binds to and hydrolyzes 4-O-acetylated sialic acids. J Virol 78:3055–3062 Hellebo A, Vilas U, Falk K, Vlasak R (2004) Infectious salmon anemia virus specifically binds to and hydrolyzes 4-O-acetylated sialic acids. J Virol 78:3055–3062
89.
go back to reference Falk K, Aspehaug V, Vlasak R, Endresen C (2004) Identification and characterization of viral structural proteins of infectious salmon anemia virus. J Virol 78:3063–3071 Falk K, Aspehaug V, Vlasak R, Endresen C (2004) Identification and characterization of viral structural proteins of infectious salmon anemia virus. J Virol 78:3063–3071
90.
go back to reference Krossoy B, Devold M, Sanders L, Knappskog PM, Aspehaug V, Falk K, Nylund A, Koumans S, Endresen C, Biering E (2001) Cloning and identification of the infectious salmon anaemia virus haemagglutinin. J Gen Virol 82:1757–1765 Krossoy B, Devold M, Sanders L, Knappskog PM, Aspehaug V, Falk K, Nylund A, Koumans S, Endresen C, Biering E (2001) Cloning and identification of the infectious salmon anaemia virus haemagglutinin. J Gen Virol 82:1757–1765
91.
go back to reference Rimstad E, Mjaaland S, Snow M, Mikalsen AB, Cunningham CO (2001) Characterization of the infectious salmon anemia virus genomic segment that encodes the putative hemagglutinin. J Virol 75:5352–5356 Rimstad E, Mjaaland S, Snow M, Mikalsen AB, Cunningham CO (2001) Characterization of the infectious salmon anemia virus genomic segment that encodes the putative hemagglutinin. J Virol 75:5352–5356
92.
go back to reference Vlasak R, Luytjes W, Spaan W, Palese P (1988) Human and bovine coronaviruses recognize sialic acid-containing receptors similar to those of influenza C viruses. Proc Natl Acad Sci U S A 85:4526–4529 Vlasak R, Luytjes W, Spaan W, Palese P (1988) Human and bovine coronaviruses recognize sialic acid-containing receptors similar to those of influenza C viruses. Proc Natl Acad Sci U S A 85:4526–4529
93.
go back to reference Schultze B, Wahn K, Klenk HD, Herrler G (1991) Isolated HE-protein from hemagglutinating encephalomyelitis virus and bovine coronavirus has receptor-destroying and receptor-binding activity. Virology 180:221–228 Schultze B, Wahn K, Klenk HD, Herrler G (1991) Isolated HE-protein from hemagglutinating encephalomyelitis virus and bovine coronavirus has receptor-destroying and receptor-binding activity. Virology 180:221–228
94.
go back to reference Vlasak R, Luytjes W, Leider J, Spaan W, Palese P (1988) The E3 protein of bovine coronavirus is a receptor-destroying enzyme with acetylesterase activity. J Virol 62:4686–4690 Vlasak R, Luytjes W, Leider J, Spaan W, Palese P (1988) The E3 protein of bovine coronavirus is a receptor-destroying enzyme with acetylesterase activity. J Virol 62:4686–4690
95.
go back to reference Yokomori K, La Monica N, Makino S, Shieh CK, Lai MM (1989) Biosynthesis, structure, and biological activities of envelope protein gp65 of murine coronavirus. Virology 173:683–691 Yokomori K, La Monica N, Makino S, Shieh CK, Lai MM (1989) Biosynthesis, structure, and biological activities of envelope protein gp65 of murine coronavirus. Virology 173:683–691
96.
go back to reference Zeng Q, Langereis MA, van Vliet AL, Huizinga EG, de Groot RJ (2008) Structure of coronavirus hemagglutinin-esterase offers insight into corona and influenza virus evolution. Proc Natl Acad Sci U S A 105:9065–9069 Zeng Q, Langereis MA, van Vliet AL, Huizinga EG, de Groot RJ (2008) Structure of coronavirus hemagglutinin-esterase offers insight into corona and influenza virus evolution. Proc Natl Acad Sci U S A 105:9065–9069
97.
go back to reference Sugiyama K, Kasai M, Kato S, Kasai H, Hatakeyama K (1998) Haemagglutinin-esterase protein (HE) of murine corona virus: DVIM (diarrhea virus of infant mice). Arch Virol 143:1523–1534 Sugiyama K, Kasai M, Kato S, Kasai H, Hatakeyama K (1998) Haemagglutinin-esterase protein (HE) of murine corona virus: DVIM (diarrhea virus of infant mice). Arch Virol 143:1523–1534
98.
go back to reference Klausegger A, Strobl B, Regl G, Kaser A, Luytjes W, Vlasak R (1999) Identification of a coronavirus hemagglutinin-esterase with a substrate specificity different from those of influenza C virus and bovine coronavirus. J Virol 73:3737–3743 Klausegger A, Strobl B, Regl G, Kaser A, Luytjes W, Vlasak R (1999) Identification of a coronavirus hemagglutinin-esterase with a substrate specificity different from those of influenza C virus and bovine coronavirus. J Virol 73:3737–3743
99.
go back to reference Regl G, Kaser A, Iwersen M, Schmid H, Kohla G, Strobl B, Vilas U, Schauer R, Vlasak R (1999) The hemagglutinin-esterase of mouse hepatitis virus strain S is a sialate-4-O-acetylesterase. J Virol 73:4721–4727 Regl G, Kaser A, Iwersen M, Schmid H, Kohla G, Strobl B, Vilas U, Schauer R, Vlasak R (1999) The hemagglutinin-esterase of mouse hepatitis virus strain S is a sialate-4-O-acetylesterase. J Virol 73:4721–4727
100.
go back to reference Smits SL, Gerwig GJ, van Vliet AL, Lissenberg A, Briza P, Kamerling JP, Vlasak R, de Groot RJ (2005) Nidovirus sialate-O-acetylesterases: evolution and substrate specificity of coronaviral and toroviral receptor-destroying enzymes. J Biol Chem 280:6933–6941 Smits SL, Gerwig GJ, van Vliet AL, Lissenberg A, Briza P, Kamerling JP, Vlasak R, de Groot RJ (2005) Nidovirus sialate-O-acetylesterases: evolution and substrate specificity of coronaviral and toroviral receptor-destroying enzymes. J Biol Chem 280:6933–6941
101.
go back to reference Storz J, Zhang XM, Rott R (1992) Comparison of hemagglutinating, receptor-destroying, and acetylesterase activities of avirulent and virulent bovine coronavirus strains. Arch Virol 125:193–204 Storz J, Zhang XM, Rott R (1992) Comparison of hemagglutinating, receptor-destroying, and acetylesterase activities of avirulent and virulent bovine coronavirus strains. Arch Virol 125:193–204
102.
go back to reference Schultze B, Herrler G (1992) Bovine coronavirus uses N-acetyl-9-O-acetylneuraminic acid as a receptor determinant to initiate the infection of cultured cells. J Gen Virol 73:901–906 Schultze B, Herrler G (1992) Bovine coronavirus uses N-acetyl-9-O-acetylneuraminic acid as a receptor determinant to initiate the infection of cultured cells. J Gen Virol 73:901–906
103.
go back to reference Lin X, O'Reilly KL, Storz J (1997) Infection of polarized epithelial cells with enteric and respiratory tract bovine coronaviruses and release of virus progeny. Am J Vet Res 58:1120–1124 Lin X, O'Reilly KL, Storz J (1997) Infection of polarized epithelial cells with enteric and respiratory tract bovine coronaviruses and release of virus progeny. Am J Vet Res 58:1120–1124
104.
go back to reference Schultze B, Krempl C, Ballesteros ML, Shaw L, Schauer R, Enjuanes L, Herrler G (1996) Transmissible gastroenteritis coronavirus, but not the related porcine respiratory coronavirus, has a sialic acid (N-glycolylneuraminic acid) binding activity. J Virol 70:5634–5637 Schultze B, Krempl C, Ballesteros ML, Shaw L, Schauer R, Enjuanes L, Herrler G (1996) Transmissible gastroenteritis coronavirus, but not the related porcine respiratory coronavirus, has a sialic acid (N-glycolylneuraminic acid) binding activity. J Virol 70:5634–5637
105.
go back to reference Schultze B, Zimmer G, Herrler G (1996) Virus entry into a polarized epithelial cell line (MDCK): similarities and dissimilarities between influenza C virus and bovine coronavirus. J Gen Virol 77(Pt 10):2507–2514 Schultze B, Zimmer G, Herrler G (1996) Virus entry into a polarized epithelial cell line (MDCK): similarities and dissimilarities between influenza C virus and bovine coronavirus. J Gen Virol 77(Pt 10):2507–2514
106.
go back to reference King B, Potts BJ, Brian DA (1985) Bovine coronavirus hemagglutinin protein. Virus Res 2:53–59 King B, Potts BJ, Brian DA (1985) Bovine coronavirus hemagglutinin protein. Virus Res 2:53–59
107.
go back to reference Yoo D, Graham FL, Prevec L, Parker MD, Benko M, Zamb T, Babiuk LA (1992) Synthesis and processing of the haemagglutinin-esterase glycoprotein of bovine coronavirus encoded in the E3 region of adenovirus. J Gen Virol 73:2591–2600 Yoo D, Graham FL, Prevec L, Parker MD, Benko M, Zamb T, Babiuk LA (1992) Synthesis and processing of the haemagglutinin-esterase glycoprotein of bovine coronavirus encoded in the E3 region of adenovirus. J Gen Virol 73:2591–2600
108.
go back to reference Schultze B, Gross HJ, Brossmer R, Herrler G (1991) The S protein of bovine coronavirus is a hemagglutinin recognizing 9-O-acetylated sialic acid as a receptor determinant. J Virol 65:6232–6237 Schultze B, Gross HJ, Brossmer R, Herrler G (1991) The S protein of bovine coronavirus is a hemagglutinin recognizing 9-O-acetylated sialic acid as a receptor determinant. J Virol 65:6232–6237
109.
go back to reference Gagneten S, Gout O, Dubois-Dalcq M, Rottier P, Rossen J, Holmes KV (1995) Interaction of mouse hepatitis virus (MHV) spike glycoprotein with receptor glycoprotein MHVR is required for infection with an MHV strain that expresses the hemagglutinin-esterase glycoprotein. J Virol 69:889–895 Gagneten S, Gout O, Dubois-Dalcq M, Rottier P, Rossen J, Holmes KV (1995) Interaction of mouse hepatitis virus (MHV) spike glycoprotein with receptor glycoprotein MHVR is required for infection with an MHV strain that expresses the hemagglutinin-esterase glycoprotein. J Virol 69:889–895
110.
go back to reference Langereis MA, van Vliet AL, Boot W, de Groot RJ (2010) Attachment of mouse hepatitis virus to O-acetylated sialic acid is mediated by hemagglutinin-esterase and not by the spike protein. J Virol 84:8970–8974 Langereis MA, van Vliet AL, Boot W, de Groot RJ (2010) Attachment of mouse hepatitis virus to O-acetylated sialic acid is mediated by hemagglutinin-esterase and not by the spike protein. J Virol 84:8970–8974
111.
go back to reference Noda M, Koide F, Asagi M, Inaba Y (1988) Physicochemical properties of transmissible gastroenteritis virus hemagglutinin. Arch Virol 99:163–172 Noda M, Koide F, Asagi M, Inaba Y (1988) Physicochemical properties of transmissible gastroenteritis virus hemagglutinin. Arch Virol 99:163–172
112.
go back to reference Noda M, Yamashita H, Koide F, Kadoi K, Omori T, Asagi M, Inaba Y (1987) Hemagglutination with transmissible gastroenteritis virus. Arch Virol 96:109–115 Noda M, Yamashita H, Koide F, Kadoi K, Omori T, Asagi M, Inaba Y (1987) Hemagglutination with transmissible gastroenteritis virus. Arch Virol 96:109–115
113.
go back to reference Krempl C, Schultze B, Laude H, Herrler G (1997) Point mutations in the S protein connect the sialic acid binding activity with the enteropathogenicity of transmissible gastroenteritis coronavirus. J Virol 71:3285–3287 Krempl C, Schultze B, Laude H, Herrler G (1997) Point mutations in the S protein connect the sialic acid binding activity with the enteropathogenicity of transmissible gastroenteritis coronavirus. J Virol 71:3285–3287
114.
go back to reference Bernard S, Laude H (1995) Site-specific alteration of transmissible gastroenteritis virus spike protein results in markedly reduced pathogenicity. J Gen Virol 76:2235–2241 Bernard S, Laude H (1995) Site-specific alteration of transmissible gastroenteritis virus spike protein results in markedly reduced pathogenicity. J Gen Virol 76:2235–2241
115.
go back to reference Krempl C, Ballesteros ML, Zimmer G, Enjuanes L, Klenk HD, Herrler G (2000) Characterization of the sialic acid binding activity of transmissible gastroenteritis coronavirus by analysis of haemagglutination-deficient mutants. J Gen Virol 81:489–496 Krempl C, Ballesteros ML, Zimmer G, Enjuanes L, Klenk HD, Herrler G (2000) Characterization of the sialic acid binding activity of transmissible gastroenteritis coronavirus by analysis of haemagglutination-deficient mutants. J Gen Virol 81:489–496
116.
go back to reference Schwegmann-Wessels C, Zimmer G, Schroder B, Breves G, Herrler G (2003) Binding of transmissible gastroenteritis coronavirus to brush border membrane sialoglycoproteins. J Virol 77:11846–11848 Schwegmann-Wessels C, Zimmer G, Schroder B, Breves G, Herrler G (2003) Binding of transmissible gastroenteritis coronavirus to brush border membrane sialoglycoproteins. J Virol 77:11846–11848
117.
go back to reference Pensaert M, Callebaut P, Vergote J (1986) Isolation of a porcine respiratory, non-enteric coronavirus related to transmissible gastroenteritis. Vet Q 8:257–261 Pensaert M, Callebaut P, Vergote J (1986) Isolation of a porcine respiratory, non-enteric coronavirus related to transmissible gastroenteritis. Vet Q 8:257–261
118.
go back to reference Delmas B, Gelfi J, L'Haridon R, Vogel LK, Sjostrom H, Noren O, Laude H (1992) Aminopeptidase N is a major receptor for the entero-pathogenic coronavirus TGEV. Nature 357:417–420 Delmas B, Gelfi J, L'Haridon R, Vogel LK, Sjostrom H, Noren O, Laude H (1992) Aminopeptidase N is a major receptor for the entero-pathogenic coronavirus TGEV. Nature 357:417–420
119.
go back to reference Cox E, Pensaert MB, Callebaut P, van Deun K (1990) Intestinal replication of a porcine respiratory coronavirus closely related antigenically to the enteric transmissible gastroenteritis virus. Vet Microbiol 23:237–243 Cox E, Pensaert MB, Callebaut P, van Deun K (1990) Intestinal replication of a porcine respiratory coronavirus closely related antigenically to the enteric transmissible gastroenteritis virus. Vet Microbiol 23:237–243
120.
go back to reference Schwegmann-Wessels C, Zimmer G, Laude H, Enjuanes L, Herrler G (2002) Binding of transmissible gastroenteritis coronavirus to cell surface sialoglycoproteins. J Virol 76:6037–6043 Schwegmann-Wessels C, Zimmer G, Laude H, Enjuanes L, Herrler G (2002) Binding of transmissible gastroenteritis coronavirus to cell surface sialoglycoproteins. J Virol 76:6037–6043
121.
go back to reference Schwegmann-Wessels C, Bauer S, Winter C, Enjuanes L, Laude H, Herrler G (2011) The sialic acid binding activity of the S protein facilitates infection by porcine transmissible gastroenteritis coronavirus. Virol J 8:435 Schwegmann-Wessels C, Bauer S, Winter C, Enjuanes L, Laude H, Herrler G (2011) The sialic acid binding activity of the S protein facilitates infection by porcine transmissible gastroenteritis coronavirus. Virol J 8:435
122.
go back to reference Bingham RW, Madge MH, Tyrrell DA (1975) Haemagglutination by avian infectious bronchitis virus – a coronavirus. J Gen Virol 28:381–390 Bingham RW, Madge MH, Tyrrell DA (1975) Haemagglutination by avian infectious bronchitis virus – a coronavirus. J Gen Virol 28:381–390
123.
go back to reference Schultze B, Cavanagh D, Herrler G (1992) Neuraminidase treatment of avian infectious bronchitis coronavirus reveals a hemagglutinating activity that is dependent on sialic acid-containing receptors on erythrocytes. Virology 189:792–794 Schultze B, Cavanagh D, Herrler G (1992) Neuraminidase treatment of avian infectious bronchitis coronavirus reveals a hemagglutinating activity that is dependent on sialic acid-containing receptors on erythrocytes. Virology 189:792–794
124.
go back to reference Winter C, Schwegmann-Wessels C, Cavanagh D, Neumann U, Herrler G (2006) Sialic acid is a receptor determinant for infection of cells by avian infectious bronchitis virus. J Gen Virol 87:1209–1216 Winter C, Schwegmann-Wessels C, Cavanagh D, Neumann U, Herrler G (2006) Sialic acid is a receptor determinant for infection of cells by avian infectious bronchitis virus. J Gen Virol 87:1209–1216
125.
go back to reference Abd El Rahman S, El-Kenawy AA, Neumann U, Herrler G, Winter C (2009) Comparative analysis of the sialic acid binding activity and the tropism for the respiratory epithelium of four different strains of avian infectious bronchitis virus. Avian Pathol 38:41–45 Abd El Rahman S, El-Kenawy AA, Neumann U, Herrler G, Winter C (2009) Comparative analysis of the sialic acid binding activity and the tropism for the respiratory epithelium of four different strains of avian infectious bronchitis virus. Avian Pathol 38:41–45
126.
go back to reference Abd El Rahman S, Winter C, El-Kenawy A, Neumann U, Herrler G (2010) Differential sensitivity of well-differentiated avian respiratory epithelial cells to infection by different strains of infectious bronchitis virus. J Virol 84:8949–8952 Abd El Rahman S, Winter C, El-Kenawy A, Neumann U, Herrler G (2010) Differential sensitivity of well-differentiated avian respiratory epithelial cells to infection by different strains of infectious bronchitis virus. J Virol 84:8949–8952
127.
go back to reference Winter C, Herrler G, Neumann U (2008) Infection of the tracheal epithelium by infectious bronchitis virus is sialic acid dependent. Microbes Infect 10:367–373 Winter C, Herrler G, Neumann U (2008) Infection of the tracheal epithelium by infectious bronchitis virus is sialic acid dependent. Microbes Infect 10:367–373
128.
go back to reference Cornelissen LA, Wierda CM, van der Meer FJ, Herrewegh AA, Horzinek MC, Egberink HF, de Groot RJ (1997) Hemagglutinin-esterase, a novel structural protein of torovirus. J Virol 71:5277–5286 Cornelissen LA, Wierda CM, van der Meer FJ, Herrewegh AA, Horzinek MC, Egberink HF, de Groot RJ (1997) Hemagglutinin-esterase, a novel structural protein of torovirus. J Virol 71:5277–5286
129.
go back to reference Duckmanton L, Tellier R, Richardson C, Petric M (1999) The novel hemagglutinin-esterase genes of human torovirus and Breda virus. Virus Res 64:137–149 Duckmanton L, Tellier R, Richardson C, Petric M (1999) The novel hemagglutinin-esterase genes of human torovirus and Breda virus. Virus Res 64:137–149
130.
go back to reference Langereis MA, Zeng Q, Gerwig GJ, Frey B, von Itzstein M, Kamerling JP, de Groot RJ, Huizinga EG (2009) Structural basis for ligand and substrate recognition by torovirus hemagglutinin esterases. Proc Natl Acad Sci U S A 106:15897–15902 Langereis MA, Zeng Q, Gerwig GJ, Frey B, von Itzstein M, Kamerling JP, de Groot RJ, Huizinga EG (2009) Structural basis for ligand and substrate recognition by torovirus hemagglutinin esterases. Proc Natl Acad Sci U S A 106:15897–15902
131.
go back to reference Lamb RA, Parks GD (2007) Paramyxoviridae: the viruses and their replication. In: Knipe DM, Howley PM (eds) Fields Virology. Lippincott, Williams and Wilkins, Philadelphia, pp 1449–1496 Lamb RA, Parks GD (2007) Paramyxoviridae: the viruses and their replication. In: Knipe DM, Howley PM (eds) Fields Virology. Lippincott, Williams and Wilkins, Philadelphia, pp 1449–1496
132.
go back to reference Zaitsev V, von Itzstein M, Groves D, Kiefel M, Takimoto T, Portner A, Taylor G (2004) Second sialic acid binding site in Newcastle disease virus hemagglutinin-neuraminidase: implications for fusion. J Virol 78:3733–3741 Zaitsev V, von Itzstein M, Groves D, Kiefel M, Takimoto T, Portner A, Taylor G (2004) Second sialic acid binding site in Newcastle disease virus hemagglutinin-neuraminidase: implications for fusion. J Virol 78:3733–3741
133.
go back to reference Lawrence MC, Borg NA, Streltsov VA, Pilling PA, Epa VC, Varghese JN, McKimm-Breschkin JL, Colman PM (2004) Structure of the haemagglutinin-neuraminidase from human parainfluenza virus type III. J Mol Biol 335:1343–1357 Lawrence MC, Borg NA, Streltsov VA, Pilling PA, Epa VC, Varghese JN, McKimm-Breschkin JL, Colman PM (2004) Structure of the haemagglutinin-neuraminidase from human parainfluenza virus type III. J Mol Biol 335:1343–1357
134.
go back to reference Yuan P, Thompson TB, Wurzburg BA, Paterson RG, Lamb RA, Jardetzky TS (2005) Structural studies of the parainfluenza virus 5 hemagglutinin-neuraminidase tetramer in complex with its receptor, sialyllactose. Structure 13:803–815 Yuan P, Thompson TB, Wurzburg BA, Paterson RG, Lamb RA, Jardetzky TS (2005) Structural studies of the parainfluenza virus 5 hemagglutinin-neuraminidase tetramer in complex with its receptor, sialyllactose. Structure 13:803–815
135.
go back to reference Alymova IV, Taylor G, Mishin VP, Watanabe M, Murti KG, Boyd K, Chand P, Babu YS, Portner A (2008) Loss of the N-linked glycan at residue 173 of human parainfluenza virus type 1 hemagglutinin-neuraminidase exposes a second receptor-binding site. J Virol 82:8400–8410 Alymova IV, Taylor G, Mishin VP, Watanabe M, Murti KG, Boyd K, Chand P, Babu YS, Portner A (2008) Loss of the N-linked glycan at residue 173 of human parainfluenza virus type 1 hemagglutinin-neuraminidase exposes a second receptor-binding site. J Virol 82:8400–8410
136.
go back to reference Holmgren J, Svennerholm L, Elwing H, Fredman P, Strannegard O (1980) Sendai virus receptor: proposed recognition structure based on binding to plastic-adsorbed gangliosides. Proc Natl Acad Sci U S A 77:1947–1950 Holmgren J, Svennerholm L, Elwing H, Fredman P, Strannegard O (1980) Sendai virus receptor: proposed recognition structure based on binding to plastic-adsorbed gangliosides. Proc Natl Acad Sci U S A 77:1947–1950
137.
go back to reference Markwell MA, Svennerholm L, Paulson JC (1981) Specific gangliosides function as host cell receptors for Sendai virus. Proc Natl Acad Sci U S A 78:5406–5410 Markwell MA, Svennerholm L, Paulson JC (1981) Specific gangliosides function as host cell receptors for Sendai virus. Proc Natl Acad Sci U S A 78:5406–5410
138.
go back to reference Markwell MA, Paulson JC (1980) Sendai virus utilizes specific sialyloligosaccharides as host cell receptor determinants. Proc Natl Acad Sci U S A 77:5693–5697 Markwell MA, Paulson JC (1980) Sendai virus utilizes specific sialyloligosaccharides as host cell receptor determinants. Proc Natl Acad Sci U S A 77:5693–5697
139.
go back to reference Suzuki Y, Suzuki T, Matsumoto M (1983) Isolation and characterization of receptor sialoglycoprotein for hemagglutinating virus of Japan (Sendai virus) from bovine erythrocyte membrane. J Biochem 93:1621–1633 Suzuki Y, Suzuki T, Matsumoto M (1983) Isolation and characterization of receptor sialoglycoprotein for hemagglutinating virus of Japan (Sendai virus) from bovine erythrocyte membrane. J Biochem 93:1621–1633
140.
go back to reference Suzuki Y, Suzuki T, Matsunaga M, Matsumoto M (1985) Gangliosides as paramyxovirus receptor. Structural requirement of sialo-oligosaccharides in receptors for hemagglutinating virus of Japan (Sendai virus) and Newcastle disease virus. J Biochem 97:1189–1199 Suzuki Y, Suzuki T, Matsunaga M, Matsumoto M (1985) Gangliosides as paramyxovirus receptor. Structural requirement of sialo-oligosaccharides in receptors for hemagglutinating virus of Japan (Sendai virus) and Newcastle disease virus. J Biochem 97:1189–1199
141.
go back to reference Suzuki T, Portner A, Scroggs RA, Uchikawa M, Koyama N, Matsuo K, Suzuki Y, Takimoto T (2001) Receptor specificities of human respiroviruses. J Virol 75:4604–4613 Suzuki T, Portner A, Scroggs RA, Uchikawa M, Koyama N, Matsuo K, Suzuki Y, Takimoto T (2001) Receptor specificities of human respiroviruses. J Virol 75:4604–4613
142.
go back to reference Prasad BV, Hardy ME, Dokland T, Bella J, Rossmann MG, Estes MK (1999) X-Ray crystallographic structure of the Norwalk virus capsid. Science 286:287–290 Prasad BV, Hardy ME, Dokland T, Bella J, Rossmann MG, Estes MK (1999) X-Ray crystallographic structure of the Norwalk virus capsid. Science 286:287–290
143.
go back to reference Prasad BV, Rothnagel R, Jiang X, Estes MK (1994) Three-dimensional structure of baculovirus-expressed Norwalk virus capsids. J Virol 68:5117–5125 Prasad BV, Rothnagel R, Jiang X, Estes MK (1994) Three-dimensional structure of baculovirus-expressed Norwalk virus capsids. J Virol 68:5117–5125
144.
go back to reference Bu W, Mamedova A, Tan M, Xia M, Jiang X, Hegde RS (2008) Structural basis for the receptor binding specificity of Norwalk virus. J Virol 82:5340–5347 Bu W, Mamedova A, Tan M, Xia M, Jiang X, Hegde RS (2008) Structural basis for the receptor binding specificity of Norwalk virus. J Virol 82:5340–5347
145.
go back to reference Cao S, Lou Z, Tan M, Chen Y, Liu Y, Zhang Z, Zhang XC, Jiang X, Li X, Rao Z (2007) Structural basis for the recognition of blood group trisaccharides by norovirus. J Virol 81:5949–5957 Cao S, Lou Z, Tan M, Chen Y, Liu Y, Zhang Z, Zhang XC, Jiang X, Li X, Rao Z (2007) Structural basis for the recognition of blood group trisaccharides by norovirus. J Virol 81:5949–5957
146.
go back to reference Choi JM, Hutson AM, Estes MK, Prasad BV (2008) Atomic resolution structural characterization of recognition of histo-blood group antigens by Norwalk virus. Proc Natl Acad Sci U S A 105:9175–9180 Choi JM, Hutson AM, Estes MK, Prasad BV (2008) Atomic resolution structural characterization of recognition of histo-blood group antigens by Norwalk virus. Proc Natl Acad Sci U S A 105:9175–9180
147.
go back to reference Katpally U, Voss NR, Cavazza T, Taube S, Rubin JR, Young VL, Stuckey J, Ward VK, Virgin HWT, Wobus CE et al. (2010) High-resolution cryo-electron microscopy structures of murine norovirus 1 and rabbit hemorrhagic disease virus reveal marked flexibility in the receptor binding domains. J Virol 84:5836–5841 Katpally U, Voss NR, Cavazza T, Taube S, Rubin JR, Young VL, Stuckey J, Ward VK, Virgin HWT, Wobus CE et al. (2010) High-resolution cryo-electron microscopy structures of murine norovirus 1 and rabbit hemorrhagic disease virus reveal marked flexibility in the receptor binding domains. J Virol 84:5836–5841
148.
go back to reference Taube S, Rubin JR, Katpally U, Smith TJ, Kendall A, Stuckey JA, Wobus CE (2010) High-resolution X-ray structure and functional analysis of the murine norovirus 1 capsid protein protruding domain. J Virol 84:5695–5705 Taube S, Rubin JR, Katpally U, Smith TJ, Kendall A, Stuckey JA, Wobus CE (2010) High-resolution X-ray structure and functional analysis of the murine norovirus 1 capsid protein protruding domain. J Virol 84:5695–5705
149.
go back to reference Wobus CE, Thackray LB, Virgin HWT (2006) Murine norovirus: a model system to study norovirus biology and pathogenesis. J Virol 80:5104–5112 Wobus CE, Thackray LB, Virgin HWT (2006) Murine norovirus: a model system to study norovirus biology and pathogenesis. J Virol 80:5104–5112
150.
go back to reference Estes MK, Prasad BV, Atmar RL (2006) Noroviruses everywhere: has something changed? Curr Opin Infect Dis 19:467–474 Estes MK, Prasad BV, Atmar RL (2006) Noroviruses everywhere: has something changed? Curr Opin Infect Dis 19:467–474
151.
go back to reference Le Pendu J, Ruvoen-Clouet N, Kindberg E, Svensson L (2006) Mendelian resistance to human norovirus infections. Semin Immunol 18:375–386 Le Pendu J, Ruvoen-Clouet N, Kindberg E, Svensson L (2006) Mendelian resistance to human norovirus infections. Semin Immunol 18:375–386
152.
go back to reference Tan M, Jiang X (2007) Norovirus-host interaction: implications for disease control and prevention. Expert Rev Mol Med 9:1–22 Tan M, Jiang X (2007) Norovirus-host interaction: implications for disease control and prevention. Expert Rev Mol Med 9:1–22
153.
go back to reference Tamura M, Natori K, Kobayashi M, Miyamura T, Takeda N (2004) Genogroup II noroviruses efficiently bind to heparan sulfate proteoglycan associated with the cellular membrane. J Virol 78:3817–3826 Tamura M, Natori K, Kobayashi M, Miyamura T, Takeda N (2004) Genogroup II noroviruses efficiently bind to heparan sulfate proteoglycan associated with the cellular membrane. J Virol 78:3817–3826
154.
go back to reference Rydell GE, Nilsson J, Rodriguez-Diaz J, Ruvoen-Clouet N, Svensson L, Le Pendu J, Larson G (2009) Human noroviruses recognize sialyl Lewis X neoglycoprotein. Glycobiology 19:309–320 Rydell GE, Nilsson J, Rodriguez-Diaz J, Ruvoen-Clouet N, Svensson L, Le Pendu J, Larson G (2009) Human noroviruses recognize sialyl Lewis X neoglycoprotein. Glycobiology 19:309–320
155.
go back to reference Taube S, Perry JW, Yetming K, Patel SP, Auble H, Shu L, Nawar HF, Lee CH, Connell TD, Shayman JA et al. (2009) Ganglioside-linked terminal sialic acid moieties on murine macrophages function as attachment receptors for murine noroviruses. J Virol 83:4092–4101 Taube S, Perry JW, Yetming K, Patel SP, Auble H, Shu L, Nawar HF, Lee CH, Connell TD, Shayman JA et al. (2009) Ganglioside-linked terminal sialic acid moieties on murine macrophages function as attachment receptors for murine noroviruses. J Virol 83:4092–4101
156.
go back to reference Stuart AD, Brown TD (2007) Alpha2,6-linked sialic acid acts as a receptor for Feline calicivirus. J Gen Virol 88:177–186 Stuart AD, Brown TD (2007) Alpha2,6-linked sialic acid acts as a receptor for Feline calicivirus. J Gen Virol 88:177–186
157.
go back to reference Tavakkol A, Burness AT (1990) Evidence for a direct role for sialic acid in the attachment of encephalomyocarditis virus to human erythrocytes. Biochemistry 29:10684–10690 Tavakkol A, Burness AT (1990) Evidence for a direct role for sialic acid in the attachment of encephalomyocarditis virus to human erythrocytes. Biochemistry 29:10684–10690
158.
go back to reference Zhou L, Luo Y, Wu Y, Tsao J, Luo M (2000) Sialylation of the host receptor may modulate entry of demyelinating persistent Theiler's virus. J Virol 74:1477–1485 Zhou L, Luo Y, Wu Y, Tsao J, Luo M (2000) Sialylation of the host receptor may modulate entry of demyelinating persistent Theiler's virus. J Virol 74:1477–1485
159.
go back to reference Anderson K, Bond CW (1987) Biological properties of mengovirus: characterization of avirulent, hemagglutination-defective mutants. Arch Virol 93:31–49 Anderson K, Bond CW (1987) Biological properties of mengovirus: characterization of avirulent, hemagglutination-defective mutants. Arch Virol 93:31–49
160.
go back to reference Stoner GD, Williams B, Kniazeff A, Shimkin MB (1973) Effect of neuraminidase pretreatment on the susceptibility of normal and transformed mammalian cells to bovine enterovirus 261. Nature 245:319–320 Stoner GD, Williams B, Kniazeff A, Shimkin MB (1973) Effect of neuraminidase pretreatment on the susceptibility of normal and transformed mammalian cells to bovine enterovirus 261. Nature 245:319–320
161.
go back to reference Nokhbeh MR, Hazra S, Alexander DA, Khan A, McAllister M, Suuronen EJ, Griffith M, Dimock K (2005) Enterovirus 70 binds to different glycoconjugates containing alpha2,3-linked sialic acid on different cell lines. J Virol 79:7087–7094 Nokhbeh MR, Hazra S, Alexander DA, Khan A, McAllister M, Suuronen EJ, Griffith M, Dimock K (2005) Enterovirus 70 binds to different glycoconjugates containing alpha2,3-linked sialic acid on different cell lines. J Virol 79:7087–7094
162.
go back to reference Lipton HL, Kumar AS, Trottier M (2005) Theiler's virus persistence in the central nervous system of mice is associated with continuous viral replication and a difference in outcome of infection of infiltrating macrophages versus oligodendrocytes. Virus Res 111:214–223 Lipton HL, Kumar AS, Trottier M (2005) Theiler's virus persistence in the central nervous system of mice is associated with continuous viral replication and a difference in outcome of infection of infiltrating macrophages versus oligodendrocytes. Virus Res 111:214–223
163.
go back to reference Helander A, Silvey KJ, Mantis NJ, Hutchings AB, Chandran K, Lucas WT, Nibert ML, Neutra MR (2003) The viral sigma1 protein and glycoconjugates containing alpha2-3-linked sialic acid are involved in type 1 reovirus adherence to M cell apical surfaces. J Virol 77:7964–7977 Helander A, Silvey KJ, Mantis NJ, Hutchings AB, Chandran K, Lucas WT, Nibert ML, Neutra MR (2003) The viral sigma1 protein and glycoconjugates containing alpha2-3-linked sialic acid are involved in type 1 reovirus adherence to M cell apical surfaces. J Virol 77:7964–7977
164.
go back to reference Barton ES, Connolly JL, Forrest JC, Chappell JD, Dermody TS (2001) Utilization of sialic acid as a coreceptor enhances reovirus attachment by multistep adhesion strengthening. J Biol Chem 276:2200–2211 Barton ES, Connolly JL, Forrest JC, Chappell JD, Dermody TS (2001) Utilization of sialic acid as a coreceptor enhances reovirus attachment by multistep adhesion strengthening. J Biol Chem 276:2200–2211
165.
go back to reference Prota AE, Campbell JA, Schelling P, Forrest JC, Watson MJ, Peters TR, Aurrand-Lions M, Imhof BA, Dermody TS, Stehle T (2003) Crystal structure of human junctional adhesion molecule 1: implications for reovirus binding. Proc Natl Acad Sci U S A 100:5366–5371 Prota AE, Campbell JA, Schelling P, Forrest JC, Watson MJ, Peters TR, Aurrand-Lions M, Imhof BA, Dermody TS, Stehle T (2003) Crystal structure of human junctional adhesion molecule 1: implications for reovirus binding. Proc Natl Acad Sci U S A 100:5366–5371
166.
go back to reference Connolly JL, Barton ES, Dermody TS (2001) Reovirus binding to cell surface sialic acid potentiates virus-induced apoptosis. J Virol 75:4029–4039 Connolly JL, Barton ES, Dermody TS (2001) Reovirus binding to cell surface sialic acid potentiates virus-induced apoptosis. J Virol 75:4029–4039
167.
go back to reference Dormitzer PR, Sun ZY, Wagner G, Harrison SC (2002) The rhesus rotavirus VP4 sialic acid binding domain has a galectin fold with a novel carbohydrate binding site. EMBO J 21:885–897 Dormitzer PR, Sun ZY, Wagner G, Harrison SC (2002) The rhesus rotavirus VP4 sialic acid binding domain has a galectin fold with a novel carbohydrate binding site. EMBO J 21:885–897
168.
go back to reference Kraschnefski MJ, Bugarcic A, Fleming FE, Yu X, von Itzstein M, Coulson BS, Blanchard H (2009) Effects on sialic acid recognition of amino acid mutations in the carbohydrate-binding cleft of the rotavirus spike protein. Glycobiology 19:194–200 Kraschnefski MJ, Bugarcic A, Fleming FE, Yu X, von Itzstein M, Coulson BS, Blanchard H (2009) Effects on sialic acid recognition of amino acid mutations in the carbohydrate-binding cleft of the rotavirus spike protein. Glycobiology 19:194–200
169.
go back to reference Bastardo JW, Holmes IH (1980) Attachment of SA-11 rotavirus to erythrocyte receptors. Infect Immun 29:1134–1140 Bastardo JW, Holmes IH (1980) Attachment of SA-11 rotavirus to erythrocyte receptors. Infect Immun 29:1134–1140
170.
go back to reference Spence L, Fauvel M, Petro R, Bloch S (1976) Haemagglutinin from rotavirus. Lancet 2:1023 Spence L, Fauvel M, Petro R, Bloch S (1976) Haemagglutinin from rotavirus. Lancet 2:1023
171.
go back to reference Ciarlet M, Estes MK (1999) Human and most animal rotavirus strains do not require the presence of sialic acid on the cell surface for efficient infectivity. J Gen Virol 80:943–948 Ciarlet M, Estes MK (1999) Human and most animal rotavirus strains do not require the presence of sialic acid on the cell surface for efficient infectivity. J Gen Virol 80:943–948
172.
go back to reference Banda K, Kang G, Varki A (2009) ‘Sialidase sensitivity’ of rotaviruses revisited. Nat Chem Biol 5:71–72 Banda K, Kang G, Varki A (2009) ‘Sialidase sensitivity’ of rotaviruses revisited. Nat Chem Biol 5:71–72
173.
go back to reference Haselhorst T, Fleming FE, Dyason JC, Hartnell RD, Yu X, Holloway G, Santegoets K, Kiefel MJ, Blanchard H, Coulson BS et al. (2009) Sialic acid dependence in rotavirus host cell invasion. Nat Chem Biol 5:91–93 Haselhorst T, Fleming FE, Dyason JC, Hartnell RD, Yu X, Holloway G, Santegoets K, Kiefel MJ, Blanchard H, Coulson BS et al. (2009) Sialic acid dependence in rotavirus host cell invasion. Nat Chem Biol 5:91–93
174.
go back to reference Monnier N, Higo-Moriguchi K, Sun ZY, Prasad BV, Taniguchi K, Dormitzer PR (2006) High-resolution molecular and antigen structure of the VP8* core of a sialic acid-independent human rotavirus strain. J Virol 80:1513–1523 Monnier N, Higo-Moriguchi K, Sun ZY, Prasad BV, Taniguchi K, Dormitzer PR (2006) High-resolution molecular and antigen structure of the VP8* core of a sialic acid-independent human rotavirus strain. J Virol 80:1513–1523
175.
go back to reference Lopez S, Arias CF (2006) Early steps in rotavirus cell entry. Curr Top Microbiol Immunol 309:39–66 Lopez S, Arias CF (2006) Early steps in rotavirus cell entry. Curr Top Microbiol Immunol 309:39–66
176.
go back to reference Dormitzer PR, Sun ZY, Blixt O, Paulson JC, Wagner G, Harrison SC (2002) Specificity and affinity of sialic acid binding by the rhesus rotavirus VP8* core. J Virol 76:10512–10517 Dormitzer PR, Sun ZY, Blixt O, Paulson JC, Wagner G, Harrison SC (2002) Specificity and affinity of sialic acid binding by the rhesus rotavirus VP8* core. J Virol 76:10512–10517
177.
go back to reference Kuhlenschmidt MS, Rolsma MD, Kuhlenschmidt TB, Gelberg HB (1997) Characterization of a porcine enterocyte receptor for group A rotavirus. Adv Exp Med Biol 412:135–143 Kuhlenschmidt MS, Rolsma MD, Kuhlenschmidt TB, Gelberg HB (1997) Characterization of a porcine enterocyte receptor for group A rotavirus. Adv Exp Med Biol 412:135–143
178.
go back to reference Delorme C, Brussow H, Sidoti J, Roche N, Karlsson KA, Neeser JR, Teneberg S (2001) Glycosphingolipid binding specificities of rotavirus: identification of a sialic acid-binding epitope. J Virol 75:2276–2287 Delorme C, Brussow H, Sidoti J, Roche N, Karlsson KA, Neeser JR, Teneberg S (2001) Glycosphingolipid binding specificities of rotavirus: identification of a sialic acid-binding epitope. J Virol 75:2276–2287
179.
go back to reference Superti F, Donelli G (1991) Gangliosides as binding sites in SA-11 rotavirus infection of LLC-MK2 cells. J Gen Virol 72:2467–2474 Superti F, Donelli G (1991) Gangliosides as binding sites in SA-11 rotavirus infection of LLC-MK2 cells. J Gen Virol 72:2467–2474
180.
go back to reference Guo CT, Nakagomi O, Mochizuki M, Ishida H, Kiso M, Ohta Y, Suzuki T, Miyamoto D, Hidari KI, Suzuki Y (1999) Ganglioside GM(1a) on the cell surface is involved in the infection by human rotavirus KUN and MO strains. J Biochem 126:683–688 Guo CT, Nakagomi O, Mochizuki M, Ishida H, Kiso M, Ohta Y, Suzuki T, Miyamoto D, Hidari KI, Suzuki Y (1999) Ganglioside GM(1a) on the cell surface is involved in the infection by human rotavirus KUN and MO strains. J Biochem 126:683–688
181.
go back to reference Liddington RC, Yan Y, Moulai J, Sahli R, Benjamin TL, Harrison SC (1991) Structure of simian virus 40 at 3.8-A resolution. Nature 354:278–284 Liddington RC, Yan Y, Moulai J, Sahli R, Benjamin TL, Harrison SC (1991) Structure of simian virus 40 at 3.8-A resolution. Nature 354:278–284
182.
go back to reference Neu U, Woellner K, Gauglitz G, Stehle T (2008) Structural basis of GM1 ganglioside recognition by simian virus 40. Proc Natl Acad Sci U S A 105:5219–5224 Neu U, Woellner K, Gauglitz G, Stehle T (2008) Structural basis of GM1 ganglioside recognition by simian virus 40. Proc Natl Acad Sci U S A 105:5219–5224
183.
go back to reference Stehle T, Harrison SC (1997) High-resolution structure of a polyomavirus VP1-oligosaccharide complex: implications for assembly and receptor binding. EMBO J 16:5139–5148 Stehle T, Harrison SC (1997) High-resolution structure of a polyomavirus VP1-oligosaccharide complex: implications for assembly and receptor binding. EMBO J 16:5139–5148
184.
go back to reference Stehle T, Yan Y, Benjamin TL, Harrison SC (1994) Structure of murine polyomavirus complexed with an oligosaccharide receptor fragment. Nature 369:160–163 Stehle T, Yan Y, Benjamin TL, Harrison SC (1994) Structure of murine polyomavirus complexed with an oligosaccharide receptor fragment. Nature 369:160–163
185.
go back to reference Cahan LD, Paulson JC (1980) Polyoma virus adsorbs to specific sialyloligosaccharide receptors on erythrocytes. Virology 103:505–509 Cahan LD, Paulson JC (1980) Polyoma virus adsorbs to specific sialyloligosaccharide receptors on erythrocytes. Virology 103:505–509
186.
go back to reference Cahan LD, Singh R, Paulson JC (1983) Sialyloligosaccharide receptors of binding variants of polyoma virus. Virology 130:281–289 Cahan LD, Singh R, Paulson JC (1983) Sialyloligosaccharide receptors of binding variants of polyoma virus. Virology 130:281–289
187.
go back to reference Fried H, Cahan LD, Paulson JC (1981) Polyoma virus recognizes specific sialyligosaccharide receptors on host cells. Virology 109:188–192 Fried H, Cahan LD, Paulson JC (1981) Polyoma virus recognizes specific sialyligosaccharide receptors on host cells. Virology 109:188–192
188.
go back to reference Tsai B, Gilbert JM, Stehle T, Lencer W, Benjamin TL, Rapoport TA (2003) Gangliosides are receptors for murine polyoma virus and SV40. EMBO J 22:4346–4355 Tsai B, Gilbert JM, Stehle T, Lencer W, Benjamin TL, Rapoport TA (2003) Gangliosides are receptors for murine polyoma virus and SV40. EMBO J 22:4346–4355
189.
go back to reference Stehle T, Harrison SC (1996) Crystal structures of murine polyomavirus in complex with straight-chain and branched-chain sialyloligosaccharide receptor fragments. Structure 4:183–194 Stehle T, Harrison SC (1996) Crystal structures of murine polyomavirus in complex with straight-chain and branched-chain sialyloligosaccharide receptor fragments. Structure 4:183–194
190.
go back to reference Caruso M, Belloni L, Sthandier O, Amati P, Garcia MI (2003) Alpha4beta1 integrin acts as a cell receptor for murine polyomavirus at the postattachment level. J Virol 77:3913–3921 Caruso M, Belloni L, Sthandier O, Amati P, Garcia MI (2003) Alpha4beta1 integrin acts as a cell receptor for murine polyomavirus at the postattachment level. J Virol 77:3913–3921
191.
go back to reference Ewers H, Romer W, Smith AE, Bacia K, Dmitrieff S, Chai W, Mancini R, Kartenbeck J, Chambon V, Berland L et al. (2010). GM1 structure determines SV40-induced membrane invagination and infection. Nat Cell Biol 12,11–18; sup pp 11–12. Ewers H, Romer W, Smith AE, Bacia K, Dmitrieff S, Chai W, Mancini R, Kartenbeck J, Chambon V, Berland L et al. (2010). GM1 structure determines SV40-induced membrane invagination and infection. Nat Cell Biol 12,11–18; sup pp 11–12.
192.
go back to reference Qian M, Cai D, Verhey KJ, Tsai B (2009) A lipid receptor sorts polyomavirus from the endolysosome to the endoplasmic reticulum to cause infection. PLoS Pathog 5:e1000465 Qian M, Cai D, Verhey KJ, Tsai B (2009) A lipid receptor sorts polyomavirus from the endolysosome to the endoplasmic reticulum to cause infection. PLoS Pathog 5:e1000465
193.
go back to reference Keppler OT, Herrmann M, Oppenlander M, Meschede W, Pawlita M (1994) Regulation of susceptibility and cell surface receptor for the B-lymphotropic papovavirus by N glycosylation. J Virol 68:6933–6939 Keppler OT, Herrmann M, Oppenlander M, Meschede W, Pawlita M (1994) Regulation of susceptibility and cell surface receptor for the B-lymphotropic papovavirus by N glycosylation. J Virol 68:6933–6939
194.
go back to reference Dugan AS, Gasparovic ML, Atwood WJ (2008) Direct correlation between sialic acid binding and infection of cells by two human polyomaviruses (JC virus and BK virus). J Virol 82:2560–2564 Dugan AS, Gasparovic ML, Atwood WJ (2008) Direct correlation between sialic acid binding and infection of cells by two human polyomaviruses (JC virus and BK virus). J Virol 82:2560–2564
195.
go back to reference Liu CK, Wei G, Atwood WJ (1998) Infection of glial cells by the human polyomavirus JC is mediated by an N-linked glycoprotein containing terminal alpha(2-6)-linked sialic acids. J Virol 72:4643–4649 Liu CK, Wei G, Atwood WJ (1998) Infection of glial cells by the human polyomavirus JC is mediated by an N-linked glycoprotein containing terminal alpha(2-6)-linked sialic acids. J Virol 72:4643–4649
196.
go back to reference Komagome R, Sawa H, Suzuki T, Suzuki Y, Tanaka S, Atwood WJ, Nagashima K (2002) Oligosaccharides as receptors for JC virus. J Virol 76:12992–13000 Komagome R, Sawa H, Suzuki T, Suzuki Y, Tanaka S, Atwood WJ, Nagashima K (2002) Oligosaccharides as receptors for JC virus. J Virol 76:12992–13000
197.
go back to reference Elphick GF, Querbes W, Jordan JA, Gee GV, Eash S, Manley K, Dugan A, Stanifer M, Bhatnagar A, Kroeze WK et al. (2004) The human polyomavirus, JCV, uses serotonin receptors to infect cells. Science 306:1380–1383 Elphick GF, Querbes W, Jordan JA, Gee GV, Eash S, Manley K, Dugan A, Stanifer M, Bhatnagar A, Kroeze WK et al. (2004) The human polyomavirus, JCV, uses serotonin receptors to infect cells. Science 306:1380–1383
198.
go back to reference Dugan AS, Eash S, Atwood WJ (2005) An N-linked glycoprotein with alpha(2,3)-linked sialic acid is a receptor for BK virus. J Virol 79:14442–14445 Dugan AS, Eash S, Atwood WJ (2005) An N-linked glycoprotein with alpha(2,3)-linked sialic acid is a receptor for BK virus. J Virol 79:14442–14445
199.
go back to reference Low JA, Magnuson B, Tsai B, Imperiale MJ (2006) Identification of gangliosides GD1b and GT1b as receptors for BK virus. J Virol 80:1361–1366 Low JA, Magnuson B, Tsai B, Imperiale MJ (2006) Identification of gangliosides GD1b and GT1b as receptors for BK virus. J Virol 80:1361–1366
200.
go back to reference Erickson KD, Garcea RL, Tsai B (2009) Ganglioside GT1b is a putative host cell receptor for the Merkel cell polyomavirus. J Virol 83:10275–10279 Erickson KD, Garcea RL, Tsai B (2009) Ganglioside GT1b is a putative host cell receptor for the Merkel cell polyomavirus. J Virol 83:10275–10279
201.
go back to reference Arnberg N, Kidd AH, Edlund K, Nilsson J, Pring-Akerblom P, Wadell G (2002) Adenovirus type 37 binds to cell surface sialic acid through a charge-dependent interaction. Virology 302:33–43 Arnberg N, Kidd AH, Edlund K, Nilsson J, Pring-Akerblom P, Wadell G (2002) Adenovirus type 37 binds to cell surface sialic acid through a charge-dependent interaction. Virology 302:33–43
202.
go back to reference Burmeister WP, Guilligay D, Cusack S, Wadell G, Arnberg N (2004) Crystal structure of species D adenovirus fiber knobs and their sialic acid binding sites. J Virol 78:7727–7736 Burmeister WP, Guilligay D, Cusack S, Wadell G, Arnberg N (2004) Crystal structure of species D adenovirus fiber knobs and their sialic acid binding sites. J Virol 78:7727–7736
203.
go back to reference Schmidt M, Chiorini JA (2006) Gangliosides are essential for bovine adeno-associated virus entry. J Virol 80:5516–5522 Schmidt M, Chiorini JA (2006) Gangliosides are essential for bovine adeno-associated virus entry. J Virol 80:5516–5522
204.
go back to reference Kaludov N, Brown KE, Walters RW, Zabner J, Chiorini JA (2001) Adeno-associated virus serotype 4 (AAV4) and AAV5 both require sialic acid binding for hemagglutination and efficient transduction but differ in sialic acid linkage specificity. J Virol 75:6884–6893 Kaludov N, Brown KE, Walters RW, Zabner J, Chiorini JA (2001) Adeno-associated virus serotype 4 (AAV4) and AAV5 both require sialic acid binding for hemagglutination and efficient transduction but differ in sialic acid linkage specificity. J Virol 75:6884–6893
205.
go back to reference Dickey DD, Excoffon KJ, Koerber JT, Bergen J, Steines B, Klesney-Tait J, Schaffer DV, Zabner J (2011) Enhanced sialic acid-dependent endocytosis explains the increased efficiency of infection of airway epithelia by a novel adeno-associated virus. J Virol 85:9023–9030 Dickey DD, Excoffon KJ, Koerber JT, Bergen J, Steines B, Klesney-Tait J, Schaffer DV, Zabner J (2011) Enhanced sialic acid-dependent endocytosis explains the increased efficiency of infection of airway epithelia by a novel adeno-associated virus. J Virol 85:9023–9030
Metadata
Title
Sialic Acid Receptors of Viruses
Authors
Mikhail Matrosovich
Georg Herrler
Hans Dieter Klenk
Copyright Year
2015
DOI
https://doi.org/10.1007/128_2013_466