nach oben

Erschienen in:

2012 | OriginalPaper | Buchkapitel

5. Protein Engineering of Bacillus thuringiensis δ-Endotoxins

verfasst von : Dr. Alvaro M. Florez, Dr. Cristina Osorio, Dr. Oscar Alzate

Erschienen in: Bacillus thuringiensis Biotechnology

Verlag: Springer Netherlands

Einloggen

Aktivieren Sie unsere intelligente Suche, um passende Fachinhalte oder Patente zu finden.

search-config

KI-gestützte Suche

Aus

Abstract

Protein engineering of insecticidal Bt δ-endotoxins is a powerful tool for designing novel Cry toxins with altered properties, including changing the toxin’s specificity. By following some elementary rules governing the structure/function relationship, it has been possible to create new toxins with modified properties including increased toxicity and binding affinity, enhanced ion-transport activity, and changes in insect specificity. These methods have also produced valuable information and have led to an improved understanding of the mode of action of these important biopesticides. The results discussed in this chapter derive from rational molecular design where protein structure is modified by incorporating single or multiple amino acid substitutions aimed at modifying specific protein functions. In this review, we analyze several protein modifications that have been successfully used for creating stable, functional proteins with minimal structural alterations. The understanding and proper use of protein engineering approaches may help in implementing appropriate pest management strategies by improving the efficacy of these toxins against insect pests.

Sie haben noch keine Lizenz? Dann Informieren Sie sich jetzt über unsere Produkte:

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!

Jetzt informieren

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!

Jetzt informieren

Springer Professional "Wirtschaft"

Online-Abonnement

Mit Springer Professional "Wirtschaft" erhalten Sie Zugriff auf:

über 67.000 Bücher
über 340 Zeitschriften

aus folgenden Fachgebieten:

Bauwesen + Immobilien
Business IT + Informatik
Finance + Banking
Management + Führung
Marketing + Vertrieb
Versicherung + Risiko

Jetzt Wissensvorsprung sichern!

Jetzt informieren

Vorheriges Kapitel Use and Efficacy of Bt Compared to Less Environmentally Safe Alternatives

Nächstes Kapitel Evolution of the Bacillus cereus Group

Abdullah MA, Alzate O, Mohammad M, McNall RJ, Adang MJ, Dean DH (2003) Introduction of Culex toxicity into Bacillus thuringiensis Cry4Ba by protein engineering. Appl Environ Microbiol 69(9):5343–5353CrossRef

Ahmad W, Ellar DJ (1990) Directed mutagenesis of selected regions of a Bacillus thuringiensis entomocidal protein. FEMS Microbiol Lett 56(1–2):97–104CrossRef

Alcantara EP, Alzate O, Lee MK, Curtiss A, Dean DH (2001) Role of a-helix 7 of Bacillus thuringiensis Cry1Ab δ-endotoxin in membrane insertion, structural stability, and ion channel activity. Biochemistry 40(8):2540–2547CrossRef

Altenbach C, Marti T, Khorana HG, Hubbell WL (1990) Transmembrane protein structure: spin labeling of bacteriorhodopsin mutants. Science 248(4959):1088–1092CrossRef

Altenbach C, Greenhalgh DA, Khorana HG, Hubbell WL (1994) A collision gradient method to determine the immersion depth of nitroxides in lipid bilayers: application to spin-labeled mutants of bacteriorhodopsin. Proc Natl Acad Sci U S A 91(5):1667–1671CrossRef

Alzate O, You T, Claybon M, Osorio C, Curtiss A, Dean DH (2006) Effects of disulfide bridges in domain I of Bacillus thuringiensis Cry1Aa δ-endotoxin on ion-channel formation in biological membranes. Biochemistry 45(45):13597–13605CrossRef

Alzate O, Hemann CF, Osorio C, Hille R, Dean DH (2009) Ser170 of Bacillus thuringiensis Cry1Ab δ-endotoxin becomes anchored in a hydrophobic moiety upon insertion of this protein into Manduca sexta brush border membranes. BMC Biochem 10:25CrossRef

Alzate O, Osorio C, Florez AM, Dean DH (2010) Participation of valine 171 in α-Helix 5 of Bacillus thuringiensis Cry1Ab δ-endotoxin in translocation of toxin into Lymantria dispar midgut membranes. Appl Environ Microbiol 76(23):7878–7880CrossRef

Arenas I, Bravo A, Soberon M, Gomez I (2010) Role of alkaline phosphatase from Manduca sexta in the mechanism of action of Bacillus thuringiensis Cry1Ab toxin. J Biol Chem 285(17):12497–12503CrossRef

Arnold S, Curtiss A, Dean DH, Alzate O (2001) The role of a proline-induced broken-helix motif in α-helix 2 of Bacillus thuringiensis δ-endotoxins. FEBS Lett 490(1–2):70–74CrossRef

Aronson A (1995) The protoxin composition of Bacillus thuringiensis insecticidal inclusions affects solubility and toxicity. Appl Environ Microbiol 61(11):4057–4060

Aronson A (2000) Incorporation of protease K into larval insect membrane vesicles does not result in disruption of integrity or function of the pore-forming Bacillus thuringiensis Bacillus thuringiensisδ-endotoxin. Appl Environ Microbiol 66(10):4568–4570CrossRef

Atherton NM (1993) Principles of electron spin resonance. Ellis Horwood, Prentice Hall, London

Audtho M, Valaitis AP, Alzate O, Dean DH (1999) Production of chymotrypsin-resistant Bacillus thuringiensis Cry2Aa1 δ-endotoxin by protein engineering. Appl Environ Microbiol 65(10):4601–4605

Berova N, Nakanishi K, Woody R (2000) Circular dichroism: principles and applications, 2nd edn. Wiley-VCH, New York

Bietlot HP, Vishnubhatla I, Carey PR, Pozsgay M, Kaplan H (1990) Characterization of the cysteine residues and disulfide linkages in the protein crystal of Bacillus thuringiensis. Biochem J 267:309–315

Boonserm P, Davis P, Ellar DJ, Li J (2005) Crystal structure of the mosquito-larvicidal toxin Cry4Ba and its biological implications. J Mol Biol 348(2):363–382CrossRef

Boonserm P, Mo M, Angsuthanasombat C, Lescar J (2006) Structure of the functional form of the mosquito larvicidal Cry4Aa toxin from Bacillus thuringiensis at a 2.8-angstrom resolution. J Bacteriol 188(9):3391–3401CrossRef

Bravo A, Gomez I, Conde J, Munoz-Garay C, Sanchez J, Miranda R, Zhuang M, Gill SS, Soberon M (2004) Oligomerization triggers binding of a Bacillus thuringiensis Cry1Ab pore-forming toxin to aminopeptidase N receptor leading to insertion into membrane microdomains. Biochim Biophys Acta 1667(1):38–46CrossRef

Burton SL, Ellar DJ, Li J, Derbyshire DJ (1999) N-acetylgalactosamine on the putative insect receptor aminopeptidase N is recognized by a site on the domain III lectin-like fold of a Bacillus thuringiensis insecticidal toxin. J Mol Biol 287:1011–1022CrossRef

Carroll J, Wolfersberger MG, Ellar DJ (1997) The Bacillus thuringiensis Cry1Ac toxin-induced permeability change in Manduca sexta midgut brush border membrane vesicles proceeds by more than one mechanism. J Cell Sci 110:3099–3104

Chandra A, Ghosh P, Mandaokar AD, Bera AK, Sharma RP, Das S, Kumar PA (1999) Amino acid substitution in α-helix 7 of Cry1Ac δ-endotoxin of Bacillus thuringiensis leads to enhanced toxicity to HelicoverpaarmigeraHubner. FEBS Lett 458(2):175–179CrossRef

Chen XJ, Curtiss A, Alcantara E, Dean DH (1995) Mutations in domain I of Bacillus thuringiensisδ-endotoxin CryIAbreduce the irreversible binding of toxin to Manduca sexta brush border membrane vesicles. J Biol Chem 270(11):6412–6419CrossRef

Choma CT, Surewicz WK, Carey PR, Pozsgay M, Raynor T, Kaplan H (1990) Unusual proteolysis of the protoxin and toxin from Bacillus thuringiensis: structural implications. Eur J Biochem 189:523–527CrossRef

Coux F, Vachon V, Rang C, Moozar K, Masson L, Royer M, Bes M, Rivest S, Brousseau R, Schwartz JL, Laprade R, Frutos R (2001) Role of interdomain salt bridges in the pore-forming ability of the Bacillus thuringiensis toxins Cry1Aa and Cry1Ac. J Biol Chem 276(38):35546–35551CrossRef

Crickmore N, Zeigler DR, Feitelson J, Schnepf E, Van Rie J, Lereclus D, Baum J, Dean DH (1998) Revision of the nomenclature for the Bacillus thuringiensis pesticidal crystal proteins. Microbiol Mol Biol Rev 62(3):807–813

Crickmore N, Zeigler DR, Schnepf E, Van Rie J, Lereclus D, Baum J, Bravo A, Dean DH (2011) Bacillus thuringiensis toxin nomenclature. http://www.lifesci.sussex.ac.uk/Home/Neil_Crickmore/Bt/

de Maagd RA, Kwa MS, van der Klei H, Yamamoto T, Schipper B, Vlak JM, Stiekema WJ, Bosch D (1996) Domain III substitution in Bacillus thuringiensis δ-endotoxin CryIA(b) results in superior toxicity for Spodopteraexigua and altered membrane protein recognition. Appl Environ Microbiol 62(5):1537–1543

de Maagd RA, Weemen-Hendriks M, Stiekema W, Bosch D (2000) Bacillus thuringiensis δ-endotoxin Cry1C domain III can function as a specificity determinant for Spodopteraexigua in different, but not all, Cry1-Cry1C hybrids. Appl Environ Microbiol 66(4):1559–1563CrossRef

Fortier M, Vachon V, Frutos R, Schwartz JL, Laprade R (2007) Effect of insect larval midgut proteases on the activity of Bacillus thuringiensis Cry toxins. Appl Environ Microbiol 73(19):6208–6213CrossRef

Gatehouse JA (2011) Prospects for using proteinase inhibitors to protect transgenic plants against attack by herbivorous insects. Curr Protein Pept Sci. (Epub ahead of print)

Gazit E, Shai Y (1993) Structural and functional characterization of the alpha 5 segment of Bacillus thuringiensis δ-endotoxin. Biochemistry 32(13):3429–3436CrossRef

Gazit E, La Rocca P, Sansom MS, Shai Y (1998) The structure and organization within the membrane of the helices composing the pore-forming domain of Bacillus thuringiensis δ-endotoxin are consistent with an “umbrella-like” structure of the pore. Proc Natl Acad Sci U S A 95(21):12289–12294CrossRef

Ge AZ, Shivarova NI, Dean DH (1989) Location of the Bombyxmori specificity domain on a Bacillus thuringiensis δ-endotoxin protein. Proc Natl Acad Sci U S A 86(11):4037–4041CrossRef

Ge AZ, Rivers D, Milne R, Dean DH (1991) Functional domains of Bacillus thuringiensis insecticidal crystal proteins: refinement of Heliothisvirescens and Trichoplusianispecificity domains on CryIA(c). J Biol Chem 266:17954–17958

Girard F, Vachon V, Prefontaine G, Marceau L, Su Y, Larouche G, Vincent C, Schwartz JL, Masson L, Laprade R (2008) Cysteine scanning mutagenesis of alpha4, a putative pore-lining helix of the Bacillus thuringiensis insecticidal toxin Cry1Aa. Appl Environ Microbiol 74(9):2565–2572CrossRef

Gomez I, Sanchez J, Miranda R, Bravo A, Soberon M (2002) Cadherin-like receptor binding facilitates proteolytic cleavage of helix alpha-1 in domain I and oligomer pre-pore formation of Bacillus thuringiensis Cry1Ab toxin. FEBS Lett 513(2–3):242–246CrossRef

Gomez I, Dean DH, Bravo A, Soberon M (2003) Molecular basis for Bacillus thuringiensis Cry1Ab toxin specificity: two structural determinants in the Manduca sexta Bt-R1 receptor interact with loops alpha-8 and 2 in domain II of Cy1Ab toxin. Biochemistry 42(35):10482–10489CrossRef

Greenfield NJ (2006) Using circular dichroism spectra to estimate protein secondary structure. Nat Protoc 1(6):2876–2890CrossRef

Grochulski P, Masson L, Borisova S, Pusztai-Carey M, Schwartz JL, Brousseau R, Cygler M (1995) Bacillus thuringiensis CryIA(a) insecticidal toxin: crystal structure and channel formation. J Mol Biol 254(3):447–464CrossRef

Höfte H, Whiteley HR (1989) Insecticidal crystal proteins of Bacillus thuringiensis. Microbiol Rev 53:242–255

Hubbell WL, Cafiso DS, Altenbach C (2000) Identifying conformational changes with site-directed spin labeling. Nat Struct Biol 7(9):735–739CrossRef

Hubbell WL, Altenbach C, Hubbell CM, Khorana HG (2003) Rhodopsin structure, dynamics, and activation: a perspective from crystallography, site-directed spin labeling, sulfhydryl reactivity, and disulfide cross-linking. Adv Protein Chem 63:243–290CrossRef

Hussain SR, Aronson AI, Dean DH (1996) Substitution of residues on the proximal side of Cry1A Bacillus thuringiensis δ-endotoxins affects irreversible binding to Manduca sexta midgut membrane. Biochem Biophys Res Commun 226(1):8–14CrossRef

Hussain SA, Flórez AM, Dean DH, Alzate O (2010) Preferential protection of domains II and III of Bacillus thuringiensis Cry1Aa toxin by brush border membrane vesicles. Rev Colomb Biotechnol 12(2):14–26

Jimenez-Juarez N, Munoz-Garay C, Gomez I, Saab-Rincon G, Damian-Almazo JY, Gill SS, Soberon M, Bravo A (2007) Bacillus thuringiensis Cry1Ab mutants affecting oligomer formation are non-toxic to Manduca sexta larvae. J Biol Chem 282(29):21222–21229CrossRef

Jimenez-Juarez N, Munoz-Garay C, Gomez I, Gill SS, Soberon M, Bravo A (2008) The pre-pore from Bacillus thuringiensis Cry1Ab toxin is necessary to induce insect death in Manduca sexta. Peptides 29(2):318–323CrossRef

Kaur S (2000) Molecular approaches towards development of novel Bacillus thuringiensis biopesticides. World J Microbiol Biotechnol 16:781–793CrossRef

Kirouac M, Vachon V, Quievy D, Schwartz JL, Laprade R (2006) Protease inhibitors fail to prevent pore formation by the activated Bacillus thuringiensis toxin Cry1Aa in insect brush border membrane vesicles. Appl Environ Microbiol 72(1):506–515CrossRef

Kumar AS, Aronson AI (1999) Analysis of mutations in the pore-forming region essential for insecticidal activity of a Bacillus thuringiensis δ-endotoxin. J Bacteriol 181(19):6103–6107

Lebel G, Vachon V, Prefontaine G, Girard F, Masson L, Juteau M, Bah A, Larouche G, Vincent C, Laprade R, Schwartz JL (2009) Mutations in domain I interhelical loops affect the rate of pore formation by the Bacillus thuringiensis Cry1Aa toxin in insect midgut brush border membrane vesicles. Appl Environ Microbiol 75(12):3842–3850CrossRef

Lee MK, Young BA, Dean DH (1995) Domain III exchanges of Bacillus thuringiensis CryIA toxins affect binding to different gypsy moth midgut receptors. Biochem Biophys Res Commun 216:306–312CrossRef

Li J, Carroll J, Ellar DJ (1991) Crystal structure of insecticidal d-endotoxin from Bacillus thuringiensis at 2.5 Å resolution. Nature 353:815–821CrossRef

Li J, Derbyshire DJ, Promdonkoy B, Ellar DJ (2001) Structural implications for the transformation of the Bacillus thuringiensis δ-endotoxins from water-soluble to membrane-inserted forms. Biochem Soc Trans 29(Pt 4):571–577CrossRef

Lightwood DJ, Ellar DJ, Jarrett P (2000) Role of proteolysis in determining potency of Bacillus thuringiensis Cry1Ac δ-endotoxin. Appl Environ Microbiol 66(12):5174–5181CrossRef

Likitvivatanavong S, Chen J, Evans AM, Bravo A, Soberon M, Gill SS (2011) Multiple receptors as targets of cry toxins in mosquitoes. J Agric Food Chem 59(7):2829–2838CrossRef

Liu XS, Dean DH (2006) Redesigning Bacillus thuringiensis Cry1Aa toxin into a mosquito toxin. Protein Eng Des Sel 19(3):107–111CrossRef

Lorence A, Darszon A, Diaz C, Lievano A, Quintero R, Bravo A (1995) Delta-endotoxins induce cation channels in Spodopterafrugiperda brush border membranes in suspension and in planar lipid bilayers. FEBS Lett 360(3):217–222CrossRef

Masson L, Tabashnik BE, Liu YB, Brousseau R, Schwartz JL (1999) Helix 4 of the Bacillus thuringiensis Cry1Aa toxin lines the lumen of the ion channel. J Biol Chem 274(45):31996–32000CrossRef

Munoz-Garay C, Sanchez J, Darszon A, de Maagd RA, Bakker P, Soberon M, Bravo A (2006) Permeability changes of Manduca sexta midgut brush border membranes induced by oligomeric structures of different Cry toxins. J Membr Biol 212(1):61–68CrossRef

Munoz-Garay C, Rodriguez-Almazan C, Aguilar JN, Portugal L, Gomez I, Saab-Rincon G, Soberon M, Bravo A (2009) Oligomerization of Cry11Aa from Bacillus thuringiensis has an important role in toxicity against Aedesaegypti. Appl Environ Microbiol 75(23):7548–7550CrossRef

Nair MS, Dean DH (2008) All domains of Cry1A toxins insert into insect brush border membranes. J Biol Chem 283(39):26324–26331CrossRef

Pacheco S, Gomez I, Arenas I, Saab-Rincon G, Rodriguez-Almazan C, Gill SS, Bravo A, Soberon M (2009) Domain II loop 3 of Bacillus thuringiensis Cry1Ab toxin is involved in a “ping pong” binding mechanism with Manduca sextaaminopeptidase-N and cadherin receptors. J Biol Chem 284(47):32750–32757CrossRef

Pardo-Lopez L, Gomez I, Rausell C, Sanchez J, Soberon M, Bravo A (2006) Structural changes of the Cry1Ac oligomeric pre-pore from Bacillus thuringiensis induced by N-Acetylgalactosamine facilitates toxin membrane insertion. Biochemistry 45(34):10329–10336CrossRef

Pigott CR, Ellar DJ (2007) Role of receptors in Bacillus thuringiensis crystal toxin activity. Microbiol Mol Biol Rev 71(2):255–281CrossRef

Pozsgay M, Fast P, Kaplan H, Carey PR (1987) The effect of sunlight on the protein crystals from Bacillus thuringiensis subsp. kurstaki HD1 and NRD12, a Raman spectroscopy study. J Invertebr Pathol 50:246–253CrossRef

Pusztai M, Fast P, Gringorten L, Kaplan H, Lessard T, Carey PR (1991) The mechanism of sunlight-mediated inactivation of Bacillus thuringiensis crystals. Biochem J 273(Pt 1):43–47

Rajamohan F, Dean DH (1996) Molecular biology of bacteria on biological control of insects. In: Gunasekaran M, Weber DJ (eds) Molecular biology of the biological control of pests and diseases of plants. CRC Press, Boca Raton, pp 105–122

Rajamohan F, Alcantara E, Lee MK, Chen XJ, Curtiss A, Dean DH (1995) Single amino acid changes in domain II of Bacillus thuringiensis CryIAb δ-endotoxin affect irreversible binding to Manduca sexta midgut membrane vesicles. J Bacteriol 177(9):2276–2282

Rajamohan F, Alzate O, Cotrill JA, Curtiss A, Dean DH (1996a) Protein engineering of Bacillus thuringiensis δ-endotoxin: mutations at domain II of CryIAb enhance receptor affinity and toxicity toward gypsy moth larvae. Proc Natl Acad Sci U S A 93(25):14338–14343CrossRef

Rajamohan F, Cotrill JA, Gould F, Dean DH (1996b) Role of domain II, loop 2 residues of Bacillus thuringiensis CryIAb δ-endotoxin in reversible and irreversible binding to Manduca sexta and Heliothisvirescens. J Biol Chem 271(5):2390–2396CrossRef

Rausell C, Munoz-Garay C, Miranda-CassoLuengo R, Gomez I, Rudino-Pinera E, Soberon M, Bravo A (2004a) Tryptophan spectroscopy studies and black lipid bilayer analysis indicate that the oligomeric structure of Cry1Ab toxin from Bacillus thuringiensis is the membrane-insertion intermediate. Biochemistry 43(1):166–174CrossRef

Rausell C, Pardo-Lopez L, Sanchez J, Munoz-Garay C, Morera C, Soberon M, Bravo A (2004b) Unfolding events in the water-soluble monomeric Cry1Ab toxin during transition to oligomeric pre-pore and membrane-inserted pore channel. J Biol Chem 279(53):55168–55175CrossRef

Rodriguez-Almazan C, Zavala LE, Munoz-Garay C, Jimenez-Juarez N, Pacheco S, Masson L, Soberon M, Bravo A (2009) Dominant negative mutants of Bacillus thuringiensis Cry1Ab toxin function as anti-toxins: demonstration of the role of oligomerization in toxicity. PLoS One 4(5):e5545CrossRef

Sanahuja G, Banakar R, Twyman RM, Capell T, Christou P (2011) Bacillus thuringiensis: a century of research, development and commercial applications. Plant Biotechnol J 9(3):283–300CrossRef

Schnepf HE (1995) Bacillus thuringiensis toxins: regulation, activities and structural diversity. Curr Opin Biotechnol 6:305–312CrossRef

Schnepf E, Crickmore N, Van Rie J, Lereclus D, Baum J, Feitelson J, Zeigler DR, Dean DH (1998) Bacillus thuringiensis and its pesticidal crystal proteins. Microbiol Mol Biol Rev 62(3):775–806

Schwartz JL, Juteau M, Grochulski P, Cygler M, Prefontaine G, Brousseau R, Masson L (1997a) Restriction of intramolecular movements within the Cry1Aa toxin molecule of Bacillus thuringiensis through disulfide bond engineering. FEBS Lett 410(2–3):397–402CrossRef

Schwartz JL, Lu YJ, Sohnlein P, Brousseau R, Laprade R, Masson L, Adang MJ (1997b) Ion channels formed in planar lipid bilayers by Bacillus thuringiensis toxins in the presence of Manduca sexta midgut receptors. FEBS Lett 412:270–276CrossRef

Schwartz JL, Potvin L, Chen XJ, Brousseau R, Laprade R, Dean DH (1997c) Single-site mutations in the conserved alternating-arginine region affect ionic channels formed by CryIAa, a Bacillus thuringiensis toxin. Appl Environ Microbiol 63(10):3978–3984

Shan S, Zhang Y, Ding X, Hu S, Sun Y, Yu Z, Liu S, Zhu Z, Xia L (2010) A Cry1Ac toxin variant generated by directed evolution has enhanced toxicity against Lepidopteran insects. Curr Microbiol 62(2):358–365CrossRef

Soberon M, Pardo-Lopez L, Lopez I, Gomez I, Tabashnik BE, Bravo A (2007) Engineering modified Bt toxins to counter insect resistance. Science 318(5856):1640–1642CrossRef

Tigue NJ, Jacoby J, Ellar DJ (2001) The α-helix 4 residue, Asn135, is involved in the oligomerization of Cry1Ac1 and Cry1Ab5 Bacillus thuringiensis toxins. Appl Environ Microbiol 67(12):5715–5720CrossRef

Vachon V, Prefontaine G, Rang C, Coux F, Juteau M, Schwartz JL, Brousseau R, Frutos R, Laprade R, Masson L (2004) Helix 4 mutants of the Bacillus thuringiensis insecticidal toxin Cry1Aa display altered pore-forming abilities. Appl Environ Microbiol 70(10):6123–6130CrossRef

van Frankenhuyzen K (2009) Insecticidal activity of Bacillus thuringiensis crystal proteins. J Invertebr Pathol 101(1):1–16CrossRef

Wolfersberger MG (1990) The toxicity of two Bacillus thuringiensis δ-endotoxins to gypsy moth larvae is inversely related to the affinity of binding sites on midgut brush border membranes for the toxins. Experientia 46(5):475–477CrossRef

Wolfersberger MG, Spaeth DD (1987) Activity of spore-crystal preparations from twenty serotypes of Bacillus thuringiensis toward Manduca sexta larvae in vivo and in vitro. Z Angew Entomol 103:138–141

Wolfersberger M, Lüthy P, Maurer A, Parenti P, Sacchi FV, Giordana B, Hanozet GM (1987) Preparation and partial characterization of amino acid transporting brush border membrane vesicles from the larval midgut of the cabbage butterfly (Pierisbrassicae). Comp Biochem Physiol 86A:301–308CrossRef

Wu D, Aronson AI (1992) Localized mutagenesis defines regions of the Bacillus thuringiensis δ-endotoxin involved in toxicity and specificity. J Biol Chem 267(4):2311–2317

Zavala LE, Pardo-Lopez L, Canton PE, Gomez I, Soberon M, Bravo A (2011) Domains II and III of Bacillus thuringiensis Cry1Ab toxin remain exposed to the solvent after insertion of part of domain I into the membrane. J Biol Chem 286:19109–19117CrossRef

Zhang X, Candas M, Griko NB, Taussig R, Bulla LA Jr (2006) A mechanism of cell death involving an adenylyl cyclase/PKA signaling pathway is induced by the Cry1Ab toxin of Bacillus thuringiensis. Proc Natl Acad Sci U S A 103(26):9897–9902CrossRef

Zhuang M, Oltean DI, Gomez I, Pullikuth AK, Soberon M, Bravo A, Gill SS (2002) Heliothisvirescens and Manduca sexta lipid rafts are involved in Cry1A toxin binding to the midgut epithelium and subsequent pore formation. J Biol Chem 277(16):13863–13872CrossRef

Titel: Protein Engineering of Bacillus thuringiensis δ-Endotoxins
verfasst von: Dr. Alvaro M. Florez
Dr. Cristina Osorio
Dr. Oscar Alzate
Verlag: Springer Netherlands
Buch: Bacillus thuringiensis Biotechnology
Print ISBN: 978-94-007-3020-5

Electronic ISBN: 978-94-007-3021-2

Copyright-Jahr: 2012
DOI: https://doi.org/10.1007/978-94-007-3021-2_5

Premium Partner

Marktübersichten

Die im Laufe eines Jahres in der „adhäsion“ veröffentlichten Marktübersichten helfen Anwendern verschiedenster Branchen, sich einen gezielten Überblick über Lieferantenangebote zu verschaffen.

Zur Marktübersicht

Springer Professional

Abstract

Bitte loggen Sie sich ein, um Zugang zu Ihrer Lizenz zu erhalten.

Sie haben noch keine Lizenz? Dann Informieren Sie sich jetzt über unsere Produkte:

Springer Professional "Wirtschaft+Technik"

Springer Professional "Technik"

Springer Professional "Wirtschaft"

Premium Partner

Marktübersichten