The peculiar collagens of mussel byssus

doi:10.1016/S0945-053X(98)90023-3

Matrix Biology

Volume 17, Issue 2, June 1998, Pages 93-106

https://doi.org/10.1016/S0945-053X(98)90023-3 Get rights and content

Abstract

The byssal collagens of marine mussels are extracorporeal collagens that function in byssal threads under tension. Each byssal thread resembles a shock absorber in its mechanical design: it is strong and stiff at one end and pliably elastic at the other. Primary structures of three of these collagens (preCols), deduced from cDNAs, reveal signal peptide sequences, but no N-glycosylation sites or propeptides typical of procollagens. The collagen domain (40–50 kDa) represents roughly half the mass of the mature molecules and is distinguished by its central location, abundant Gly-Gly-X repeats, and “flaws” (usually Gly deletions). Flanking the collagen domains on both sides are structural domains that resemble elastin in preCol-P, spider drag-line silk in preCol-D, and Gly-rich cell wall proteins in preCol-NG. Not surprisingly, studies of preCol distribution in byssal threads suggest preCol P enhancement in the elastic proximal portion, while preCol-D predominates in the stiffer distal portion. PreCol-NG, in contrast, is evenly distributed. Although no data are yet available on the fibrillogenesis and cross-linking of the preCols, the quarter-stagger assembly of fibrillar interstitial collagens does not pertain since preCols lack the terminal peptides of tropocollagen. Metal-binding by histidines may mediate the initial inter- and intramolecular stabilization of preCols in the byssus.

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Citation Excerpt :
Our results suggest that the attachment strength of triploid mussels to be stronger than that of diploids because the triploids produced more byssal threads than diploid mussels. Byssal threads can be compared to human tendons because they are stiff and able to sustain substantial tension, but byssal threads are six times stronger than tendons (Bell and Gosline, 1996; Waite et al., 1998; Troncoso et al., 2008) and have the capacity to self-repair (Allen et al., 1976; Vaccaro and Waite, 2001; Carrington and Gosline, 2004; Harrington and Waite, 2007; Harrington et al., 2009; Reinecke et al., 2016; Bouhlel et al., 2017). The byssus allows mussels to hold onto their substrate even under water and in dynamic conditions.
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MinireviewThe peculiar collagens of mussel byssus

Abstract

J. Biol. Chem.

Curr. Biol.

Aquat. Toxicol.

J. Biol. Chem.

Endeavour

Biophys. J.

Arch. Biochem. Biophys.

J. Mol. Biol.

Arch. Biochem. Biophys.

J. Biol. Chem.

Biophys. J.

J. Biol. Chem.

J. Biol. Chem.

J. Ultrastruct. Res.

Biochimie

Comp. Biochem. Physiol.

Comp. Biochem. Physiol.

Molecular structure of the fibers of the collagen group

J. Int. Soc. Leather Trades Chem.

The byssus of the mussel Mytilus from the molecules to the organ: functional performance resides in the ultrastructural assembly

The ultrastructure of the byssal apparatus of Mytilus galloprovincialis. Analysis of byssus by polarized light microscopy

J. Submicr. Cytol.

The ultrastructure of the byssal apparatus of Mytilus galloprovincialis. Observations by transmission electron microscopy

Cell Tiss. Res.

Mechanical design of mussel byssus: Material yield enhances attachment strength

J. Exp. Biol.

Location and analysis of byssal structural proteins of Mytilus edulis

J. Morphol.

Étude roentgénographique des kératines sécrétées

C. R. Acad. Sci., Paris

A gene encoding a novel glycine-rich structural protein of petunia

Nature

Extensible collagen in mussel byssus: A natural block copolymer

Science

The sequence HGLGHGHEQQHGLGHGH in the light chain of high molecular weight kininogen serves as a primary structural feature for zinc-dependent binding to an anionic surface

Protein Sci.

The physical properties of spider's silk and their role in the design of orb webs

J. Exp. Biol.

Biology and Mechanics of the Wave Swept Environment

Attachment and orientation of Mytilus edulis L. in flowing water

Ophelia

Versatile collagens in invertebrates

Science

Sea urchin collagen evolutionarily homologous to vertebrate pro-α2(I) collagen

J. Biol. Chem.

The stabilization of fibrillar collagen matrices with 3,4-dihydroxyphenylalanine

J. Biomed. Mat. Res.

Light microscopic waveforms in collagenous tissues and their structural implications

Minireview
The peculiar collagens of mussel byssus