An ultrastructutal study of the byssal thread forming system in Mytilus

Tamarin, Arnold; Keller, Patricia J.

doi:10.1016/s0022-5320(72)90110-4

Cited by 83 publications

(51 citation statements)

References 13 publications

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“…2a) revealed three glands with distinct staining signatures, similar in location to descriptions given in previous studies5212223. We provide evidence, however, that directly links the protein contents of each of the three glands to the core, cuticle or plaque of the thread.…”

Section: Resultssupporting

confidence: 84%

“…Currently, however, the mechanistic understanding of this dynamic assembly process is extremely limited and has advanced little in the last 30 years, aside from recent elegant studies on the formation of the plaque adhesive interface1920. The little we do know about this process is principally based on histological and transmission electron microscopy (TEM) investigations, which identified three secretory glands within the mussel foot, each with vesicles of distinctive shape, size and texture52122232425. During thread assembly, these three glands, which have accumulated an excessive number of names over time, presumably secrete the 11 known protein building blocks of the byssus26.…”

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confidence: 99%

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Rapid self-assembly of complex biomolecular architectures during mussel byssus biofabrication

et al. 2017

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Protein-based biogenic materials provide important inspiration for the development of high-performance polymers. The fibrous mussel byssus, for instance, exhibits exceptional wet adhesion, abrasion resistance, toughness and self-healing capacity–properties that arise from an intricate hierarchical organization formed in minutes from a fluid secretion of over 10 different protein precursors. However, a poor understanding of this dynamic biofabrication process has hindered effective translation of byssus design principles into synthetic materials. Here, we explore mussel byssus assembly in Mytilus edulis using a synergistic combination of histological staining and confocal Raman microspectroscopy, enabling in situ tracking of specific proteins during induced thread formation from soluble precursors to solid fibres. Our findings reveal critical insights into this complex biological manufacturing process, showing that protein precursors spontaneously self-assemble into complex architectures, while maturation proceeds in subsequent regulated steps. Beyond their biological importance, these findings may guide development of advanced materials with biomedical and industrial relevance.

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Section: Resultssupporting

confidence: 84%

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confidence: 99%

Rapid self-assembly of complex biomolecular architectures during mussel byssus biofabrication

et al. 2017

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“…The polyphenolic gland has been identified and demonstrated to contain o -diphenols. 47, 48 If dilute FeCl 3 is incubated with the foot, this structure turns grey-green in color, and if Na 2 CO 3 is subsequently added, the structure turns red.47 This, together with research suggesting iron is secreted from the foot into the thread, 17 provides limited support for the idea that Fe 3+ and the DOPA-rich mfps are stored separately in the glandular mussel foot. If this case were true, our results suggest that the mussel may use Fe 3+ as an oxidant for DOPA during the initial (acidic) stages of byssal secretion to induce covalent DOPA-DOPA crosslinks.…”

Section: Discussionmentioning

confidence: 99%

pH-dependent cross-linking of catechols through oxidation via Fe³⁺and potential implications for mussel adhesion

et al. 2014

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The mussel byssus is a remarkable attachment structure that is formed by injection molding and rapid in-situ hardening of concentrated solutions of proteins enriched in the catecholic amino acid 3,4-dihydroxy-L-phenylalanine (DOPA). Fe3+, found in high concentrations in the byssus, has been speculated to participate in redox reactions with DOPA that lead to protein polymerization, however direct evidence to support this hypothesis has been lacking. Using small molecule catechols, DOPA-containing peptides, and native mussel foot proteins, we report the first direct observation of catechol oxidation and polymerization accompanied by reduction of Fe3+ to Fe2+. In the case of the small molecule catechol, we identified two dominant dimer species and characterized their connectivities by nuclear magnetic resonance (NMR), with the C6-C6 and C5-C6 linked species as the major and minor products, respectively. For the DOPA-containing peptide, we studied the pH dependence of the reaction and demonstrated that catechol polymerization occurs readily at low pH, but is increasingly diminished in favor of metal-catechol coordination interactions at higher pH. Finally, we demonstrate that Fe3+ can induce cross-links in native byssal mussel proteins mefp-1 and mcfp-1 at acidic pH. Based on these findings, we discuss the potential implications to the chemistry of mussel adhesion.

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“…Collagen granules are secreted from the collagen gland and go through several identifiable steps during maturation in the foot (Tamarin and Keller, 1972). The most immature collagen granules are referred to as condensing vacuoles, in which the preCols are loosely packed.…”

Section: Significance Of Deamidationmentioning

confidence: 99%

Hyperunstable matrix proteins in the byssus of Mytilus galloprovincialis

Sagert

Waite

2009

Journal of Experimental Biology

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SUMMARYThe marine mussel Mytilus galloprovincialis is tethered to rocks in the intertidal zone by a holdfast known as the byssus. Functioning as a shock absorber, the byssus is composed of threads, the primary molecular components of which are collagencontaining proteins (preCOLs) that largely dictate the higher order self-assembly and mechanical properties of byssal threads. The threads contain additional matrix components that separate and perhaps lubricate the collagenous microfibrils during deformation in tension. In this study, the thread matrix proteins (TMPs), a glycine-, tyrosine-and asparagine-rich protein family, were shown to possess unique repeated sequence motifs, significant transcriptional heterogeneity and were distributed throughout the byssal thread. Deamidation was shown to occur at a significant rate in a recombinant TMP and in the byssal thread as a function of time. Furthermore, charge heterogeneity presumably due to deamidation was observed in TMPs extracted from threads. The TMPs were localized to the preCOL-containing secretory granules in the collagen gland of the foot and are assumed to provide a viscoelastic matrix around the collagenous fibers in byssal threads. Supplementary material available online at

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An ultrastructutal study of the byssal thread forming system in Mytilus

Cited by 83 publications

References 13 publications

Rapid self-assembly of complex biomolecular architectures during mussel byssus biofabrication

Rapid self-assembly of complex biomolecular architectures during mussel byssus biofabrication

pH-dependent cross-linking of catechols through oxidation via Fe³⁺and potential implications for mussel adhesion

Hyperunstable matrix proteins in the byssus of Mytilus galloprovincialis

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An ultrastructutal study of the byssal thread forming system in Mytilus

Cited by 83 publications

References 13 publications

Rapid self-assembly of complex biomolecular architectures during mussel byssus biofabrication

Rapid self-assembly of complex biomolecular architectures during mussel byssus biofabrication

pH-dependent cross-linking of catechols through oxidation via Fe3+and potential implications for mussel adhesion

Hyperunstable matrix proteins in the byssus of Mytilus galloprovincialis

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pH-dependent cross-linking of catechols through oxidation via Fe³⁺and potential implications for mussel adhesion