Byssus Formation in Mytilus

Silverman, Heather G.; Roberto, Francisco

doi:10.1007/978-3-7091-0286-2_18

Cited by 15 publications

(12 citation statements)

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“…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. As gland names from previous studies 26 have little correspondence to the functional roles we demonstrate in this study ( Table 1 ), we designate the glands here as the core, cuticle and plaque glands, respectively, and use these names throughout the paper ( Fig. 2a , Table 1 ).…”

Section: Resultsmentioning

confidence: 99%

“…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 texture 5 21 22 23 24 25 . 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 byssus 26 . However, there has been little direct correlation between the proteins identified in the threads and those present in the glands.…”

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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: Resultsmentioning

confidence: 99%

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confidence: 99%

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

et al. 2017

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“…To place our results into context, it is useful to consider the mechanism and conditions under which mussel byssal proteins are secreted. 44 Byssal threads and adhesive plaques are formed by injection molding of liquid precursors within the distal depression and ventral groove of the mussel foot, followed by release of the newly formed thread and adhesive plaque after several minutes of ‘curing’. Recent unpublished work has determined that the initial pH of secreted byssal proteins is ~4, 45 while published work from the same group had earlier indicated an initial pH of ~5.8 ± 0.3.…”

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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“…It is composed of bundles of threads that terminate in the byssal plaque, which attaches to the substrate. The molecules of the plaque have already been identified [ 8 - 13 ]. Substantial progress has been made in characterizing the cement glue of barnacles [ 14 - 18 ].…”

Section: Introductionmentioning

confidence: 99%

Biological adhesion of the flatworm Macrostomum lignano relies on a duo-gland system and is mediated by a cell type-specific intermediate filament protein

et al. 2014

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BackgroundFree-living flatworms, in both marine and freshwater environments, are able to adhere to and release from a substrate several times within a second. This reversible adhesion relies on adhesive organs comprised of three cell types: an adhesive gland cell, a releasing gland cell, and an anchor cell, which is a modified epidermal cell responsible for structural support. However, nothing is currently known about the molecules that are involved in this adhesion process.ResultsIn this study we present the detailed morphology of the adhesive organs of the free-living marine flatworm Macrostomum lignano. About 130 adhesive organs are located in a horse-shoe-shaped arc along the ventral side of the tail plate. Each organ consists of exactly three cells, an adhesive gland cell, a releasing gland cell, and an anchor cell. The necks of the two gland cells penetrate the anchor cell through a common pore. Modified microvilli of the anchor cell form a collar surrounding the necks of the adhesive- and releasing glands, jointly forming the papilla, the outer visible part of the adhesive organs. Next, we identified an intermediate filament (IF) gene, macif1, which is expressed in the anchor cells. RNA interference mediated knock-down resulted in the first experimentally induced non-adhesion phenotype in any marine animal. Specifically, the absence of intermediate filaments in the anchor cells led to papillae with open tips, a reduction of the cytoskeleton network, a decline in hemidesmosomal connections, and to shortened microvilli containing less actin.ConclusionOur findings reveal an elaborate biological adhesion system in a free-living flatworm, which permits impressively rapid temporary adhesion-release performance in the marine environment. We demonstrate that the structural integrity of the supportive cell, the anchor cell, is essential for this adhesion process: the knock-down of the anchor cell-specific intermediate filament gene resulted in the inability of the animals to adhere. The RNAi mediated changes of the anchor cell morphology are comparable to situations observed in human gut epithelia. Therefore, our current findings and future investigations using this powerful flatworm model system might contribute to a better understanding of the function of intermediate filaments and their associated human diseases.

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Byssus Formation in Mytilus

Cited by 15 publications

References 50 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

Biological adhesion of the flatworm Macrostomum lignano relies on a duo-gland system and is mediated by a cell type-specific intermediate filament protein

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Byssus Formation in Mytilus

Cited by 15 publications

References 50 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

Biological adhesion of the flatworm Macrostomum lignano relies on a duo-gland system and is mediated by a cell type-specific intermediate filament protein

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