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Predator-labeling effect on byssus production in marine mussels Perna viridis (L.) and Brachidontes variabilis (Krauss).

Mussels Perna viridis and Brachidontes variabilis were exposed to chemical cues from the predatory crab Thalamita danae maintained on different diets, and byssal thread production of the mussels was studied. P. viridis produced the highest number as well as the thickest and longest byssal threads when they were exposed to crabs maintained on a diet of P. viridis as compared with those exposed to crabs maintained on a diet of the top shell Monodonta labio, the rock oyster Saccostrea cucullata, or crabs that were starved. For B. variabilis, results were similar, in that a diet containing B. variabilis elicited the greatest response as compared with other treatments. This indicates that the mussels were able to discriminate chemical cues released from predators maintained on different diets, and respond accordingly to the level of predation risk. By increasing the strength of byssal attachment as a defensive trait, the chance of being dislodged and consumed by crabs is reduced. As energy cost involved in the induction of an antipredatory response is considerable, this defensive trait seems to be an advantage to the mussels in enhancing efficiency. The short response time in byssal thread production allows the mussels to increase resistance against predation by crabs at the time when predation pressure is the highest in a tidal cycle.

Animals↗

Mussel byssus and biomolecular materials.

Mussel adhesive proteins are remarkable materials that display an extraordinary capability to adhere to substrates underwater. Recent investigations from groups with quite diverse areas of expertise have made substantial progress in the identification of the genes and proteins that are involved in adhesive formation. These discoveries have led to the development of recombinant proteins and synthetic polypeptides that are able to reproduce the properties of mussel adhesives for applications in medicine and biotechnology.

Adhesiveness↗

The influence of cross-linking on protein-protein interactions in a marine adhesive: the case of two byssus plaque proteins from the blue mussel.

The interaction between two proteins, Mefp-1 and Mefp-2, from the byssal plaque of the blue mussel, Mytilus edulis, was investigated using a quartz crystal microbalance with dissipation monitoring (QCM-D) technique. The challenge in using a surface-sensitive technique to investigate the interaction between two strongly adhesive proteins was met by coupling a biotinylated version of one of the proteins (b-Mefp-1) to an inert two-dimensional arrangement of streptavidin (SA) formed on top of a biotin-doped supported phospholipid bilayer. The interaction between Mefp-1 and Mefp-2 was further investigated by addition of Mefp-2 to SA-coupled b-Mefp-1, where the latter was either in the native state or cross-linked using sodium periodate (NaIO(4)), Cu(2+), or mushroom tyrosinase. With this coupling strategy it is shown that a requirement for attraction between the two proteins is that tyrosinase is used as the cross-linking agent of b-Mefp-1. By inhibiting the enzymatic activity of tyrosinase it is also shown that enzymatic activity is required for both efficient binding of tyrosinase to SA-coupled b-Mefp-1 as well as for the subsequent binding of Mefp-2. In contrast, spontaneous adsorption of Mefp-1 to a methyl-terminated (thiolated) gold surface followed by addition of Mefp-2 results in binding of Mefp-2 for all cross-linking agents. This suggests that cross-linking of Mefp-1 adsorbed on a solid surface induces structural changes in the adsorbed protein layer, resulting in exposure of free surface patches on which Mefp-2 binds.

Animals↗

Tough tendons. Mussel byssus has collagen with silk-like domains.

The primary structure of the alpha-chain of preCol-D (molecular mass = 80 kDa), a tanned collagenous protein predominating in the distal portion of the byssal threads of the mussel Mytilus edulis, was deduced from cDNA to encode an unprecedented natural block copolymer with three major domain types: a central collagen domain flanked by fibroin-like domains and followed by histidine-rich termini. The fibroin-like domains have sequence motifs that strongly resemble the crystalline polyalanine-rich and amorphous glycine-rich regions of spider dragline silk fibroins. The terminal regions resemble the histidine-rich domains of a variety of metal-binding proteins. The silk domains may toughen the collagen by increasing its strength and extensibility. PreCol-D expression is limited to the mussel foot, which contains a longitudinal gradient of preCol-D mRNA. This gradient increases linearly in the proximal to distal direction and reaches a maximum just before the distal depression of the foot.

Amino Acid Sequence↗

Mussel (Mytilus edulis) byssus deposition in response to variations in surface wettability.

Mussels (Mytilus edulis) are economically important in their role as an aquaculture species and also with regard to marine biofouling. They attach tenaciously to a wide variety of submerged surfaces by virtue of collagenous attachment threads termed 'byssi'. The aim of this study was to characterize the spreading of the byssal attachment plaque, which mediates attachment to the surface, on a range of surfaces in response to changes in wettability. To achieve this, well characterized self-assembled monolayers of omega-terminated alkanethiolates on gold were used, allowing correlation of byssal plaque spreading with a single surface characteristic--wettability. The present results were inconsistent with those from previous studies, in that there was a positive correlation between plaque size and surface wettability; a trend which is not explained by conventional wetting theory for a three-phase system. A recent extension to wetting theory with regard to hydrophilic proteins is discussed and the results of settlement assays are used to attempt reconciliation of these results with those of similar previous studies and, also, with recent data presented for the spreading of Ulva linza spore adhesive.

Adhesiveness↗