Epiphragmin, the major protein of epiphragm mucus from the vineyard snail, Cernuella virgata

The organic fraction of epiphragm mucus from the snail Cernuella virgata (Mollusca: Helicidae) consists predominantly of protein (17-23 dry wt.%) rather than carbohydrate (<= 0.4-2.0 dry wt.%), and the former underpins epiphragm membrane structure. The major protein ('epiphragmin') has an apparent molecular mass of similar to 86 kDa and is encoded by a cDNA (Genbank accession EF602752) which specifies a secreted protein of 81.2 kDa. The central region of the epiphragmin polypeptide is a coiled coil-forming region which is homologous to part of Ag1Z, a bacterial filament-forming protein. Coiled coil-driven self-assembly of epiphragmin probably underpins the formation of sheets in epiphragm membranes and the ability of epiphragm mucus to serve as an adhesive. The C-terminal region of epiphragmin is a fibrinogen-related domain (FReD) that is homologous to the fibrinogen-related proteins (FREPs) found in the hemolymph of freshwater snails. The material properties of epiphragm membranes resemble those of bovine ligament elastin. Wooden lap joints bonded by rehydrated epiphragm fragments developed dry shear strength values of 1.4 +/- 0.1 MPa. Crown Copyright (C) 2007 Published by Elsevier Inc. All rights reserved.