| Summary: | The freshwater zebra mussel Dreissena polymorpha is a biofouling species that adheres to varied substrates underwater using a proteinaceous byssus that consists of a bundle of threads tipped with adhesive plaques. This underwater adhesion is an inspiration for the development of medical and dental bioadhesives, however, the byssus is highly resistant to biochemical characterization owing to extensive cross-linking and therefore, limited information is available on the mechanisms of adhesion and cohesion of byssal proteins. We report here on the identification and sequence analysis of eight novel byssal proteins identified in the soluble extract and insoluble matrix from induced, freshly secreted byssal threads with minimal cross-linking, using gel electrophoresis and LC-MS/MS sequencing techniques. Identified byssal proteins have theoretical molecular weights ranging from 4.1 kDa to 20.1 kDa and isoelectric points ranging from 4.2 to 9.6 and have several common characteristics including consensus repeat patterns, block structures and defined sequence motifs.
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