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Byssal proteins of the freshwater zebra mussel, Dreissena polymorpha.

Authors
  • Gantayet, Arpita1
  • Ohana, Lily
  • Sone, Eli D
  • 1 Institute of Biomaterials & Biomedical Engineering, University of Toronto, Toronto, ON, Canada. , (Canada)
Type
Published Article
Journal
Biofouling
Publisher
Informa UK (Taylor & Francis)
Publication Date
Jan 01, 2013
Volume
29
Issue
1
Pages
77–85
Identifiers
DOI: 10.1080/08927014.2012.746672
PMID: 23211030
Source
Medline
License
Unknown

Abstract

The freshwater zebra mussel (Dreissena polymorpha) is a notorious biofouling organism. It adheres to a variety of substrata underwater by means of a proteinaceous structure called the byssus, which consists of a number of threads with adhesive plaques at the tips. The byssal proteins are difficult to characterize due to extensive cross-linking of 3,4-dihydroxyphenylalanine (DOPA), which renders the mature structure largely resistant to protein extraction and immunolocalization. By inducing secretion of fresh threads and plaques in which cross-linking is minimized, three novel zebra mussel byssal proteins were identified following extraction and separation by gel electrophoresis. Peptide fragment fingerprinting was used to match tryptic digests of several gel bands against a cDNA library of genes expressed uniquely in the mussel foot, the organ which secretes the byssus. This allowed identification of a more complete sequence of Dpfp2 (D. polymorpha foot protein 2), a known DOPA-containing byssal protein, and a partial sequence of Dpfp5, a novel protein with several typical characteristics of mussel adhesive proteins.

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