ArticleMarine biotechnology (New York, N.Y.)2014
Novel proteins identified in the insoluble byssal matrix of the freshwater zebra mussel.
Article in Marine biotechnology (New York, N.Y.), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 28 citations in OpenAlex.
- Identification and characterization of a wet adhesive protein extracted fromProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Invasive mussels fashion silk-like byssus via mechanical processing of massive horizontally acquired coiled coils.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Glycoproteins Involved in Sea Urchin Temporary Adhesion.Marine drugs · 2023Article
- The genome of the zebra mussel, Dreissena polymorpha: a resource for comparative genomics, invasion genetics, and biocontrol.G3 (Bethesda, Md.) · 2022Article
- Structure, function and parallel evolution of the bivalve byssus, with insights from proteomes and the zebra mussel genome.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2021Article
- Integrative Transcriptome and Proteome Analysis of the Tube Foot and Adhesive Secretions of the Sea UrchinInternational journal of molecular sciences · 2020Article
- Fingerprinting of Proteins that Mediate Quagga Mussel Adhesion using a De Novo Assembled Foot Transcriptome.Scientific reports · 2019Article
- Tick attachment cement - reviewing the mysteries of a biological skin plug system.Biological reviews of the Cambridge Philosophical Society · 2018Review
- Byssus Structure and Protein Composition in the Highly Invasive Fouling MusselFrontiers in physiology · 2018Article
- A cohort of new adhesive proteins identified from transcriptomic analysis of mussel foot glands.Journal of the Royal Society, Interface · 2017Article
- Mussel adhesion is dictated by time-regulated secretion and molecular conformation of mussel adhesive proteins.Nature communications · 2015Article
- Extensible byssus of Pinctada fucata: Ca(2+)-stabilized nanocavities and a thrombospondin-1 protein.Scientific reports · 2015Article
- Integration of Transcriptomic and Proteomic Approaches Provides a Core Set of Genes for Understanding of Scallop Attachment.Marine biotechnology (New York, N.Y.) · 2015Article
- Experimental strategies for the identification and characterization of adhesive proteins in animals: a review.Interface focus · 2015Review
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3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The freshwater zebra mussel, Dreissena polymorpha, is an invasive, biofouling species that adheres to a variety of substrates underwater, using a proteinaceous anchor called the byssus. The byssus consists of a number of threads with adhesive plaques at the tips. It contains the unusual amino acid 3, 4-dihydroxyphenylalanine (DOPA), which is believed to play an important role in adhesion, in addition to providing structural integrity to the byssus through cross-linking. Extensive DOPA cross-linking, however, renders the zebra mussel byssus highly resistant to protein extraction, and therefore limits byssal protein identification. We report here on the identification of seven novel byssal proteins in the insoluble byssal matrix following protein extraction from induced, freshly secreted byssal threads with minimal cross-linking. These proteins were identified by LC-MS/MS analysis of tryptic digests of the matrix proteins by spectrum matching against a zebra mussel cDNA library of genes unique to the mussel foot, the organ that secretes the byssus. All seven proteins were present in both the plaque and thread. Comparisons of the protein sequences revealed common features of zebra mussel byssal proteins, and several recurring sequence motifs. Although their sequences are unique, many of the proteins display similarities to marine mussel byssal proteins, as well as to adhesive and structural proteins from other species. The large expansion of the byssal proteome reported here represents an important step towards understanding zebra mussel adhesion.
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