Identification of proteins in the adhesive trails of the diatom Amphora coffeaeformis
Research output: Contribution to journal › Research article › Contributed › peer-review
Contributors
Abstract
Throughout all kingdoms of life, a large number of adhesive biomolecules have evolved to allow organisms to adhere to surfaces underwater. Proteins play an important role in the adhesion of numerous marine invertebrates (e.g. mussels, sea stars, sea urchins) whereas much less is known about the biological adhesive:, from marine plants, including the diatoms. Diatoms arc unicellular microalgae that together with bacteria dominate marine biofilms in sunlit habitats. In this study we present the first proteomics analyses of the diatom adhesive material isolated from the tenacious fouling species Amphora coffeaeformis. W identified 21 proteins, of which 13 are diatom-specific. Ten of these proteins share a conserved C-terminal domain, termed GDPH domain, which is widespread yet not ubiquitously present in all diatom classes. Immunofluorescence localization of a GDPH domain bearing protein (Ac629) as Well as two other proteins identified in this study (Ac1442, Ac9617) demonstrated that these are components of the adhesive trails that are secreted by cells that glide on surfaces.
This article is part of the theme issue 'Transdisciplinary approaches to the study of adhesion and adhesives in biological systems'.
Details
Original language | English |
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Article number | 20190196 |
Number of pages | 9 |
Journal | Philosophical Transactions of the Royal Society B: Biological Sciences |
Volume | 374 |
Issue number | 1784 |
Publication status | Published - 9 Sept 2019 |
Peer-reviewed | Yes |
External IDs
Scopus | 85071896858 |
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ORCID | /0000-0002-4533-8860/work/142241021 |
Keywords
Sustainable Development Goals
Keywords
- diatom, adhesion, motility, marine biofouling, BIOCHEMICAL-CHARACTERIZATION, SUBSTRATUM ADHESION, SEA, MECHANISMS, MUCIN, LOCALIZATION, AGGREGATION, CLEAVAGE, SEQUENCE, MUCILAGE