Identification of proteins in the adhesive trails of the diatom Amphora coffeaeformis

Research output: Contribution to journalResearch articleContributedpeer-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 languageEnglish
Article number20190196
Number of pages9
JournalPhilosophical Transactions of the Royal Society B: Biological Sciences
Volume374
Issue number1784
Publication statusPublished - 9 Sept 2019
Peer-reviewedYes

External IDs

Scopus 85071896858
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

Library keywords