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Polymer Adhesin Domains in Gram-Positive Cell Surface Proteins

Surface proteins in Gram-positive bacteria are often involved in biofilm formation, host-cell interactions, and surface attachment. Here we review a protein module found in surface proteins that are often encoded on various mobile genetic elements like conjugative plasmids. This module binds to diff...

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Autores principales: Järvå, Michael A., Hirt, Helmut, Dunny, Gary M., Berntsson, Ronnie P.-A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7726212/
https://www.ncbi.nlm.nih.gov/pubmed/33324381
http://dx.doi.org/10.3389/fmicb.2020.599899
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author Järvå, Michael A.
Hirt, Helmut
Dunny, Gary M.
Berntsson, Ronnie P.-A.
author_facet Järvå, Michael A.
Hirt, Helmut
Dunny, Gary M.
Berntsson, Ronnie P.-A.
author_sort Järvå, Michael A.
collection PubMed
description Surface proteins in Gram-positive bacteria are often involved in biofilm formation, host-cell interactions, and surface attachment. Here we review a protein module found in surface proteins that are often encoded on various mobile genetic elements like conjugative plasmids. This module binds to different types of polymers like DNA, lipoteichoic acid and glucans, and is here termed polymer adhesin domain. We analyze all proteins that contain a polymer adhesin domain and classify the proteins into distinct classes based on phylogenetic and protein domain analysis. Protein function and ligand binding show class specificity, information that will be useful in determining the function of the large number of so far uncharacterized proteins containing a polymer adhesin domain.
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spelling pubmed-77262122020-12-14 Polymer Adhesin Domains in Gram-Positive Cell Surface Proteins Järvå, Michael A. Hirt, Helmut Dunny, Gary M. Berntsson, Ronnie P.-A. Front Microbiol Microbiology Surface proteins in Gram-positive bacteria are often involved in biofilm formation, host-cell interactions, and surface attachment. Here we review a protein module found in surface proteins that are often encoded on various mobile genetic elements like conjugative plasmids. This module binds to different types of polymers like DNA, lipoteichoic acid and glucans, and is here termed polymer adhesin domain. We analyze all proteins that contain a polymer adhesin domain and classify the proteins into distinct classes based on phylogenetic and protein domain analysis. Protein function and ligand binding show class specificity, information that will be useful in determining the function of the large number of so far uncharacterized proteins containing a polymer adhesin domain. Frontiers Media S.A. 2020-11-26 /pmc/articles/PMC7726212/ /pubmed/33324381 http://dx.doi.org/10.3389/fmicb.2020.599899 Text en Copyright © 2020 Järvå, Hirt, Dunny and Berntsson. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Microbiology
Järvå, Michael A.
Hirt, Helmut
Dunny, Gary M.
Berntsson, Ronnie P.-A.
Polymer Adhesin Domains in Gram-Positive Cell Surface Proteins
title Polymer Adhesin Domains in Gram-Positive Cell Surface Proteins
title_full Polymer Adhesin Domains in Gram-Positive Cell Surface Proteins
title_fullStr Polymer Adhesin Domains in Gram-Positive Cell Surface Proteins
title_full_unstemmed Polymer Adhesin Domains in Gram-Positive Cell Surface Proteins
title_short Polymer Adhesin Domains in Gram-Positive Cell Surface Proteins
title_sort polymer adhesin domains in gram-positive cell surface proteins
topic Microbiology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7726212/
https://www.ncbi.nlm.nih.gov/pubmed/33324381
http://dx.doi.org/10.3389/fmicb.2020.599899
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