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Trehalose and bacterial virulence

Trehalose is a disaccharide of two D-glucose molecules linked by a glycosidic linkage, which plays both structural and functional roles in bacteria. Trehalose can be synthesized and degraded by several pathways, and induction of trehalose biosynthesis is typically associated with exposure to abiotic...

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Autores principales: Vanaporn, Muthita, Titball, Richard W
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Taylor & Francis 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7549927/
https://www.ncbi.nlm.nih.gov/pubmed/32862781
http://dx.doi.org/10.1080/21505594.2020.1809326
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author Vanaporn, Muthita
Titball, Richard W
author_facet Vanaporn, Muthita
Titball, Richard W
author_sort Vanaporn, Muthita
collection PubMed
description Trehalose is a disaccharide of two D-glucose molecules linked by a glycosidic linkage, which plays both structural and functional roles in bacteria. Trehalose can be synthesized and degraded by several pathways, and induction of trehalose biosynthesis is typically associated with exposure to abiotic stress. The ability of trehalose to protect against abiotic stress has been exploited to stabilize a range of bacterial vaccines. More recently, there has been interest in the role of this molecule in microbial virulence. There is now evidence that trehalose or trehalose derivatives play important roles in virulence of a diverse range of Gram-positive and Gram-negative pathogens of animals or plants. Trehalose and/or trehalose derivatives can play important roles in host colonization and growth in the host, and can modulate the interactions with host defense mechanisms. However, the roles are typically pathogen-specific. These findings suggest that trehalose metabolism may be a target for novel pathogen-specific rather than broad spectrum interventions.
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spelling pubmed-75499272020-10-27 Trehalose and bacterial virulence Vanaporn, Muthita Titball, Richard W Virulence Review Article Trehalose is a disaccharide of two D-glucose molecules linked by a glycosidic linkage, which plays both structural and functional roles in bacteria. Trehalose can be synthesized and degraded by several pathways, and induction of trehalose biosynthesis is typically associated with exposure to abiotic stress. The ability of trehalose to protect against abiotic stress has been exploited to stabilize a range of bacterial vaccines. More recently, there has been interest in the role of this molecule in microbial virulence. There is now evidence that trehalose or trehalose derivatives play important roles in virulence of a diverse range of Gram-positive and Gram-negative pathogens of animals or plants. Trehalose and/or trehalose derivatives can play important roles in host colonization and growth in the host, and can modulate the interactions with host defense mechanisms. However, the roles are typically pathogen-specific. These findings suggest that trehalose metabolism may be a target for novel pathogen-specific rather than broad spectrum interventions. Taylor & Francis 2020-08-30 /pmc/articles/PMC7549927/ /pubmed/32862781 http://dx.doi.org/10.1080/21505594.2020.1809326 Text en © 2020 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group. https://creativecommons.org/licenses/by/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Review Article
Vanaporn, Muthita
Titball, Richard W
Trehalose and bacterial virulence
title Trehalose and bacterial virulence
title_full Trehalose and bacterial virulence
title_fullStr Trehalose and bacterial virulence
title_full_unstemmed Trehalose and bacterial virulence
title_short Trehalose and bacterial virulence
title_sort trehalose and bacterial virulence
topic Review Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7549927/
https://www.ncbi.nlm.nih.gov/pubmed/32862781
http://dx.doi.org/10.1080/21505594.2020.1809326
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