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Pathogenicity and virulence of Streptococcus pneumoniae: Cutting to the chase on proteases

Bacterial proteases and peptidases are integral to cell physiology and stability, and their necessity in Streptococcus pneumoniae is no exception. Protein cleavage and processing mechanisms within the bacterial cell serve to ensure that the cell lives and functions in its commensal habitat and can r...

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Detalles Bibliográficos
Autor principal: Marquart, Mary E.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Taylor & Francis 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7939560/
https://www.ncbi.nlm.nih.gov/pubmed/33660565
http://dx.doi.org/10.1080/21505594.2021.1889812
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author Marquart, Mary E.
author_facet Marquart, Mary E.
author_sort Marquart, Mary E.
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description Bacterial proteases and peptidases are integral to cell physiology and stability, and their necessity in Streptococcus pneumoniae is no exception. Protein cleavage and processing mechanisms within the bacterial cell serve to ensure that the cell lives and functions in its commensal habitat and can respond to new environments presenting stressful conditions. For S. pneumoniae, the human nasopharynx is its natural habitat. In the context of virulence, movement of S. pneumoniae to the lungs, blood, or other sites can instigate responses by the bacteria that result in their proteases serving dual roles of self-protein processors and virulence factors of host protein targets.
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spelling pubmed-79395602021-03-18 Pathogenicity and virulence of Streptococcus pneumoniae: Cutting to the chase on proteases Marquart, Mary E. Virulence Review Article Bacterial proteases and peptidases are integral to cell physiology and stability, and their necessity in Streptococcus pneumoniae is no exception. Protein cleavage and processing mechanisms within the bacterial cell serve to ensure that the cell lives and functions in its commensal habitat and can respond to new environments presenting stressful conditions. For S. pneumoniae, the human nasopharynx is its natural habitat. In the context of virulence, movement of S. pneumoniae to the lungs, blood, or other sites can instigate responses by the bacteria that result in their proteases serving dual roles of self-protein processors and virulence factors of host protein targets. Taylor & Francis 2021-03-04 /pmc/articles/PMC7939560/ /pubmed/33660565 http://dx.doi.org/10.1080/21505594.2021.1889812 Text en © 2021 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
Marquart, Mary E.
Pathogenicity and virulence of Streptococcus pneumoniae: Cutting to the chase on proteases
title Pathogenicity and virulence of Streptococcus pneumoniae: Cutting to the chase on proteases
title_full Pathogenicity and virulence of Streptococcus pneumoniae: Cutting to the chase on proteases
title_fullStr Pathogenicity and virulence of Streptococcus pneumoniae: Cutting to the chase on proteases
title_full_unstemmed Pathogenicity and virulence of Streptococcus pneumoniae: Cutting to the chase on proteases
title_short Pathogenicity and virulence of Streptococcus pneumoniae: Cutting to the chase on proteases
title_sort pathogenicity and virulence of streptococcus pneumoniae: cutting to the chase on proteases
topic Review Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7939560/
https://www.ncbi.nlm.nih.gov/pubmed/33660565
http://dx.doi.org/10.1080/21505594.2021.1889812
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