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Remodeling of host glycoproteins during bacterial infection

Protein glycosylation is a common post-translational modification found in all living organisms. This modification in bacterial pathogens plays a pivotal role in their infectious processes including pathogenicity, immune evasion, and host-pathogen interactions. Importantly, many key proteins of host...

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Autores principales: Kim, Yeolhoe, Ko, Jeong Yeon, Yang, Won Ho
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Korean Society for Biochemistry and Molecular Biology 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8633524/
https://www.ncbi.nlm.nih.gov/pubmed/34674797
http://dx.doi.org/10.5483/BMBRep.2021.54.11.129
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author Kim, Yeolhoe
Ko, Jeong Yeon
Yang, Won Ho
author_facet Kim, Yeolhoe
Ko, Jeong Yeon
Yang, Won Ho
author_sort Kim, Yeolhoe
collection PubMed
description Protein glycosylation is a common post-translational modification found in all living organisms. This modification in bacterial pathogens plays a pivotal role in their infectious processes including pathogenicity, immune evasion, and host-pathogen interactions. Importantly, many key proteins of host immune systems are also glycosylated and bacterial pathogens can notably modulate glycosylation of these host proteins to facilitate pathogenesis through the induction of abnormal host protein activity and abundance. In recent years, interest in studying the regulation of host protein glycosylation caused by bacterial pathogens is increasing to fully understand bacterial pathogenesis. In this review, we focus on how bacterial pathogens regulate remodeling of host glycoproteins during infections to promote the pathogenesis.
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spelling pubmed-86335242021-12-13 Remodeling of host glycoproteins during bacterial infection Kim, Yeolhoe Ko, Jeong Yeon Yang, Won Ho BMB Rep Invited Mini Review Protein glycosylation is a common post-translational modification found in all living organisms. This modification in bacterial pathogens plays a pivotal role in their infectious processes including pathogenicity, immune evasion, and host-pathogen interactions. Importantly, many key proteins of host immune systems are also glycosylated and bacterial pathogens can notably modulate glycosylation of these host proteins to facilitate pathogenesis through the induction of abnormal host protein activity and abundance. In recent years, interest in studying the regulation of host protein glycosylation caused by bacterial pathogens is increasing to fully understand bacterial pathogenesis. In this review, we focus on how bacterial pathogens regulate remodeling of host glycoproteins during infections to promote the pathogenesis. Korean Society for Biochemistry and Molecular Biology 2021-11-30 2021-11-30 /pmc/articles/PMC8633524/ /pubmed/34674797 http://dx.doi.org/10.5483/BMBRep.2021.54.11.129 Text en Copyright © 2021 by the The Korean Society for Biochemistry and Molecular Biology https://creativecommons.org/licenses/by-nc/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0 (https://creativecommons.org/licenses/by-nc/4.0/) ) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Invited Mini Review
Kim, Yeolhoe
Ko, Jeong Yeon
Yang, Won Ho
Remodeling of host glycoproteins during bacterial infection
title Remodeling of host glycoproteins during bacterial infection
title_full Remodeling of host glycoproteins during bacterial infection
title_fullStr Remodeling of host glycoproteins during bacterial infection
title_full_unstemmed Remodeling of host glycoproteins during bacterial infection
title_short Remodeling of host glycoproteins during bacterial infection
title_sort remodeling of host glycoproteins during bacterial infection
topic Invited Mini Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8633524/
https://www.ncbi.nlm.nih.gov/pubmed/34674797
http://dx.doi.org/10.5483/BMBRep.2021.54.11.129
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