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Virus glycosylation: role in virulence and immune interactions

The study of N-linked glycosylation as it relates to virus biology has become an area of intense interest in recent years due to its ability to impart various advantages to virus survival and virulence. HIV and influenza, two clear threats to human health, have been shown to rely on expression of sp...

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Detalles Bibliográficos
Autores principales: Vigerust, David J., Shepherd, Virginia L.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier Ltd. 2007
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7127133/
https://www.ncbi.nlm.nih.gov/pubmed/17398101
http://dx.doi.org/10.1016/j.tim.2007.03.003
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author Vigerust, David J.
Shepherd, Virginia L.
author_facet Vigerust, David J.
Shepherd, Virginia L.
author_sort Vigerust, David J.
collection PubMed
description The study of N-linked glycosylation as it relates to virus biology has become an area of intense interest in recent years due to its ability to impart various advantages to virus survival and virulence. HIV and influenza, two clear threats to human health, have been shown to rely on expression of specific oligosaccharides to evade detection by the host immune system. Additionally, other viruses such as Hendra, SARS-CoV, influenza, hepatitis and West Nile rely on N-linked glycosylation for crucial functions such as entry into host cells, proteolytic processing and protein trafficking. This review focuses on recent findings on the importance of glycosylation to viral virulence and immune evasion for several prominent human pathogens.
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spelling pubmed-71271332020-04-08 Virus glycosylation: role in virulence and immune interactions Vigerust, David J. Shepherd, Virginia L. Trends Microbiol Article The study of N-linked glycosylation as it relates to virus biology has become an area of intense interest in recent years due to its ability to impart various advantages to virus survival and virulence. HIV and influenza, two clear threats to human health, have been shown to rely on expression of specific oligosaccharides to evade detection by the host immune system. Additionally, other viruses such as Hendra, SARS-CoV, influenza, hepatitis and West Nile rely on N-linked glycosylation for crucial functions such as entry into host cells, proteolytic processing and protein trafficking. This review focuses on recent findings on the importance of glycosylation to viral virulence and immune evasion for several prominent human pathogens. Elsevier Ltd. 2007-05 2007-03-30 /pmc/articles/PMC7127133/ /pubmed/17398101 http://dx.doi.org/10.1016/j.tim.2007.03.003 Text en Copyright © 2007 Elsevier Ltd. All rights reserved. Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.
spellingShingle Article
Vigerust, David J.
Shepherd, Virginia L.
Virus glycosylation: role in virulence and immune interactions
title Virus glycosylation: role in virulence and immune interactions
title_full Virus glycosylation: role in virulence and immune interactions
title_fullStr Virus glycosylation: role in virulence and immune interactions
title_full_unstemmed Virus glycosylation: role in virulence and immune interactions
title_short Virus glycosylation: role in virulence and immune interactions
title_sort virus glycosylation: role in virulence and immune interactions
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7127133/
https://www.ncbi.nlm.nih.gov/pubmed/17398101
http://dx.doi.org/10.1016/j.tim.2007.03.003
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