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Specificity switching in virus–receptor complexes

Several structures of complexes between viral attachment proteins and their cellular receptors have been determined recently, enhancing our understanding of the molecular recognition processes that guide formation of virus–receptor complexes. Moreover, these structures also highlight strategies by w...

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Detalles Bibliográficos
Autores principales: Stehle, Thilo, Casasnovas, José M
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier Ltd. 2009
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7126087/
https://www.ncbi.nlm.nih.gov/pubmed/19342221
http://dx.doi.org/10.1016/j.sbi.2009.02.013
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author Stehle, Thilo
Casasnovas, José M
author_facet Stehle, Thilo
Casasnovas, José M
author_sort Stehle, Thilo
collection PubMed
description Several structures of complexes between viral attachment proteins and their cellular receptors have been determined recently, enhancing our understanding of the molecular recognition processes that guide formation of virus–receptor complexes. Moreover, these structures also highlight strategies by which highly similar viral proteins within a single virus family can adapt to engage different receptors. Consequences of such differences are altered tropism and pathogenicity. An improved understanding of the molecular details of this specificity switching in receptor binding will help to establish links between receptor tropism, spread, and disease. Moreover, it also has relevance for the design and use of viruses as gene delivery vehicles with altered properties as well as for the identification of target viral epitopes of new vaccines.
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spelling pubmed-71260872020-04-08 Specificity switching in virus–receptor complexes Stehle, Thilo Casasnovas, José M Curr Opin Struct Biol Article Several structures of complexes between viral attachment proteins and their cellular receptors have been determined recently, enhancing our understanding of the molecular recognition processes that guide formation of virus–receptor complexes. Moreover, these structures also highlight strategies by which highly similar viral proteins within a single virus family can adapt to engage different receptors. Consequences of such differences are altered tropism and pathogenicity. An improved understanding of the molecular details of this specificity switching in receptor binding will help to establish links between receptor tropism, spread, and disease. Moreover, it also has relevance for the design and use of viruses as gene delivery vehicles with altered properties as well as for the identification of target viral epitopes of new vaccines. Elsevier Ltd. 2009-04 2009-04-01 /pmc/articles/PMC7126087/ /pubmed/19342221 http://dx.doi.org/10.1016/j.sbi.2009.02.013 Text en Copyright © 2009 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
Stehle, Thilo
Casasnovas, José M
Specificity switching in virus–receptor complexes
title Specificity switching in virus–receptor complexes
title_full Specificity switching in virus–receptor complexes
title_fullStr Specificity switching in virus–receptor complexes
title_full_unstemmed Specificity switching in virus–receptor complexes
title_short Specificity switching in virus–receptor complexes
title_sort specificity switching in virus–receptor complexes
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7126087/
https://www.ncbi.nlm.nih.gov/pubmed/19342221
http://dx.doi.org/10.1016/j.sbi.2009.02.013
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