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Molecular gymnastics at the herpesvirus surface

This review analyses recent structural results that provide clues about a possible molecular mechanism for the transmission of a fusogenic signal among the envelope glycoproteins of the herpes simplex virus on receptor binding by glycoprotein gD. This signal triggers the membrane-fusion machinery of...

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Detalles Bibliográficos
Autor principal: Rey, Félix A
Formato: Texto
Lenguaje:English
Publicado: 2006
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1618366/
https://www.ncbi.nlm.nih.gov/pubmed/17016458
http://dx.doi.org/10.1038/sj.embor.7400807
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author Rey, Félix A
author_facet Rey, Félix A
author_sort Rey, Félix A
collection PubMed
description This review analyses recent structural results that provide clues about a possible molecular mechanism for the transmission of a fusogenic signal among the envelope glycoproteins of the herpes simplex virus on receptor binding by glycoprotein gD. This signal triggers the membrane-fusion machinery of the virus—contained in glycoproteins gB, gH and gL—to induce the merging of viral and cellular membranes, and to allow virus entry into target cells. This activating process parallels that of γ-retroviruses, in which receptor binding by the amino-terminal domain of the envelope protein activates the fusogenic potential of the virion in a similar way, despite the different organization of the envelope complexes of these two types of viruses. Therefore, the new structural results on the interaction of gD with its receptors might also provide insights into the mechanism of fusogenic signal transmission in γ-retroviruses. Furthermore, the fusion activation parallels with retroviruses, together with the recently reported structural homology of gB with the rhabdovirus envelope glycoprotein indicate that the complex entry apparatus of herpesviruses appears to be functionally related to that of simpler enveloped viruses.
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spelling pubmed-16183662007-10-01 Molecular gymnastics at the herpesvirus surface Rey, Félix A EMBO Rep Review Article This review analyses recent structural results that provide clues about a possible molecular mechanism for the transmission of a fusogenic signal among the envelope glycoproteins of the herpes simplex virus on receptor binding by glycoprotein gD. This signal triggers the membrane-fusion machinery of the virus—contained in glycoproteins gB, gH and gL—to induce the merging of viral and cellular membranes, and to allow virus entry into target cells. This activating process parallels that of γ-retroviruses, in which receptor binding by the amino-terminal domain of the envelope protein activates the fusogenic potential of the virion in a similar way, despite the different organization of the envelope complexes of these two types of viruses. Therefore, the new structural results on the interaction of gD with its receptors might also provide insights into the mechanism of fusogenic signal transmission in γ-retroviruses. Furthermore, the fusion activation parallels with retroviruses, together with the recently reported structural homology of gB with the rhabdovirus envelope glycoprotein indicate that the complex entry apparatus of herpesviruses appears to be functionally related to that of simpler enveloped viruses. 2006-10 /pmc/articles/PMC1618366/ /pubmed/17016458 http://dx.doi.org/10.1038/sj.embor.7400807 Text en Copyright © 2006, European Molecular Biology Organization
spellingShingle Review Article
Rey, Félix A
Molecular gymnastics at the herpesvirus surface
title Molecular gymnastics at the herpesvirus surface
title_full Molecular gymnastics at the herpesvirus surface
title_fullStr Molecular gymnastics at the herpesvirus surface
title_full_unstemmed Molecular gymnastics at the herpesvirus surface
title_short Molecular gymnastics at the herpesvirus surface
title_sort molecular gymnastics at the herpesvirus surface
topic Review Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1618366/
https://www.ncbi.nlm.nih.gov/pubmed/17016458
http://dx.doi.org/10.1038/sj.embor.7400807
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