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A Viral Pilot for HCMV Navigation?

gH/gL virion envelope glycoprotein complexes of herpesviruses serve as entry complexes and mediate viral cell tropism. By binding additional viral proteins, gH/gL forms multimeric complexes which bind to specific host cell receptors. Both Epstein–Barr virus (EBV) and human cytomegalovirus (HCMV) exp...

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Detalles Bibliográficos
Autor principal: Adler, Barbara
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4517130/
https://www.ncbi.nlm.nih.gov/pubmed/26184287
http://dx.doi.org/10.3390/v7072801
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author Adler, Barbara
author_facet Adler, Barbara
author_sort Adler, Barbara
collection PubMed
description gH/gL virion envelope glycoprotein complexes of herpesviruses serve as entry complexes and mediate viral cell tropism. By binding additional viral proteins, gH/gL forms multimeric complexes which bind to specific host cell receptors. Both Epstein–Barr virus (EBV) and human cytomegalovirus (HCMV) express alternative multimeric gH/gL complexes. Relative amounts of these alternative complexes in the viral envelope determine which host cells are preferentially infected. Host cells of EBV can modulate the gH/gL complex complement of progeny viruses by cell type-dependent degradation of one of the associating proteins. Host cells of HCMV modulate the tropism of their virus progenies by releasing or not releasing virus populations with a specific gH/gL complex complement out of a heterogeneous pool of virions. The group of Jeremy Kamil has recently shown that the HCMV ER-resident protein UL148 controls integration of one of the HCMV gH/gL complexes into virions and thus creates a pool of virions which can be routed by different host cells. This first mechanistic insight into regulation of the gH/gL complex complement of HCMV progenies presents UL148 as a pilot candidate for HCMV navigation in its infected host.
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spelling pubmed-45171302015-07-28 A Viral Pilot for HCMV Navigation? Adler, Barbara Viruses Commentary gH/gL virion envelope glycoprotein complexes of herpesviruses serve as entry complexes and mediate viral cell tropism. By binding additional viral proteins, gH/gL forms multimeric complexes which bind to specific host cell receptors. Both Epstein–Barr virus (EBV) and human cytomegalovirus (HCMV) express alternative multimeric gH/gL complexes. Relative amounts of these alternative complexes in the viral envelope determine which host cells are preferentially infected. Host cells of EBV can modulate the gH/gL complex complement of progeny viruses by cell type-dependent degradation of one of the associating proteins. Host cells of HCMV modulate the tropism of their virus progenies by releasing or not releasing virus populations with a specific gH/gL complex complement out of a heterogeneous pool of virions. The group of Jeremy Kamil has recently shown that the HCMV ER-resident protein UL148 controls integration of one of the HCMV gH/gL complexes into virions and thus creates a pool of virions which can be routed by different host cells. This first mechanistic insight into regulation of the gH/gL complex complement of HCMV progenies presents UL148 as a pilot candidate for HCMV navigation in its infected host. MDPI 2015-07-15 /pmc/articles/PMC4517130/ /pubmed/26184287 http://dx.doi.org/10.3390/v7072801 Text en © 2015 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Commentary
Adler, Barbara
A Viral Pilot for HCMV Navigation?
title A Viral Pilot for HCMV Navigation?
title_full A Viral Pilot for HCMV Navigation?
title_fullStr A Viral Pilot for HCMV Navigation?
title_full_unstemmed A Viral Pilot for HCMV Navigation?
title_short A Viral Pilot for HCMV Navigation?
title_sort viral pilot for hcmv navigation?
topic Commentary
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4517130/
https://www.ncbi.nlm.nih.gov/pubmed/26184287
http://dx.doi.org/10.3390/v7072801
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