Antibody evasion by a gammaherpesvirus O-glycan shield.

All gammaherpesviruses encode a major glycoprotein homologous to the Epstein-Barr virus gp350. These glycoproteins are often involved in cell binding, and some provide neutralization targets. However, the capacity of gammaherpesviruses for long-term transmission from immune hosts implies that in viv...

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Autores principales:	Bénédicte Machiels, Céline Lété, Antoine Guillaume, Jan Mast, Philip G Stevenson, Alain Vanderplasschen, Laurent Gillet
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2011
Materias:	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/a5a9fe012b994b9bade2cab122bdee48
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spelling	oai:doaj.org-article:a5a9fe012b994b9bade2cab122bdee482021-11-18T06:05:06ZAntibody evasion by a gammaherpesvirus O-glycan shield.1553-73661553-737410.1371/journal.ppat.1002387https://doaj.org/article/a5a9fe012b994b9bade2cab122bdee482011-11-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22114560/?tool=EBIhttps://doaj.org/toc/1553-7366https://doaj.org/toc/1553-7374All gammaherpesviruses encode a major glycoprotein homologous to the Epstein-Barr virus gp350. These glycoproteins are often involved in cell binding, and some provide neutralization targets. However, the capacity of gammaherpesviruses for long-term transmission from immune hosts implies that in vivo neutralization is incomplete. In this study, we used Bovine Herpesvirus 4 (BoHV-4) to determine how its gp350 homolog--gp180--contributes to virus replication and neutralization. A lack of gp180 had no impact on the establishment and maintenance of BoHV-4 latency, but markedly sensitized virions to neutralization by immune sera. Antibody had greater access to gB, gH and gL on gp180-deficient virions, including neutralization epitopes. Gp180 appears to be highly O-glycosylated, and removing O-linked glycans from virions also sensitized them to neutralization. It therefore appeared that gp180 provides part of a glycan shield for otherwise vulnerable viral epitopes. Interestingly, this O-glycan shield could be exploited for neutralization by lectins and carbohydrate-specific antibody. The conservation of O-glycosylation sites in all gp350 homologs suggests that this is a general evasion mechanism that may also provide a therapeutic target.Bénédicte MachielsCéline LétéAntoine GuillaumeJan MastPhilip G StevensonAlain VanderplasschenLaurent GilletPublic Library of Science (PLoS)articleImmunologic diseases. AllergyRC581-607Biology (General)QH301-705.5ENPLoS Pathogens, Vol 7, Iss 11, p e1002387 (2011)
institution	DOAJ
collection	DOAJ
language	EN
topic	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
spellingShingle	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5 Bénédicte Machiels Céline Lété Antoine Guillaume Jan Mast Philip G Stevenson Alain Vanderplasschen Laurent Gillet Antibody evasion by a gammaherpesvirus O-glycan shield.
description	All gammaherpesviruses encode a major glycoprotein homologous to the Epstein-Barr virus gp350. These glycoproteins are often involved in cell binding, and some provide neutralization targets. However, the capacity of gammaherpesviruses for long-term transmission from immune hosts implies that in vivo neutralization is incomplete. In this study, we used Bovine Herpesvirus 4 (BoHV-4) to determine how its gp350 homolog--gp180--contributes to virus replication and neutralization. A lack of gp180 had no impact on the establishment and maintenance of BoHV-4 latency, but markedly sensitized virions to neutralization by immune sera. Antibody had greater access to gB, gH and gL on gp180-deficient virions, including neutralization epitopes. Gp180 appears to be highly O-glycosylated, and removing O-linked glycans from virions also sensitized them to neutralization. It therefore appeared that gp180 provides part of a glycan shield for otherwise vulnerable viral epitopes. Interestingly, this O-glycan shield could be exploited for neutralization by lectins and carbohydrate-specific antibody. The conservation of O-glycosylation sites in all gp350 homologs suggests that this is a general evasion mechanism that may also provide a therapeutic target.
format	article
author	Bénédicte Machiels Céline Lété Antoine Guillaume Jan Mast Philip G Stevenson Alain Vanderplasschen Laurent Gillet
author_facet	Bénédicte Machiels Céline Lété Antoine Guillaume Jan Mast Philip G Stevenson Alain Vanderplasschen Laurent Gillet
author_sort	Bénédicte Machiels
title	Antibody evasion by a gammaherpesvirus O-glycan shield.
title_short	Antibody evasion by a gammaherpesvirus O-glycan shield.
title_full	Antibody evasion by a gammaherpesvirus O-glycan shield.
title_fullStr	Antibody evasion by a gammaherpesvirus O-glycan shield.
title_full_unstemmed	Antibody evasion by a gammaherpesvirus O-glycan shield.
title_sort	antibody evasion by a gammaherpesvirus o-glycan shield.
publisher	Public Library of Science (PLoS)
publishDate	2011
url	https://doaj.org/article/a5a9fe012b994b9bade2cab122bdee48
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Antibody evasion by a gammaherpesvirus O-glycan shield.

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