Reference : Antibody evasion by a gammaherpesvirus o-glycan shield.
Scientific journals : Article
Life sciences : Microbiology
http://hdl.handle.net/2268/107116
Antibody evasion by a gammaherpesvirus o-glycan shield.
English
Machiels, Bénédicte mailto [Université de Liège - ULg > > Immunologie et vaccinologie]
Lété, Céline mailto [Université de Liège - ULg > > Immunologie et vaccinologie]
Guillaume, Antoine mailto [Université de Liège - ULg > > Immunologie et vaccinologie]
Mast, Jan [> > > >]
Stevenson, Philip G [> > > >]
Vanderplasschen, Alain mailto [Université de Liège - ULg > > Immunologie et vaccinologie]
Gillet, Laurent mailto [Université de Liège - ULg > > Immunologie et vaccinologie]
2011
PLoS Pathogens
Public Library of Science
7
11
e1002387
Yes (verified by ORBi)
International
1553-7366
1553-7374
San Francisco
CA
[en] 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.
http://hdl.handle.net/2268/107116
10.1371/journal.ppat.1002387

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