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PLoS Pathog. 2011 Nov;7(11):e1002387. doi: 10.1371/journal.ppat.1002387. Epub 2011 Nov 17.

Antibody evasion by a gammaherpesvirus O-glycan shield.

Author information

1
Immunology-Vaccinology B43b, Department of Infectious and Parasitic Diseases B43b, Faculty of Veterinary Medicine, University of Liège, Liège, Belgium.

Abstract

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.

PMID:
22114560
PMCID:
PMC3219721
DOI:
10.1371/journal.ppat.1002387
[Indexed for MEDLINE]
Free PMC Article
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