Antibody Evasion by a Gammaherpesvirus O-Glycan Shield

Machiels, Benedicte, Lete, Celine, Guillaume, Antoine, Mast, Jan, Stevenson, Philip G., Vanderplasschen, Alain and Gillet, Laurent (2011) Antibody Evasion by a Gammaherpesvirus O-Glycan Shield. PLoS Pathogens, 7 11: e1002387-e1002387. doi:10.1371/journal.ppat.1002387

Author Machiels, Benedicte
Lete, Celine
Guillaume, Antoine
Mast, Jan
Stevenson, Philip G.
Vanderplasschen, Alain
Gillet, Laurent
Title Antibody Evasion by a Gammaherpesvirus O-Glycan Shield
Journal name PLoS Pathogens   Check publisher's open access policy
ISSN 1553-7366
Publication date 2011-11
Year available 2011
Sub-type Article (original research)
DOI 10.1371/journal.ppat.1002387
Open Access Status DOI
Volume 7
Issue 11
Start page e1002387
End page e1002387
Total pages 15
Place of publication San Francisco, CA United States
Publisher Public Library of Science
Collection year 2011
Language eng
Formatted 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.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Chemistry and Molecular Biosciences
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Citation counts: TR Web of Science Citation Count  Cited 15 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 16 times in Scopus Article | Citations
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Created: Mon, 23 Mar 2015, 10:48:40 EST by Mrs Louise Nimwegen on behalf of School of Chemistry & Molecular Biosciences