Antibody evasion by the N terminus of murid herpesvirus-4 glycoprotein B

Gillet, Laurent and Stevenson, Philip G. (2007) Antibody evasion by the N terminus of murid herpesvirus-4 glycoprotein B. EMBO Journal, 26 5131-5142. doi:10.1038/sj.emboj.7601925

Author Gillet, Laurent
Stevenson, Philip G.
Title Antibody evasion by the N terminus of murid herpesvirus-4 glycoprotein B
Journal name EMBO Journal   Check publisher's open access policy
ISSN 0261-4189
Publication date 2007-12-12
Year available 2007
Sub-type Article (original research)
DOI 10.1038/sj.emboj.7601925
Open Access Status DOI
Volume 26
Start page 5131
End page 5142
Total pages 12
Place of publication Chichester, West Sussex, United Kingdom
Publisher Wiley-Blackwell Publishing
Language eng
Abstract Herpesviruses characteristically transmit infection from immune hosts. Although their success in escaping neutralization by pre-formed antibody is indisputable, the underlying molecular mechanisms remain largely unknown. Glycoprotein B (gB) is the most conserved component of the herpesvirus entry machinery and its N terminus (gB-NT) is a common neutralization target. We used murid herpesvirus-4 to determine how gB-NT contributes to the virus-antibody interaction. Deleting gB-NT had no obvious impact on virus replication, but paradoxically increased virion neutralization by immune sera. This reflected greater antibody access to neutralization epitopes on gH/gL, with which gB was associated. gB-NT itself was variably protected against antibody by O-linked glycans; on virions from epithelial cells it was protected almost completely. gB-NT therefore provides a protective and largely protected cover for a vulnerable part of gH/gL. The conservation of predicted glycosylation sites in other mammalian herpesvirus gB-NTs suggests that this evasion mechanism is widespread. Interestingly, the gB-NT glycans that blocked antibody binding could be targeted for neutralization instead by a lectin, suggesting a means of therapeutic counterattack.
Keyword Antibody
Immune evasion
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 22 times in Thomson Reuters Web of Science Article | Citations
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