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| Subject Categories: Microbiology & Pathogens | Molecular Biology of Disease |
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| The EMBO Journal
(2007) 26, 5131–5142, doi:10.1038/sj.emboj.7601925 Published online 22 November 2007 |
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| Antibody evasion by the N terminus of murid herpesvirus-4 glycoprotein B EMBO Open |
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| Laurent Gillet1 and Philip G Stevenson |
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Division of Virology, Department of Pathology, University of Cambridge, Cambridge, UK To whom correspondence should be addressed Philip G Stevenson, Division of Virology, Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP, UK. Tel.: +44 1223 336921; Fax: +44 1223 336926; E-mail: pgs27@cam.ac.uk 1 Present address: Immunology-Vaccinology, Faculty of Veterinary Medicine, University of Liège, Liège, Belgium Received 20 August 2007; Accepted 19 October 2007; Published online 22 November 2007. |
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| Abstract |
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| 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. |
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| Keywords: antibody, glycoprotein, immune evasion, virus |
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