Murine gammaherpesvirus-68 glycoprotein H-glycoprotein L complex is a major target for neutralizing monoclonal antibodies

Gill, Michael B., Gillet, Laurent, Colaco, Susanna, May, Janet S., de Lima, Brigitte D. and Stevenson, Philip G. (2006) Murine gammaherpesvirus-68 glycoprotein H-glycoprotein L complex is a major target for neutralizing monoclonal antibodies. Journal of General Virology, 87 6: 1465-1475. doi:10.1099/vir.0.81760-0


Author Gill, Michael B.
Gillet, Laurent
Colaco, Susanna
May, Janet S.
de Lima, Brigitte D.
Stevenson, Philip G.
Title Murine gammaherpesvirus-68 glycoprotein H-glycoprotein L complex is a major target for neutralizing monoclonal antibodies
Journal name Journal of General Virology   Check publisher's open access policy
ISSN 0022-1317
1465-2099
Publication date 2006-06-01
Year available 2006
Sub-type Article (original research)
DOI 10.1099/vir.0.81760-0
Open Access Status
Volume 87
Issue 6
Start page 1465
End page 1475
Total pages 11
Place of publication London, United Kingdom
Publisher The Microbiology Society
Language eng
Abstract Herpesviruses characteristically persist in immune hosts as latent genomes, but to transmit infection they must reactivate and replicate lytically. The interaction between newly formed virions and pre-existing antibody is therefore likely to be a crucial determinant of viral fitness. Murine gammaherpesvirus-68 (MHV-68) behaves as a natural pathogen of conventional, inbred mice and consequently allows such interactions to be analysed experimentally in a relatively realistic setting. Here, monoclonal antibodies (mAbs) were derived from MHV-68-infected mice and all those recognizing infected-cell surfaces were tested for their capacity to neutralize MHV-68 virions. All of the neutralizing mAbs identified were specific for the viral glycoprotein H (gH)-gL heterodimer and required both gH and gL to reproduce their cognate epitopes. Based on antibody interference, there appeared to be two major neutralization epitopes on gH-gL. Analysis of a representative mAb indicated that it blocked infection at a post-binding step - either virion endocytosis or membrane fusion.
Keyword Biotechnology & Applied Microbiology
Virology
Biotechnology & Applied Microbiology
Virology
BIOTECHNOLOGY & APPLIED MICROBIOLOGY
VIROLOGY
Q-Index Code C1
Q-Index Status Provisional Code
Grant ID G0400427
GR076956MA
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Chemistry and Molecular Biosciences
 
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