Murine gammaherpesvirus-68 glycoprotein B presents a difficult neutralization target to monoclonal antibodies derived from infected mice

Gillet, Laurent, Gill, Michael B., Colaco, Susanna, Smith, Christopher M. and Stevenson, Philip G. (2006) Murine gammaherpesvirus-68 glycoprotein B presents a difficult neutralization target to monoclonal antibodies derived from infected mice. Journal of General Virology, 87 12: 3515-3527. doi:10.1099/vir.0.82313-0


Author Gillet, Laurent
Gill, Michael B.
Colaco, Susanna
Smith, Christopher M.
Stevenson, Philip G.
Title Murine gammaherpesvirus-68 glycoprotein B presents a difficult neutralization target to monoclonal antibodies derived from infected mice
Journal name Journal of General Virology   Check publisher's open access policy
ISSN 0022-1317
1465-2099
Publication date 2006-12-01
Year available 2006
Sub-type Article (original research)
DOI 10.1099/vir.0.82313-0
Open Access Status DOI
Volume 87
Issue 12
Start page 3515
End page 3527
Total pages 13
Place of publication London, United Kingdom
Publisher The Microbiology Society
Language eng
Abstract Persistent viruses disseminate from immune hosts. They must therefore resist neutralization by antibody. Murine gammaherpesvirus-68 (MHV-68) represents an accessible model with which to address how resistance to neutralization is achieved and how overcoming it might improve infection control. The MHV-68 glycoprotein B (gB), like that of other herpesviruses, is a virion protein that is essential for infectivity. As such, it presents a potential neutralization target. In order to test whether virus-induced antibodies reduce virion infectivity by binding to gB, monoclonal antibodies (mAbs) were derived from MHV-68-infected mice. gB-specific mAbs were common, but only an IgM specific for the gB N terminus reduced virion infectivity significantly. It inhibited MHV-68 entry into BHK-21 cells at a post-binding step that was linked closely to membrane fusion. Reducing the mAb to IgM monomers compromised neutralization severely, suggesting that a pentameric structure was crucial to its function. Antibody treatment never blocked BHK-21 cell infection completely and blocked the infection of NMuMG epithelial cells hardly at all. Virions saturated with antibody also remained infectious to mice. Thus, the MHV-68 gB presents at best a very difficult target for antibody-mediated neutralization.
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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