ArticleThe Journal of general virology2006
Murine gammaherpesvirus-68 glycoprotein B presents a difficult neutralization target to monoclonal antibodies derived from infected mice.
Article in The Journal of general virology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed.
- Glycoproteins gM and gN are indispensable factors for rhesus macaque rhadinovirus replication and spread but can be reconstituted by KSHV chimeras.Journal of virology · 2025Article
- Viral FGARAT ORF75A promotes early events in lytic infection and gammaherpesvirus pathogenesis in mice.PLoS pathogens · 2018Article
- Deletion of Murid Herpesvirus 4 ORF63 Affects the Trafficking of Incoming Capsids toward the Nucleus.Journal of virology · 2015Article
- KSHV-TK is a tyrosine kinase that disrupts focal adhesions and induces Rho-mediated cell contraction.The EMBO journal · 2015Article
- Glycoprotein B cleavage is important for murid herpesvirus 4 to infect myeloid cells.Journal of virology · 2013Article
- Article
- Tiled microarray identification of novel viral transcript structures and distinct transcriptional profiles during two modes of productive murine gammaherpesvirus 68 infection.Journal of virology · 2012Article
- Article
- Antibody evasion by a gammaherpesvirus O-glycan shield.PLoS pathogens · 2011Article
- A mechanistic basis for potent, glycoprotein B-directed gammaherpesvirus neutralization.The Journal of general virology · 2011Article
- Vaccination with murid herpesvirus-4 glycoprotein B reduces viral lytic replication but does not induce detectable virion neutralization.The Journal of general virology · 2010Article
- A gammaherpesvirus complement regulatory protein promotes initiation of infection by activation of protein kinase Akt/PKB.PloS one · 2010Article
- Virus susceptibility of Chinese hamster ovary (CHO) cells and detection of viral contaminations by adventitious agent testing.Biotechnology and bioengineering · 2010Article
- Antibody limits in vivo murid herpesvirus-4 replication by IgG Fc receptor-dependent functions.The Journal of general virology · 2009Article
- Glycoprotein L sets the neutralization profile of murid herpesvirus 4.The Journal of general virology · 2009Article
- In vivo importance of heparan sulfate-binding glycoproteins for murid herpesvirus-4 infection.The Journal of general virology · 2009Article
- Lack of heparan sulfate expression in B-cell lines: implications for Kaposi's sarcoma-associated herpesvirus and murine gammaherpesvirus 68 infections.Journal of virology · 2008Article
- Article
- Article
- Glycoprotein B switches conformation during murid herpesvirus 4 entry.The Journal of general virology · 2008Article
Corrections and comments
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Authors and funding
5 authors.
Funding
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.
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