Virion endocytosis is a major target for Murid Herpesvirus-4 neutralization

Glauser, Daniel L., Gillet, Laurent and Stevenson, Philip G. (2012) Virion endocytosis is a major target for Murid Herpesvirus-4 neutralization. Journal of General Virology, 93 6: 1316-1327. doi:10.1099/vir.0.040790-0

Author Glauser, Daniel L.
Gillet, Laurent
Stevenson, Philip G.
Title Virion endocytosis is a major target for Murid Herpesvirus-4 neutralization
Journal name Journal of General Virology   Check publisher's open access policy
ISSN 0022-1317
Publication date 2012-06
Year available 2012
Sub-type Article (original research)
DOI 10.1099/vir.0.040790-0
Open Access Status DOI
Volume 93
Issue 6
Start page 1316
End page 1327
Total pages 12
Place of publication Reading, Berks, United Kingdom
Publisher Society for General Microbiology
Collection year 2012
Language eng
Formatted abstract
Herpesviruses consistently transmit from immunocompetent carriers, implying that their neutralization is hard to achieve. Murid herpesvirus-4 (MuHV-4) exploits host IgG Fc receptors to bypass blocks to cell binding, and pH-dependent protein conformation changes to unveil its fusion machinery only after endocytosis. Nevertheless, neutralization remains possible by targeting the virion glycoprotein H (gH)-gL heterodimer, and the neutralizing antibody responses of MuHV- 4 carriers are improved by boosting with recombinant gH-gL. We analysed here how gH-gLdirected neutralization works. The MuHV-4 gH-gL binds to heparan sulfate. However, most gH- gL-specific neutralizing antibodies did not block this interaction; neither did they act directly on fusion. Instead, they blocked virion endocytosis and transport to the late endosomes, where membrane fusion normally occurs. The poor endocytosis of gH-gL-neutralized virions was recapitulated precisely by virions genetically lacking gL. Therefore, driving virion uptake appears to be an important function of gH-gL that provides a major target for antibody-mediated neutralization.
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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Created: Mon, 23 Mar 2015, 11:14:01 EST by Mrs Louise Nimwegen on behalf of School of Chemistry & Molecular Biosciences