Evidence for a multiprotein gamma-2 herpesvirus entry complex

Gillet, Laurent and Stevenson, Philip G. (2007) Evidence for a multiprotein gamma-2 herpesvirus entry complex. Journal of Virology, 81 23: 13082-13091. doi:10.1128/JVI.01141-07

Author Gillet, Laurent
Stevenson, Philip G.
Title Evidence for a multiprotein gamma-2 herpesvirus entry complex
Journal name Journal of Virology   Check publisher's open access policy
ISSN 0022-538X
Publication date 2007-12-01
Year available 2007
Sub-type Article (original research)
DOI 10.1128/JVI.01141-07
Open Access Status DOI
Volume 81
Issue 23
Start page 13082
End page 13091
Total pages 10
Place of publication Washington, DC, United States
Publisher American Society for Microbiology
Language eng
Formatted abstract
Herpesviruses use multiple virion glycoproteins to enter cells. How these work together is not well understood: some may act separately or they may form a single complex. Murine gammaherpesvirus 68 (MHV-68) gB, gH, gL, and gp150 all participate in entry. gB and gL are involved in binding, gB and gH are conserved fusion proteins, and gp150 inhibits cell binding until glycosaminoglycans are engaged. Here we show that a gH-specific antibody coprecipitates gB and thus that gH and gB are associated in the virion membrane. A gH/gL-specific antibody also coprecipitated gB, implying a tripartite complex of gL/gH/gB, although the gH/gB association did not require gL. The association was also independent of gp150, and gp150 was not demonstrably bound to gB or gH. However, gp150 incorporation into virions was partly gL dependent, suggesting that it too contributes to a single entry complex. gp150 and gL gp150 mutants bound better than the wild type to B cells and readily colonized B cells in vivo. Thus, gp150 and gL appear to be epithelial cell-adapted accessories of a core gB/gH entry complex. The cell binding revealed by gp150 disruption did not require gL and therefore seemed most likely to involve gB.
Keyword Virology
Q-Index Code C1
Q-Index Status Provisional Code
Grant ID G9800943
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Chemistry and Molecular Biosciences
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 23 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 23 times in Scopus Article | Citations
Google Scholar Search Google Scholar
Created: Wed, 21 May 2014, 22:33:22 EST by System User on behalf of Scholarly Communication and Digitisation Service