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Journal of Virology, December 2007, p. 13082-13091, Vol. 81, No. 23
0022-538X/07/$08.00+0     doi:10.1128/JVI.01141-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Evidence for a Multiprotein Gamma-2 Herpesvirus Entry Complex{triangledown}

Laurent Gillet and Philip G. Stevenson*

Division of Virology, Department of Pathology, University of Cambridge, Cambridge, United Kingdom

Received 25 May 2007/ Accepted 17 September 2007

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.

* Corresponding author. Mailing address: Division of Virology, Department of Pathology, Tennis Court Road, Cambridge CB2 1QP, United Kingdom. Phone: 44-1223-336921. Fax: 44-1223-336926. E-mail: pgs27{at}cam.ac.uk

{triangledown} Published ahead of print on 26 September 2007.

Journal of Virology, December 2007, p. 13082-13091, Vol. 81, No. 23
0022-538X/07/$08.00+0     doi:10.1128/JVI.01141-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Gianni, T., Amasio, M., Campadelli-Fiume, G. (2009). Herpes Simplex Virus gD Forms Distinct Complexes with Fusion Executors gB and gH/gL in Part through the C-terminal Profusion Domain. J. Biol. Chem. 284: 17370-17382 [Abstract] [Full Text]  
  • Gill, M. B., Wright, D. E., Smith, C. M., May, J. S., Stevenson, P. G. (2009). Murid herpesvirus-4 lacking thymidine kinase reveals route-dependent requirements for host colonization. J. Gen. Virol. 90: 1461-1470 [Abstract] [Full Text]  
  • Gillet, L., Alenquer, M., Glauser, D. L., Colaco, S., May, J. S., Stevenson, P. G. (2009). Glycoprotein L sets the neutralization profile of murid herpesvirus 4. J. Gen. Virol. 90: 1202-1214 [Abstract] [Full Text]  
  • Gillet, L., May, J. S., Stevenson, P. G. (2009). In vivo importance of heparan sulfate-binding glycoproteins for murid herpesvirus-4 infection. J. Gen. Virol. 90: 602-613 [Abstract] [Full Text]  
  • Gillet, L., Colaco, S., Stevenson, P. G. (2008). Glycoprotein B switches conformation during murid herpesvirus 4 entry. J. Gen. Virol. 89: 1352-1363 [Abstract] [Full Text]  


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