J Gen Virol Try IJSEM Online
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

J Gen Virol 87 (2006), 1465-1475; DOI 10.1099/vir.0.81760-0

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Gill, M. B.
Right arrow Articles by Stevenson, P. G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Gill, M. B.
Right arrow Articles by Stevenson, P. G.
Agricola
Right arrow Articles by Gill, M. B.
Right arrow Articles by Stevenson, P. G.
© 2006 Society for General Microbiology

Murine gammaherpesvirus-68 glycoprotein H–glycoprotein L complex is a major target for neutralizing monoclonal antibodies

Michael B. Gill, Laurent Gillet, Susanna Colaco, Janet S. May, Brigitte D. de Lima and Philip G. Stevenson

Division of Virology, Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP, UK

Correspondence
Philip G. Stevenson
pgs27{at}cam.ac.uk

Herpesviruses characteristically persist in immune hosts as latent genomes, but to transmit infection they must reactivate and replicate lytically. The interaction between newly formed virions and pre-existing antibody is therefore likely to be a crucial determinant of viral fitness. Murine gammaherpesvirus-68 (MHV-68) behaves as a natural pathogen of conventional, inbred mice and consequently allows such interactions to be analysed experimentally in a relatively realistic setting. Here, monoclonal antibodies (mAbs) were derived from MHV-68-infected mice and all those recognizing infected-cell surfaces were tested for their capacity to neutralize MHV-68 virions. All of the neutralizing mAbs identified were specific for the viral glycoprotein H (gH)–gL heterodimer and required both gH and gL to reproduce their cognate epitopes. Based on antibody interference, there appeared to be two major neutralization epitopes on gH–gL. Analysis of a representative mAb indicated that it blocked infection at a post-binding step – either virion endocytosis or membrane fusion.




This article has been cited by other articles:


Home page
 J. Gen. Virol.Home page
D. E. Wright, S. Colaco, C. Colaco, and P. G. Stevenson
Antibody limits in vivo murid herpesvirus-4 replication by IgG Fc receptor-dependent functions
J. Gen. Virol., November 1, 2009; 90(11): 2592 - 2603.
[Abstract] [Full Text] [PDF]

Home page
 J. Gen. Virol.Home page
P. G. Stevenson, J. P. Simas, and S. Efstathiou
Immune control of mammalian gamma-herpesviruses: lessons from murid herpesvirus-4
J. Gen. Virol., October 1, 2009; 90(10): 2317 - 2330.
[Abstract] [Full Text] [PDF]

Home page
 J. Virol.Home page
A. E. Plate, J. Smajlovic, T. S. Jardetzky, and R. Longnecker
Functional Analysis of Glycoprotein L (gL) from Rhesus Lymphocryptovirus in Epstein-Barr Virus-Mediated Cell Fusion Indicates a Direct Role of gL in gB-Induced Membrane Fusion
J. Virol., August 1, 2009; 83(15): 7678 - 7689.
[Abstract] [Full Text] [PDF]

Home page
 J. Gen. Virol.Home page
L. Gillet, M. Alenquer, D. L. Glauser, S. Colaco, J. S. May, and P. G. Stevenson
Glycoprotein L sets the neutralization profile of murid herpesvirus 4
J. Gen. Virol., May 1, 2009; 90(5): 1202 - 1214.
[Abstract] [Full Text] [PDF]

Home page
 J. Gen. Virol.Home page
L. Gillet, J. S. May, and P. G. Stevenson
In vivo importance of heparan sulfate-binding glycoproteins for murid herpesvirus-4 infection
J. Gen. Virol., March 1, 2009; 90(3): 602 - 613.
[Abstract] [Full Text] [PDF]

Home page
 J. Virol.Home page
S. Hwang, T.-T. Wu, L. M. Tong, K. S. Kim, D. Martinez-Guzman, A. D. Colantonio, C. H. Uittenbogaart, and R. Sun
Persistent Gammaherpesvirus Replication and Dynamic Interaction with the Host In Vivo
J. Virol., December 15, 2008; 82(24): 12498 - 12509.
[Abstract] [Full Text] [PDF]

Home page
 J. Gen. Virol.Home page
L. Gillet, S. Colaco, and P. G. Stevenson
Glycoprotein B switches conformation during murid herpesvirus 4 entry
J. Gen. Virol., June 1, 2008; 89(6): 1352 - 1363.
[Abstract] [Full Text] [PDF]

Home page
 J. Immunol.Home page
B. Kayhan, E. J. Yager, K. Lanzer, T. Cookenham, Q. Jia, T.-T. Wu, D. L. Woodland, R. Sun, and M. A. Blackman
A Replication-Deficient Murine {gamma}-Herpesvirus Blocked in Late Viral Gene Expression Can Establish Latency and Elicit Protective Cellular Immunity
J. Immunol., December 15, 2007; 179(12): 8392 - 8402.
[Abstract] [Full Text] [PDF]

Home page
 J. Virol.Home page
L. Gillet and P. G. Stevenson
Evidence for a Multiprotein Gamma-2 Herpesvirus Entry Complex
J. Virol., December 1, 2007; 81(23): 13082 - 13091.
[Abstract] [Full Text] [PDF]

Home page
 J. Virol.Home page
L. Gillet, J. S. May, S. Colaco, and P. G. Stevenson
Glycoprotein L Disruption Reveals Two Functional Forms of the Murine Gammaherpesvirus 68 Glycoprotein H
J. Virol., January 1, 2007; 81(1): 280 - 291.
[Abstract] [Full Text] [PDF]

Home page
 J. Gen. Virol.Home page
L. Gillet, M. B. Gill, S. Colaco, C. M. Smith, and P. G. Stevenson
Murine gammaherpesvirus-68 glycoprotein B presents a difficult neutralization target to monoclonal antibodies derived from infected mice
J. Gen. Virol., December 1, 2006; 87(12): 3515 - 3527.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
INT J SYST EVOL MICROBIOL MICROBIOLOGY J GEN VIROL
J MED MICROBIOL ALL SGM JOURNALS
Copyright © 2006 by the Society for General Microbiology.