Reference : A mechanistic basis for potent, glycoprotein B-directed gammaherpesvirus neutralization.
Scientific journals : Article
Life sciences : Microbiology
http://hdl.handle.net/2268/102550
A mechanistic basis for potent, glycoprotein B-directed gammaherpesvirus neutralization.
English
Glauser, Daniel L [> > > >]
Kratz, Anne*-Sophie [> > > >]
Gillet, Laurent mailto [Université de Liège - ULg > > Immunologie et vaccinologie]
Stevenson, Philip G [> > > >]
2011
Journal of General Virology (The)
Society for General Microbiology
92
Pt 9
2020-33
Yes (verified by ORBi)
International
0022-1317
1465-2099
London
United Kingdom
[en] Animals ; Antibodies, Monoclonal/immunology ; Antibodies, Neutralizing/immunology ; Antibodies, Viral/immunology ; Cell Line ; Epitopes/immunology ; Glycoproteins/immunology ; Mice ; Mice, Inbred BALB C ; Neutralization Tests ; Rhadinovirus/immunology ; Viral Structural Proteins/immunology
[en] Glycoprotein B (gB) is a conserved, essential component of gammaherpes virions and so potentially vulnerable to neutralization. However, few good gB-specific neutralizing antibodies have been identified. Here, we show that murid herpesvirus 4 is strongly neutralized by mAbs that recognize an epitope close to one of the gB fusion loops. Antibody binding did not stop gB interacting with its cellular ligands or initiating its fusion-associated conformation change, but did stop gB resolving stably to its post-fusion form, and so blocked membrane fusion to leave virions stranded in late endosomes. The conservation of gB makes this mechanism a possible general route to gammaherpesvirus neutralization.
http://hdl.handle.net/2268/102550
10.1099/vir.0.032177-0

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