Reference : A mechanistic basis for potent, glycoprotein B-directed gammaherpesvirus neutralization.
Scientific journals : Article
Life sciences : Microbiology
A mechanistic basis for potent, glycoprotein B-directed gammaherpesvirus neutralization.
Glauser, Daniel L [> > > >]
Kratz, Anne*-Sophie [> > > >]
Gillet, Laurent mailto [Université de Liège - ULiège > > Immunologie et vaccinologie]
Stevenson, Philip G [> > > >]
Journal of General Virology (The)
Society for General Microbiology
Pt 9
Yes (verified by ORBi)
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.

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