Reference : Synthesis and Processing of Bovine Herpesvirus-1 Glycoprotein H
Scientific journals : Article
Life sciences : Microbiology
Life sciences : Veterinary medicine & animal health
http://hdl.handle.net/2268/19396
Synthesis and Processing of Bovine Herpesvirus-1 Glycoprotein H
English
Baranowski, Eric [> > > >]
Dubuisson, Jean [> > > >]
van Drunen Little-van den Hurk, Sylvia [> > > >]
Babiuk, A. Lorne [> > > >]
Michel, Alain [> >]
Pastoret, Paul-Pierre [Université de Liège - ULg > Département des maladies infectieuses et parasitaires > Département des maladies infectieuses et parasitaires >]
Thiry, Etienne mailto [Université de Liège - ULg > Département des maladies infectieuses et parasitaires > Virologie, épidémiologie et pathologie des maladies virales >]
10-Jan-1995
Virology
206
1
651-4
Yes (verified by ORBi)
International
0042-6822
[en] The translation product of the bovine herpesvirus-1 (BHV-1) gH gene was identified and characterized. Synthetic peptides were used to generate specific antisera and a glycoprotein of 108K was precipitated by one of the antisera. Cross-immunoprecipitations with monoclonal antibodies to BHV-1 glycoprotein gp108 and the anti-gH peptide antiserum demonstrated that gp108 is the translation product of the gH open reading frame. Glycoprotein gH synthesis and intracellular processing was analyzed in infected Madin-Darby bovine kidney cells using anti-gp 108 monoclonal antibodies. Glycoprotein gH is expressed as a beta-gamma protein and could be detected by radioimmunoprecipitation as early as 2 hr postinfection. Cotranslational N-glycosylation of gH is essential for the recognition by monoclonal antibodies, suggesting that N-linked glycans are involved in protein folding or that they are targets for most of monoclonal antibodies used in this study.
http://hdl.handle.net/2268/19396

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