Synthesis and processing of bovine herpesvirus-1 glycoprotein H.
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.
Baranowski
E
E
Department of Virology and Immunology, Faculty of Veterinary Medicine, University of Liège, Liège Sart Tilman, Belgium.
Dubuisson
J
J
van Drunen Little-van den Hurk
S
S
Babiuk
A L
AL
Michel
A
A
Pastoret
P P
PP
Thiry
E
E
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D006023:Glycoproteins / Q000096:biosynthesis* / Q000235:genetics / Q000378:metabolism; D007242:Herpesvirus 1, Bovine / Q000378:metabolism*; D008969:Molecular Sequence Data; D011499:Protein Processing, Post-Translational; D015531:Radioimmunoprecipitation Assay
D006023:Glycoproteins