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.
Department of Virology and Immunology, Faculty of Veterinary Medicine, University of Liège, Liège Sart Tilman, Belgium.
E
E
Baranowski
J
J
Dubuisson
S
S
van Drunen Little-van den Hurk
A L
AL
Babiuk
A
A
Michel
P P
PP
Pastoret
E
E
Thiry
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