Glycoprotein H (gII/gp108) and glycoprotein L form a functional complex which plays a role in penetration, but not in attachment, of bovine herpesvirus 1
1996
van Drunen Littel-van den Hurk, Sylvia | Khattar, Sunil | Tikoo, Suresh K. | Babiuk, Lorne A. | Baranowski, Eric | Plainchamp, Dominique | Thiry, Etienne | University of Saskatchewan [Saskatoon, Canada] (U of S) | Université de Liège = University of Liège = Universiteit van Luik = Universität Lüttich (ULiège) | GlaxoSmithKline | National Science and Engineering, Council and Medical Research Council of Canada
International audience
显示更多 [+] 显示较少 [-]英语. The glycoproteins of bovine herpesvirus 1 (BHV-1) play important roles in the interactions between virions and target cells. A 108 kDa glycoprotein, designated gII or gp 108, has been identified by two different panels of monoclonal antibodies. The gII- and gp 108-specific monoclonal antibodies were shown to react with the same protein, which was identified by N-terminal sequencing as the homologue of herpes simplex virus type 1 (HSV-1) gH. When BHV-1 gH was purified by immunoadsorbent chromatography, gL was co-purified. The gH-gL complex induced the production of antibodies that neutralized virus infectivity and inhibited virus penetration. Affinity-purified gH-gL did prevent penetration, but not attachment of BHV-1, which suggests that the gH-gL complex is essential for penetration of BHV-1 into susceptible cells.
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