Reference : Glycoprotein H (gII/gp108) and glycoprotein L form a functional complex which plays a...
Scientific journals : Article
Life sciences : Microbiology
Life sciences : Veterinary medicine & animal health
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.
van Drunen Littel-van den Hurk, S. [> > > >]
Khattar, S. [> > > >]
Tikoo, S. K. [> > > >]
Babiuk, L. A. [> > > >]
Baranowski, E. [> > > >]
Plainchamp, D. [> > > >]
Thiry, Etienne mailto [Université de Liège - ULg > Département des maladies infectieuses et parasitaires > Virologie, épidémiologie et pathologie des maladies virales >]
Journal of General Virology (The)
Society for General Microbiology
77 ( Pt 7)
Yes (verified by ORBi)
United Kingdom
[en] Amino Acid Sequence ; Animals ; Antibodies, Viral/immunology ; Cattle ; Cell Line ; Herpesvirus 1, Bovine/immunology/pathogenicity ; Humans ; Molecular Sequence Data ; Rabbits ; Viral Proteins/immunology/isolation & purification/metabolism/physiology
[en] 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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