ORBi: van Drunen Littel-van den Hurk S. - 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.

Reference : Glycoprotein H (gII/gp108) and glycoprotein L form a functional complex which plays a ro...


	Document type :	Scientific journals : Article
	Discipline(s) :	Life sciences : Microbiology Life sciences : Veterinary medicine & animal health
	To cite this reference:	http://hdl.handle.net/2268/7740

Title :	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.
Language :	English
Author, co-author :	van Drunen Littel-van den Hurk, S. [> > > >]
	Khattar, S. [> > > >]
	Tikoo, S. K. [> > > >]
	Babiuk, L. A. [> > > >]
	Baranowski, E. [> > > >]
	Plainchamp, D. [> > > >]
	Thiry, Etienne [Université de Liège - ULg > Département des maladies infectieuses et parasitaires > Virologie, épidémiologie et pathologie des maladies virales >]
Publication date :	1996
Journal title :	Journal of General Virology (The)
Publisher :	Society for General Microbiology
Volume :	77 ( Pt 7)
Pages :	1515-20
Audience :	International
ISSN :	0022-1317
e-ISSN :	1465-2099
City :	London
Country :	United Kingdom
Keywords :	[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
Abstract :	[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.
Permalink :	http://hdl.handle.net/2268/7740

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