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Mapping of 10 epitopes on bovine herpesvirus type 1 glycoproteins gl and glll

Identifieur interne : 004886 ( Main/Exploration ); précédent : 004885; suivant : 004887

Mapping of 10 epitopes on bovine herpesvirus type 1 glycoproteins gl and glll

Auteurs : David R. Fitzpatrick [Canada] ; Mark J. Redmondz [Canada] ; Sam K. Attah-Poku [Canada] ; Sylvia Van Drunen Littel-Van Den Hurk [Canada] ; Lorne A. Babiuk [Canada] ; Tim J. Zamb [Canada]

Source :

RBID : ISTEX:79AF8CBC3F54BAA69F559D914081F408629107A9

Abstract

In order to map some of the immunologically important sites on bovine herpesvirus type 1 (BHV-1), deleted, truncated, and hybrid forms of glycoproteins gl and gill were expressed in transfected murine LMTK− cells. The cells were tested for reactivity with a panel of 16 gl- or gill-specific monoclonal antibodies (MAbs) possessing conformation-independent antigen binding properties. This panel represented five epitopes on gl and five epitopes on gill. For gl, two epitopes were mapped between residues 68 and 119, one epitope was mapped between residues 370 and 440, one epitope was mapped to the vicinity of residue 487, and one epitope was mapped between residues 744 and 763. For gill, three epitopes were mapped between residues 22 and 150, one epitope was mapped between residues 140 and 240, and one epitope was mapped between residues 230 and 287. The location of the gl epitope in the vicinity of residue 487, which was recognized by a virus-neutralizing MAb, was verified by synthetic peptide binding studies. The epitope locations were consistent with proposed models for the structures of gl and gill, and comparable to some of the epitope locations reported for the homologous glycoproteins of herpes simplex virus type 1. The implications of these results for development of a subunit vaccine against BHV-1 are discussed.

Url:
DOI: 10.1016/0042-6822(90)90239-N


Affiliations:


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