Monoclonal antibodies to equine arteritis virus proteins identify the GL protein as a target for virus neutralization

• Published in: Journal of general virology Vol. 75; no. 9; pp. 2439 - 2444
• Main Authors: Deregt, Dirk, de Vries, Antoine A. F, Raamsman, Martin J. B, Elmgren, Lindsay D, Rottier, Peter J. M
• Format: Journal Article
• Language: English
• Published: Reading Soc General Microbiol 01.09.1994; Society for General Microbiology
• Subjects: Animals; Antibodies, Monoclonal; Antibodies, Viral; Arteritis Virus, Equine - immunology; Biological and medical sciences; Cell Line; Cricetinae; Electrophoresis, Polyacrylamide Gel; Fundamental and applied biological sciences. Psychology; GTP-Binding Proteins - analysis; GTP-Binding Proteins - immunology; Hybridomas; Kidney; Mice; Mice, Inbred BALB C - immunology; Microbiology; Neutralization Tests; Recombinant Proteins - biosynthesis; Recombinant Proteins - immunology; Recombinant Proteins - isolation & purification; Recombination, Genetic; Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains; Vaccinia virus; Viral Structural Proteins - biosynthesis; Viral Structural Proteins - immunology; Viral Structural Proteins - isolation & purification; Virology; Pestivirus; Virus; Proteins; Antigenic determinant; Togaviridae; Hybridoma; Equine arteritis virus; Monoclonal antibody; Virus envelope; Neutralization
• ISSN: 0022-1317; 1465-2099
• DOI: 10.1099/0022-1317-75-9-2439

1 Animal Diseases Research Institute, Agriculture Canada, P.O. Box 640, Lethbridge, Alberta, Canada T1J 3Z4 and 2 Institute of Virology, Department of Infectious Diseases and Immunology, Veterinary Faculty, Utrecht University, Yalelaan 1, 3584 CL Utrecht, The Netherlands Monoclonal antibodies (MAbs) to equine arteritis virus (EAV) proteins were produced and characterized. The protein specificities of eight MAbs were determined definitively by immunoprecipitation of EAV proteins expressed from vaccinia virus recombinants (VVRs). Included were two new VVRs produced for this study, expressing the M and the G L proteins, respectively. Three MAbs were determined to be N-specific and five MAbs recognized the G L protein. One G L -specific MAb, 17F5, of the IgA class, efficiently neutralized EAV infectivity. In competitive binding assays (CBAs), the N-specific MAbs defined a single antigenic domain on this protein. Four G L -specific MAbs, including MAb 17F5, demonstrated strong reciprocal competition in binding to the G L protein but differed in their virus-neutralizing ability. Thus the antigenic domain defined by these MAbs is probably composed of overlapping or closely adjacent epitopes. The fifth G L -specific MAb, a non-neutralizing antibody, may define an epitope adjacent to this antigenic domain as reciprocal CBAs demonstrated lower competition. Received 27 September 1993; accepted 14 March 1994.