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Clinical and Diagnostic Laboratory Immunology, January 2001, p. 44-51, Vol. 8, No. 1
1071-412X/01/$04.00+0   DOI: 10.1128/CDLI.8.1.44-51.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Monoclonal Antibodies to Conformational Epitopes of the Surface Glycoprotein of Caprine Arthritis-Encephalitis Virus: Potential Application to Competitive-Inhibition Enzyme-Linked Immunosorbent Assay for Detecting Antibodies in Goat Sera

Fuat Özyörük,1 William P. Cheevers,1 Gordon A. Hullinger,1 Travis C. McGuire,1 Melinda Hutton,1 and Donald P. Knowles1,2,*

Department of Veterinary Microbiology and Pathology, Washington State University, Pullman, Washington 99164-7040,1 and Animal Disease Research Unit, Agricultural Research Service, U.S. Department of Agriculture, Pullman, Washington 99164-70302

Received 28 July 2000/Returned for modification 2 October 2000/Accepted 17 October 2000

Four immunoglobulin G1 monoclonal antibodies (MAbs) to the gp135 surface envelope glycoprotein (SU) of the 79-63 isolate of caprine arthritis-encephalitis virus (CAEV), referred to as CAEV-63, were characterized and evaluated for their ability to compete with antibody from CAEV-infected goats. Three murine MAbs (MAbs GPB16A, 29A, and 74A) and one caprine MAb (MAb F7-299) were examined. All MAbs reacted in nitrocellulose dot blots with native CAEV-63 SU purified by MAb F7-299 affinity chromatography, whereas none reacted with denatured and reduced SU. All MAbs reacted in Western blots with purified CAEV-63 SU or the SU component of whole-virus lysate following denaturation in the absence of reducing agent, indicating that intramolecular disulfide bonding was essential for epitope integrity. Peptide-N-glycosidase F digestion of SU abolished the reactivities of MAbs 74A and F7-299, whereas treatment of SU with N-acetylneuraminate glycohydrolase (sialidase A) under nonreducing conditions enhanced the reactivities of all MAbs as well as polyclonal goat sera. MAbs 29A and F7-299 were cross-reactive with the SU of an independent strain of CAEV (CAEV-Co). By enzyme-linked immunosorbent assay (ELISA), the reactivities of horseradish peroxidase (HRP)-conjugated MAbs 16A and 29A with homologous CAEV-63 SU were <10% of that of HRP-conjugated MAb 74A. The reactivity of HRP-conjugated MAb 74A was blocked by sera from goats immunized with CAEV-63 SU or infected with CAEV-63. The reactivity of MAb 74A was also blocked by sera from goats infected with a CAEV-Co molecular clone, although MAb 74A did not react with CAEV-Co SU in Western blots. Thus, goats infected with either CAEV-63 or CAEV-Co make antibodies that inhibit binding of MAb 74A to CAEV-63 SU. A competitive-inhibition ELISA based on displacement of MAb 74A reactivity has potential applicability for the serologic diagnosis of CAEV infection.

* Corresponding author. Mailing address: Animal Disease Research Unit, ARS-USDA, Washington State University, Pullman, WA 99164-7030. Phone: (509) 335-6022. Fax: (509) 335-8328. E-mail: dknowles{at}vetmed.wsu.edu.

Clinical and Diagnostic Laboratory Immunology, January 2001, p. 44-51, Vol. 8, No. 1
1071-412X/01/$04.00+0   DOI: 10.1128/CDLI.8.1.44-51.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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