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Clinical and Diagnostic Laboratory Immunology, July 2004, p. 658-664, Vol. 11, No. 4
1071-412X/04/$08.00+0     DOI: 10.1128/CDLI.11.4.658-664.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Characterization of Immunodominant Linear B-Cell Epitopes on the Carboxy Terminus of the Rinderpest Virus Nucleocapsid Protein

Foreign Animal Disease Research Division, National Veterinary Research and Quarantine Service, Anyang, Kyounggi 430-824,¹ Research Institute of Veterinary Medicine/College of Veterinary Medicine, Chungbuk National University, Cheongju, Chungbuk 361-763, South Korea,² Department of Veterinary Diagnostic and Production Animal Medicine, College of Veterinary Medicine, Iowa State University, Ames, Iowa 50011³

Received 13 January 2004/ Returned for modification 9 March 2004/ Accepted 6 April 2004

The nucleocapsid (N) protein of rinderpest virus (RPV) is one of the most abundant and immunogenic viral proteins expressed during natural or experimental infection. To identify immunogenic epitopes on the N protein, different forms of RPV N protein, including the full-length protein (N_1-525), an amino-terminal construct (N_1-179), and a carboxy-terminal construct (N_414-496), were expressed in Escherichia coli as glutathione S-transferase (GST) fusion proteins. The antigenicity of each recombinant protein was evaluated by Western immunoblotting. All recombinants were recognized by hyperimmune RPV bovine antisera, indicating that immunoreactive epitopes may be present at both ends of the N protein. However, GST-N_414-496 was much more antigenic than GST-N_1-179 when tested with sera from vaccinated cattle, suggesting that an immunodominant or highly immunogenic epitope(s) may be located at the carboxy terminus of the N protein. Epitope mapping with overlapping peptides representing different regions of the carboxy terminus (amino acids 415 to 524) revealed three nonoverlapping antigenic sites in regions containing the residues ⁴⁴⁰VPQVRKETRASSR⁴⁵² (site 1), ⁴⁷⁹PEADTDPL⁴⁸⁶ (site 2), and ⁵²⁰DKDLL⁵²⁴ (site 3). Among these, antigenic site 2 showed the strongest reactivity with hyperimmune anti-RPV bovine sera in a peptide enzyme-linked immunosorbent assay but did not react with hyperimmune caprine sera raised against peste-des-petits-ruminants virus, which is antigenically closely related to RPV. Identification of an immunodominant linear antigenic site at the carboxy terminus of the N protein may provide an antigen basis for designing diagnostics specific for RPV.

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