Characterization of Antigenic Sites on the Rinderpest Virus N Protein Uusing Monoclonal Antibodies.
- Author:
Kang Seuk CHOI
1
;
Jin Ju NAH
;
Young Joon KO
;
Cheong Up CHOI
;
Jae Hong KIM
;
Shien Young KANG
;
Yi Seok JOO
Author Information
1. National Veterinary Research and Quarantine service, Ministry of Agriculture and Forestry, 480 Anyang, Kyounggi 430-824, Korea. choiks@nvrqs.go.kr
- Publication Type:Original Article ; Research Support, Non-U.S. Gov't
- Keywords:
monoclonal antibody;
N protein;
rinderpest virus;
antigenicity
- MeSH:
Antibodies, Monoclonal/*immunology;
Antigens, Viral/chemistry/*immunology;
Binding, Competitive;
Enzyme-Linked Immunosorbent Assay;
Epitopes/immunology;
Nucleocapsid Proteins/chemistry/*immunology;
Rinderpest virus/*immunology
- From:Journal of Veterinary Science
2003;4(1):57-65
- CountryRepublic of Korea
- Language:English
-
Abstract:
The N protein of the rinderpest virus (RPV) was analyzed topologically and antigenically by using anti-N monoclonal antibodies (Mabs). Ten Mabs were raised against the N protein of the RPV. At least six non-overlapping antigenic sites (sites A-F) were delineated by competitive binding assays using biotinylated Mabs. Of them 5 sites (A, C, D, E and F) on the N protein were recognized by RPV-specific Mabs in ELISA and IFA while site B was recognized by Mabs reacting with both RPV and PPRV. Non- reciprocal competition was found among sites C, D and E. Recombinant RPV N protein after exposure to 0.2% SDS exhibited higher ELISA titers in all Mabs recognizing 6 sites. Four sites (A, B, E and F) on 2% SDS-treated N protein lost completely reactivity with Mabs while the remaining sites (C and D) on the protein retained their antigenicity to some degree. It indicates that two sites (C and D) were sequential. Six representative Mabs bound to each site exhibited competition with rinderpest antibodies in a blocking ELISA, indicating that the sites were actively involved in antigenicity in cattle.
