Characterization of Antigenic Sites on the Rinderpest Virus N Protein Uusing Monoclonal Antibodies
Journal of Veterinary Science
;
: 57-65, 2003.
Article
in English
| WPRIM
| ID: wpr-122777
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.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Rinderpest virus
/
Binding, Competitive
/
Enzyme-Linked Immunosorbent Assay
/
Nucleocapsid Proteins
/
Antibodies, Monoclonal
/
Epitopes
/
Antigens, Viral
Language:
English
Journal:
Journal of Veterinary Science
Year:
2003
Type:
Article
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