Localization of Antigenic Sites at the Amino-terminus of Rinderpest Virus N Protein Using Deleted N Mutants and Monoclonal Antibody
Journal of Veterinary Science
;
: 167-173, 2003.
Article
in English
| WPRIM
| ID: wpr-105179
ABSTRACT
The nucleocapsid (N) protein of rinderpest virus (RPV) is highly conserved, immunogenic, and abundantly expressed during infection. Six antigenic sites (sites A, B, C, D, E and F), defined previously by a competitive binding assay using corresponding monoclonal antibodies (Mabs), have been further localized by immunoassays using deleted N mutants. Five different forms of RPV N protein, containing residues aa 1-79, aa 1-149, aa 1-421, aa 414-525 and aa 1-525, were expressed as glutathione S transferase (GST) fusion proteins (designated as GST-N1-79, GST-N1-149, GST-N1-421, GST-N414-525, and GST-N1-525, respectively) in E.coli BL21 cells. In ELISA using deleted N mutants, Mabs recognizing sites A, B, C, D and E reacted with 3 GST fusion proteins (GST-N1-149, GST-N1-421 and GST-N1-525), indicating that they are located at aa 80-149. Mab recognizing site F reacted with 4 GST fusion proteins (GST-N1-79, GST-N1-149, GST-N1-421 and GST-N1-525), indicating that site F is located at aa 1-79. Identification of the amino-terminal antigenic sites of the N protein would provide antigen basis for developing sensitive and specific diagnostic reagents for RPV, although it remains to be further investigated antigenic sites at the carboxyl-terminus.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Rinderpest virus
/
Viral Proteins
/
Vero Cells
/
Recombinant Proteins
/
Molecular Sequence Data
/
Base Sequence
/
Chlorocebus aethiops
/
Sequence Alignment
/
Amino Acid Sequence
/
Cloning, Molecular
Limits:
Animals
Language:
English
Journal:
Journal of Veterinary Science
Year:
2003
Type:
Article
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