作者: J. A. L. de Turiso , E. Cortes , A. Ranz , J. Garcia , A. Sanz
DOI: 10.1099/0022-1317-72-10-2445
关键词: Molecular biology 、 Virology 、 Immunogenicity 、 Peptide sequence 、 Epitope 、 Capsid 、 Biology 、 Canine parvovirus 、 Neutralization 、 Monoclonal antibody 、 Fusion protein
摘要: In this report we describe the topological mapping of neutralizing domains canine parvovirus (CPV). We obtained 11 CPV-specific monoclonal antibodies (MAbs), six which are neutralizing. The reactivities were as determined by ELISA and Western blot (immunoblot) analysis. VP2, most abundant protein CPV capsid, seemed to contain all neutralization sites. Also, an almost full-length genomic clone was constructed in bacterial plasmid pUC18 enable expression proteins. All MAbs recognized recombinant VP2 when it expressed a free Escherichia coli but not fusion with glutathione-S-transferase. When two large fragments containing about 85% 67% C terminus expressed, no sites detected. proteins N linear determinants mapped, one between residues 1 10 other amino acids 23. peptide GQPAVRNERATGS 23, MAb 3C9, synthesized chemically checked for immunogenicity, being able induce activity. Although antibody response rabbits uniformly high, anti-CPV very variable. Protein from pCPVEx11, contains T cell epitope (peptide PKIFINLAKKKKAG) present VP1-specific region well B epitopes, be effective inducing virus neutralization.