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Purification of Cross‐Reacting Protein Antigen Shared by Yersinia enterocolitica and Other Gram‐Negative Bacteria with Monoclonal Antibody
Author(s) -
Yamaguchi Hiroyuki,
Taguchi Haruhiko,
Katura Takuya,
Kumada Junko,
Uekusa Takeyuki,
Ogata Sachio
Publication year - 1989
Publication title -
microbiology and immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.664
H-Index - 70
eISSN - 1348-0421
pISSN - 0385-5600
DOI - 10.1111/j.1348-0421.1989.tb02018.x
Subject(s) - yersinia enterocolitica , microbiology and biotechnology , biology , monoclonal antibody , antigen , antiserum , epitope , enterobacteriaceae , shigella flexneri , yersinia , escherichia coli , serratia marcescens , antibody , bacteria , biochemistry , genetics , gene , immunology
A monoclonal antibody against the Yersinia enterocolitica 60‐kilodalton (kDa) antigen, designated cross‐reacting protein antigen (CRPA), was obtained by cell fusion. The CRPA common to gram‐negative bacteria was purified from Y. enterocolitica by the affinity chromatography with the monoclonal antibody (IgGl) thus obtained. The purified CRPA showed a single band of 60 kDa in SDS‐polyacrylamide gel electrophoresis (SDS‐PAGE), and reacted with rabbit antisera against Y. enterocolitica, Vibrio cholerae, Escherichia coli, Pseudomonas aeruginosa , and Shigella sonnei in Western blot analysis. The monoclonal antibody, however, reacted with a 60 kDa peptide from Y. enterocolitica , but not with the antigens from other gram‐negative bacteria such as V. cholerae, E. coli, S. sonnei, Salmonella enteritidis, Serratia marcescens, Klebsiella pneumoniae, Proteus mirabilis , and P. aeruginosa . The results suggested that both species‐specific and cross‐reactive epitopes were present on a CRPA molecule.