IDENTIFICATION AND PURIFICATION OF F11 FIMBRIAE ON AVIAN PATHOGENIC ESCHERICHIA COLI
2000
POURBAKHSH, S.A., RAZI VACCINE and SERUM RESEARCH INSTITUTE,TEHRAN, IRAN | GOUDARZI, H., RAZI VACCINE and SERUM RESEARCH INSTITUTE,TEHRAN, IRAN | KHODASHENAS, M., RAZI VACCINE and SERUM RESEARCH INSTITUTE,TEHRAN, IRAN | MADANI, R., RAZI VACCINE and SERUM RESEARCH INSTITUTE,TEHRAN, IRAN
A mannose-resistant hemagglutinating (MRHA) P or P-related fimbriae was purified from three E.coli isolates from chickens with colisepticemia. The polyclonal antiserum against the fimbriae was prepared in rabbits. Examination of the purified fimbriae by SDS-polyacrylamide gel electrophoresis (SDS-PAGE) demonstrated a major fimbriae subunit of approximately 18 kDa. This band was also reacted with anti-F11 serum on Western blotting. The antiserum against the avian P fimbriae strongly reacted with the major subunit of the homologous fimbriae and with F11 fimbriae on Western blotting. The first 21 N-terminal amino acid sequence of the major fimbrial subunit of the avian P fimbriae was identical to that of F11 fimbriae. The adhesive properties of the avian P fimbriae were similar to that of F11 fimbriae with regard to both MRHA of human erythrocytes and binding to the Gal-Gal class II receptor. These results indicate that these fimbriae on avian E.coli isolates are closely related to F11 fimbriae which are associated with E.coli isolated from human urinary tract infection.
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