Production and evaluation of monoclonal antibodies directed against the K88 fimbrial adhesin produced by Escherichia coli enterotoxigenic for piglets

Autor: C.J. Thorns, J.A. Morris, C.D.H. Boarer
Rok vydání: 1987
Předmět:
Zdroj: Research in Veterinary Science. 43:233-238
ISSN: 0034-5288
DOI: 10.1016/s0034-5288(18)30779-3
Popis: Fifty murine monoclonal antibodies were produced against a purified preparation of K88ab antigen. Two monoclonal antibodies were selected for further studies together with a monoclonal antibody directed against the c region of K88 (5CA3). Monoclonal antibody K88–13 bound to all K88 + Escherichia coli examined, whereas K88–18 and 5CA3 bound to K88ab + and K88ac + strains, respectively. The monoclonal antibodies failed to react with K88 + E coli grown at 18°C or with K88 − E coli grown at 37°C or 18°C. Binding of monoclonal antibody K88–13 to K88 antigen was blocked by OK antisera to G7 (O8:K87 K88ab) and Abbotstown (O149:K91 K88ac), whereas absorbed antisera to K88b, c and d had no effect. Monoclonal K88–18 was inhibited by OK G7 antiserum and absorbed antiserum to K88b. One hundred and forty-nine strains of K88 + E coli representing seven somatic O groups were agglutinated by antibody K88–13; 142 of these, from at least six somatic O groups were agglutinated by 5CA3 and the remainder by K88–18. Monoclonal antibody K88–13 bound to cryostat sections of ileum from piglets infected with E coli strains Abbotstown and G7. K88–18 and 5CA3 bound only to sections from piglets infected with G7 and Abbotstown strains, respectively. It is concluded that monoclonal antibody K88–13 recognises an epitope on the a region of K88 while monoclonal antibody K88–18 is directed towards the b region. These monoclonal antibodies together with 5CA3 can be used to routinely identify K88 + E coli isolates.
Databáze: OpenAIRE