Abstract
A major Mycoplasma gallisepticum polypeptide of 64 kDa (p64) was characterized using two distinct monoclonal antibodies (MAbs), MAb KI produced in our laboratory and MAb MyG 001 produced by Avakian & Ley (1993). The p64 antigen was shown to be a lipoprotein in a radioimmunoprecipitation assay using [(3)H] palmitic acid-labelled M. gallisepticum cultures. The two MAbs inhibited the growth of M. gallisepticum in liquid medium and reacted to two distinct epitopes on the same p64 antigen in competitive enzyme-linked immunosorbent and chemiluminescence Western immunoblot assays. MAb Kl inhibited haemagglutination of chicken and turkey erythrocytes whereas MAb MyG 001 did not. The results of our study indicate that p64 has two distinct epitopes involved in haemagglutination and growth inhibition of M. gallisepticum. MAb Kl also inhibited the attachment of the mycoplasma to TLT lymphoblastoid chicken B cell line, suggesting that p64 is a cytadhesin.
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