M467 - MURINE IGA MYELOMA PROTEIN THAT BINDS A BACTERIAL PROTEIN .1. RECOGNITION OF COMMON ANTIGENIC DETERMINANTS ON SALMONELLA-FLAGELLINS

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  • 1 January 1979
    • journal article
    • research article
    • Vol. 123  (4) , 1715-1720
Abstract
The binding of M467, an Ig[immunoglobulin]A murine myeloma protein, to flagellin from 7 spp. of Salmonella [S. milwaukee, S. adelaide, S. mississippi, S. typhimurium, S. anatum, S. donna and S. greenside] was studied. M467 reacted with antigenic determinants that were common to all the flagellins studied. These determinants were not related to serotypic antigens. EM of unreduced M467 showed a variety of polymeric species bound to flagella in a manner that could produce immobilization as well as agglutination and precipitation through cross-linking of antigenic determinants. Immunodiffusion in agar gel revealed that M467 was recognizing more than 1 group of peptide determinants on the flagellins studied. Passive hemagglutination inhibition and a solid phase radioimmunoassay provided evidence that there were differences in binding activities between M467 and the various Salmonella flagellins studied. M467 is binding more than 1 specific group of antigenic peptide determinants on flagellin molecules. Flagellin from 4 of the 7 spp. of Salmonella studied were deficient in 1 or more of these determinants.