The pore-forming proteins porins isolated from Yersinia pseudotuberculosis and Y. enterocolitica outer membranes and purified were found, by means of enzyme-linked immunosorbent assays, to be genus-specific antigens. Antiporin antibodies were detected in rabbit antisera to the isolated proteins as well as to total outer membrane proteins and whole bacterial cells. Enzyme-linked immunosorbent and immunoblotting assays demonstrated an antigenic relatedness of porins from five Yersinia species.
Key Words: Yersinia porins; antigenic relatedness; enzyme-linked irnmunosorbent assaysThe pore-forming proteins (porins) present in the outer membrane of gram-negative bacteria have pores allowing for transmembrane transfer of hydrophilic substances [8], and some also serve as receptors for bacteriophages [8]. Being among the major surface antigens of bacterial ceils, porins play an important role in the pathogenesis of infection by promoting adhesion of bacteria to (and possibly their invasion into) host cells [3] and affecting the immune response [5,9].Recent years have witnessed mounting interest in the immunochemical and immunobiological properties of outer membranes proteins, including porins, found in gram-negative bacteria. Porins from several members of the family Enterobacteriaceae have been shown to be antigenically related [6,13], and variations in biological activity among surface epitopes of outer membrane proteins have been reported [16]. However, information on the antigenic structures of porins in the genus Yersinia is scarce [2,10].Identification of antigenically related surface components on the outer cell membrane within Enterobacteriaceae genera may provide a basis for the
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