Characterization of hemagglutinating components on the Anaplasma marginale initial body surface and identification of possible adhesins.

摘要: Interaction of Anaplasma marginale initial bodies with the bovine erythrocyte surface was examined by a direct hemagglutination assay. Purified were shown to specifically hemagglutinate erythrocytes but not from nonhost animal species. Hemagglutination inhibited treatment purified trypsin, alpha-chymotrypsin, or proteinase K neuraminidase sodium periodate. Treatment alpha-chymotrypsin partially treated cells bodies. In contrast, no inhibition occurred after phospholipases, periodate when monosaccharides and disaccharides used as potential competitive inhibitors. Thus, body receptor is probably protein, whereas may comprise both protein carbohydrate. unaffected monoclonal polyclonal antibodies raised against A. 31-kDa (MSP4) major polypeptide non-A. proteins antibody MSP1a neutralization-sensitive epitope. antiserum whole monospecific polypeptides molecular sizes 105 (MSP1a), 100 (MSP1b), 61, 36 (MSP2) kDa completely hemagglutination. These data confirm proposed location susceptible suggest that they mediate erythrocytes. We propose these are possible adhesins.