Abstract
The K88ab antigen of porcine enteropathogenic strains of Escherichia coli exhibited specific affinity for the chicken erythrocyte membrane which correlated with its adhesion characteristics for piglet enterocytes. Thus the chicken erythrocyte provided a useful model for defining the underlying mechanisms of interaction between K88 bearing E. coli and host cell membranes.
This affinity of enteropathogenic E. coli for chicken erythrocytes and piglet enterocytes has been used in an investigation of the role of antibody against the a, b and c determinants of K88 in blocking microbial adhesion to cell membranes. Antisera raised against K88ab and K88ac inhibited the adhesion of both K88ab and K88ac bearing organisms to the microvilli of piglet enterocytes. Antisera specific for the K88a determinant also blocked adhesion of both K88 organisms to the enterocyte indicating the potential of a broad spectrum of activity against porcine enteropathogens. Antibodies against K88b and K88c determinants showed appropriate selectivity for homologous strains.
The selectivity of antibodies specific for the b and c determinants of K88 was also apparent in the chicken erythrocyte haemagglutination inhibition (HI) assay. However, only low inhibitory activity was demonstrated by anti-K88a sera indicating that the specificity of adhesion of K88ab to chicken erythrocytes does not reside in this determinant.
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