Abstract
Specific adherence of pathogenic Escherichia coli (serotypes O1, O2, and O78) to chicken tracheal epithelium was investigated using adherence-inhibition procedures. The role of pilus as adhesin was studied by blocking the pilus with antipilus antibodies. The nature of the host cell receptor was determined by blocking bacterial adhesion with specific carbohydrates or lectins and destroying the receptor with sodium metaperiodate. Antipilus antibodies to all three serotypes significantly (P less than or equal to 0.05) inhibited their adherence. Sodium metaperiodate considerably inhibited the adhesion of all three serotypes, indicating a role for monosaccharides in the host cell receptor. D-Mannose and its derivative methyl-alpha-D-mannopyranoside inhibited the adhesion of serotypes O1 and O78, indicating a role for these sugars in the host cell receptor; this was further supported by the inhibition of both serotypes after treatment of tracheal epithelium with concanavalin A. None of the sugars or lectins used inhibited adhesion of serotype O2.
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