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We isolated pili from Escherichia coli SS142. These pili had a diameter of 6 nm and an average length of 400 nm. They were composed of subunits with a molecular weight of 18,000. Their amino acid composition was determined; methionine and proline were not detected. The isolated pili retained mannose-resistant hemagglutinating activity. Proteolytic digestion and glutaraldehyde fixation led to partial or complete loss of the hemagglutinating activity of the pili without causing any detectable damage to their supramolecular structure, which was only disintegrated by treatment with hot sodium dodecyl sulfate. The hemagglutinating activity of E. coli SS142 was inhibited by the glycoproteins fetuin and Tamm-Horsfall protein, as well as by the glycolipids phytyl lactoside, dansyl-sphingosine lactoside, and digalactosyl diglyceride. Isolated pili inhibited the adhesion of the homologous strain E. coli SS142 to Intestine 407 cell monolayers, but did not inhibit the adhesion of E. coli strain B-413, B-506, or 2699. This indicates that E. coli SS142 binds to a receptor different from those recognized by the other strains and that mannose-resistant adhesion to tissue culture cells can be classified into different subtypes.

Properties of pili from Escherichia coli SS142 that mediate mannose-resistant adhesion to mammalian cells