Partial Purification and Characterization of Two Non K99 Mannoseresistant Haemagglutinins of Escherichia coli B41

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Abstract
A K99- variant of E. coli B41 was produced by growing the parent strain in the presence of antiserum to E. coli K12K99. Two mannose-resistant and eluting (MRE) hemagglutinins with MW > 20 .times. 106 were extracted from the cell surface of the variant. One was an anionic antigen, partially purified by ammonium sulfate and isoelectric point precipitation, which adhered to calf intestinal brush borders; it was a protein composed of subunits with MW 34,000. EM showed that this material did not have a regular fimbrial appearance, but contained some fine fibrillar structures. A 2nd MRE hemagglutinin, which was also partially purified by ammonium sulfate precipitation, had a definite fimbrial structure, being a protein composed of 2 subunits of MW 49,500 and 48,000. This antigen was probably responsible for the fimbrial appearance of the K99- variant, but it was antigenically distinct from the anionic adhesin and did not adhere to calf intestinal brush borders.