SUMMARY: A K99 variant of B41 was produced by growing the parent strain in the presence of antiserum to K12K99. Two mannose-resistant and eluting (MRE) haemagglutinins with molecular weights greater than 20 × 10 were extracted from the cell surface of the variant. One was an anionic antigen, partially purified by ammonium sulphate and isoelectric point precipitation, which adhered to calf intestinal brush borders; it was a protein composed of subunits with mol. wt 34000. Electron microscopy showed that this material did not have a regular fimbrial appearance, but contained some fine fibrillar structures. A second MRE haemagglutinin which was also partially purified by ammonium sulphate precipitation, had a definite fimbrial structure, being a protein composed of two subunits of mol. wt 49 500 and 48000. 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.


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