ABSTRACT
Pili of Aeromonas sobria Ae1 were purified and characterized. The molecular mass of the pilin was estimated to be about 23 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The Ae1 pili were electrophoretically and immunologically distinguishable from the W pili of A. hydrophila Ae6, although the two pili were morphologically indistinguishable. The N-terminal amino acid sequences of the two pilins were identical in the first 10 residues. Strain Ae1 and its purified pili adhered to human and rabbit intestines and agglutinated human and rabbit erythrocytes. Hemagglutination was inhibited by D-galactose and D-mannose, but not by L-fucose. Organisms pretreated with the Fab fraction of the antipilus antibody failed to adhere to the intestines. Organisms did not adhere to intestines pretreated with the purified pili. These findings suggest that the pili are a colonization factor of A. sobria Ae1.
