An adhesive protein capsule of Escherichia coli

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Abstract
The nature of the adhesive capacity of 3 hemagglutinating E. coli strains that had earlier been described as nonfimbriated was studied. The strains that were isolated from human disease adhered to human buccal and urinary tract epithelial cells, an adhesion that was not inhibited by D-mannose. Crossed immunoelectrophoresis showed that the 3 strains produced a common antigen, Z1, developed after growth at 37.degree. C, but not 18.degree. C. One of the strains produced an additional antigen, Z2, of almost the same electrophoretic mobility in crossed immunoelectrophoresis. A mutant of this strain deficient of its polysaccharide K antigen maintained adhesive capacity, indicating that the K antigen was not responsible for adhesion. A further mutant of the acapsular mutant produced a strongly reduced amount of the Z antigens and lost the ability to adhere. The Z1 (and Z2?) antigens were therefore probably responsible for adhesion. In sodium dodecyl sulfate-polyacrylamide gel electrophoresis of extracts of cells of the 3 strains, a heavy Coomassie-blue stained line was seen, indicating the presence of a protein subunit of MW slightly > 14,400. Immunoblotting with absorbed antiserum showed that this protein was the same as that detected by crossed immunoelectrophoresis. Protease from Streptomyces griseus, but not trypsin, digested the protein. Heating to 100.degree. C did not affect it. By immunoelectron microscopy of embedded and sectioned bacteria that had first been treated with specific antisera and ferritin-labeled antirabbit Ig, the protein adhesion-antibody complex was found to surround the bacteria as a heavy capsule. After negative staining with uranylacetate (pH .apprx. 4), the capsule appeared as a mesh of very fine filaments. The possible role of this capsule in the pathogenesis of disease is discussed.

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