Genes of pyelonephritogenic E. coli required for digalactoside-specific agglutination of human cells.

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Abstract
Most pyelonephritic Escherichia coli strains bind to digalactoside‐containing glycolipids on uroepithelial cells. Purified Pap pili (pili associated with pyelonephritis) show the same binding specificity. A non‐polar mutation early in the papA pilin gene abolishes formation of Pap pili but does not affect the degree of digalactoside‐specific hemagglutination. Three novel pap genes, papE, papF and papG are defined in this report. The papF and papG gene products are both required for digalactoside‐specific agglutination by whole bacteria cells as well as for agglutination by pilus preparations. Pili prepared from a papE mutant have lost their binding ability although whole cells from this mutant retain it, implying an adhesin anchoring role for the papE gene product. A mutant with lesions both in the papA and the papE genes does not mediate digalactoside‐specific agglutination. The implications of this finding for pilus biogenesis are discussed.