| Description | The Gram-negative pathogen Escherichia coli causes several common bacterial illnesses in humans, including diarrhoea, neonatal meningitidis and urinary tract infections. Attachment to host tissues is essential for successful invasion, and requires interaction between a bacterial adhesive protein and its target receptor. This protein is usually supported on a larger structure made up of heteropolymeric fibres [ ]. Pyelonephritogenic E. coli specifically invade the uroepithelium by expressing between 100 and 300 pili on their cell surface. Pili are macromolecular structures that allow binding to a digalactoside receptor in the urinary tract.P pili, or fimbriae, are ~68A in diameter and 1 micron in length, the bulk of which is a fibre composed of the main structural protein PapA [ ]. At its tip, the pilus is terminated by a fibrillum consisting of repeating units of the PapE protein. This, in turn, is topped by the adhesins, PapF and PapG, both of which are needed for receptor binding. The tip fibrillum is anchored to the main PapA fibre by the PapK pilus-adaptor protein. PapH, an outer membrane protein, then anchors the entire rod in the bacterial envelope [ ]. A cytoplasmic chaperone (PapD) assists in assembling the monomers of the macromolecule in the membrane.PapF, in addition to aiding in the virulence and binding of uropathogenic E. coli, also functions as an adapter protein that joins the distal end of the tip fibrillum to the main PapG adherence factor. By providing a complementary binding surface for PapE and PapG, pilus assembly is rapidly completed [ ]. | Name | P pili tip fibrillum PapF protein |
| Short Name | P_pili_tip_PapF | Type | Family |
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