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PMID: 1348107 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

P pili in uropathogenic E. coli are composite fibres with distinct fibrillar adhesive tips.

Nature ·Vol. 356 ·No. 6366 ·1992-03-19 ·Pages 252-5

Kuehn MJ, Heuser J, Normark S, Hultgren SJ

Abstract

Escherichia coli is a frequent cause of several common bacterial infections in humans and animals, including urinary tract infections, bacteraemia and bacteria-related diarrhoea and is also the main cause of neonatal meningitis. Microbial attachment to surfaces is a key event in colonization and infection and results mainly from a stereochemical fit between microbial adhesins and complementary receptors on host cells. Bacterial adhesins required for extracellular colonization by Gram-negative bacteria are often minor components of heteropolymeric fibres called pili which must be oriented in an accessible manner in these structures to be able to bind to specific receptor architectures. P pili mediate the binding of uropathogenic E. coli to a digalactoside receptor determinant present in the urinary tract epithelium. We report here that the adhesin is a component of distinct fibrillar structures present at the tips of the pili. These virulence-associated tip fibrillae are thin, flexible polymers composed mostly of repeating subunits of PapE that frequently terminate with the alpha-D-galactopyranosyl-(1-4)-beta-D-galactopyranose or Gal alpha (1-4)Gal binding PapG adhesin.

Related Genes
pap
MeSH Terms
Adhesins, Escherichia coli Bacterial Outer Membrane Proteins/chemistry,genetics Carbohydrate Sequence Cloning, Molecular Epithelium/microbiology Escherichia coli/genetics,pathogenicity,ultrastructure Fimbriae, Bacterial/chemistry,physiology,ultrastructure Microscopy, Electron Molecular Sequence Data Mutation Operon Plasmids Polymerase Chain Reaction Repetitive Sequences, Nucleic Acid Restriction Mapping Urinary Tract/microbiology Urinary Tract Infections/microbiology
Chemicals
Adhesins, Escherichia coli Bacterial Outer Membrane Proteins
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Kuehn M J
Department of Molecular Microbiology, Washington University School of Medicine, St. Louis, Missouri 63110.
Heuser J
Normark S
Hultgren S J
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
1992-03-19
Pages
252-5
Language
English
Region
England
NLM ID
0410462
Subset
IM
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