Document Detail


Characterization of fimbriae produced by enteropathogenic Escherichia coli.
MedLine Citation:
PMID:  7901197     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Enteropathogenic Escherichia coli (EPEC) express rope-like bundles of filaments, termed bundle-forming pili (BFP) (J. A. Girón, A. S. Y. Ho, and G. K. Schoolnik, Science 254:710-713, 1991). Expression of BFP is associated with localized adherence to HEp-2 cells and the presence of the EPEC adherence factor plasmid. In this study, we describe the identification of rod-like fimbriae and fibrillae expressed simultaneously on the bacterial surface of three prototype EPEC strains. Upon fimbrial extraction from EPEC B171 (O111:NM), three fimbrial subunits with masses of 16.5, 15.5, and 14.7 kDa were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Their N-terminal amino acid sequence showed homology with F9 and F7(2) fimbriae of uropathogenic E. coli and F1845 of diffuse-adhering E. coli, respectively. The mixture of fimbrial subunits (called FB171) exhibited mannose-resistant agglutination of human erythrocytes only, and this activity was not inhibited by alpha-D-Gal(1-4)-beta-Gal disaccharide or any other described receptor analogs for P, S, F, M, G, and Dr hemagglutinins of uropathogenic E. coli, which suggests a different receptor specificity. Hemagglutination was inhibited by extracellular matrix glycoproteins, i.e., collagen type IV, laminin, and fibronectin, and to a lesser extent by gangliosides, fetuin, and asialofetuin. Scanning electron microscopic studies performed on clusters of bacteria adhering to HEp-2 cells revealed the presence of structures resembling BFP and rod-like fimbriae linking bacteria to bacteria and bacteria to the eukaryotic cell membrane. We suggest a role of these surface appendages in the interaction of EPEC with eukaryotic cells as well as in the overall pathogenesis of intestinal disease caused by EPEC.
Authors:
J A Girón; A S Ho; G K Schoolnik
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Journal of bacteriology     Volume:  175     ISSN:  0021-9193     ISO Abbreviation:  J. Bacteriol.     Publication Date:  1993 Nov 
Date Detail:
Created Date:  1993-12-14     Completed Date:  1993-12-14     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  2985120R     Medline TA:  J Bacteriol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  7391-403     Citation Subset:  IM    
Affiliation:
Department of Microbiology and Immunology, Howard Hughes Medical Institute, Stanford University, California 94305.
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MeSH Terms
Descriptor/Qualifier:
ABO Blood-Group System
Amino Acid Sequence
Bacterial Adhesion
Bacterial Outer Membrane Proteins / analysis*,  isolation & purification
Blotting, Western
Diarrhea / microbiology
Electrophoresis, Polyacrylamide Gel
Escherichia coli / pathogenicity,  physiology,  ultrastructure*
Extracellular Matrix Proteins / pharmacology
Fimbriae, Bacterial / ultrastructure*
Hemagglutination / drug effects
Hemagglutination Inhibition Tests
Humans
Infant
Macromolecular Substances
Microscopy, Electron, Scanning
Microscopy, Immunoelectron
Molecular Sequence Data
Tumor Cells, Cultured
Urinary Tract Infections / microbiology
Grant Support
ID/Acronym/Agency:
DK 38707/DK/NIDDK NIH HHS
Chemical
Reg. No./Substance:
0/ABO Blood-Group System; 0/Bacterial Outer Membrane Proteins; 0/Extracellular Matrix Proteins; 0/Macromolecular Substances
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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