Abstract
The afimbrial adhesive sheath, encoded by the afa-3 gene cluster, is composed of two proteins with different roles in bacterium-HeLa cell interactions. AfaE is required for adhesion and AfaD for internalization. In this study, we found that the AfaD invasin was structurally and functionally conserved among human afa-expressing strains, independently of AfaE subtype and clinical origin of the Escherichia coli isolate. The AggB protein from enteroaggregative E. coli was also found to be an AfaD-related invasin. These data suggest that AfaD is the prototype of a family of invasins encoded by adhesion-associated operons in pathogenic E. coli.
MeSH terms
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Adhesins, Bacterial*
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Adhesins, Escherichia coli / chemistry*
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Adhesins, Escherichia coli / metabolism
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Amino Acid Sequence
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Animals
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Bacterial Proteins / chemistry*
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Bacterial Proteins / metabolism
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CHO Cells
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Cell Adhesion
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Conserved Sequence
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Cricetinae
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DNA Primers / metabolism
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Escherichia coli / genetics
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Escherichia coli / metabolism*
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Escherichia coli / pathogenicity
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Escherichia coli Infections / microbiology*
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Genetic Complementation Test
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HeLa Cells
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Humans
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Intestinal Diseases / microbiology*
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Microscopy, Electron
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Molecular Sequence Data
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Multigene Family
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Mutagenesis
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Plasmids / metabolism
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Recombinant Proteins / metabolism
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Sequence Analysis, DNA
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Sequence Homology, Amino Acid
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Urinary Tract Infections / microbiology
Substances
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Adhesins, Bacterial
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Adhesins, Escherichia coli
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AfaD protein, E coli
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AfaE protein, E coli
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Bacterial Proteins
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DNA Primers
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Recombinant Proteins
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invasin, Yersinia
Associated data
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GENBANK/AF233530
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GENBANK/AF233531
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GENBANK/AF233532
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GENBANK/AF233533
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GENBANK/AF284829