Abstract
The adhesive fimbrial antigen F12 from a strain of uropathogenic Escherichia coli has been isolated and characterized. The antigen was purified by ammonium sulfate precipitation and gel chromatography. The protein subunit of the F12 fimbria has a molecular weight of 18,200; the N-terminal amino acid sequence of the subunit shows close resemblance to that of the subunits of other F fimbriae and the type 1 fimbriae. We identified in these proteins a pattern of alternating conserved and variable amino acid residues which could indicate a special structural and functional feature.
MeSH Terms
Amino Acid Sequence
Amino Acids/analysis
Antigens, Bacterial/analysis,isolation & purification
Chemical Phenomena
Chemistry
Escherichia coli/growth & development,immunology,pathogenicity
Escherichia coli Infections/etiology,immunology,microbiology
Fimbriae Proteins
Humans
Immunoelectrophoresis, Two-Dimensional
Molecular Weight
Urinary Tract Infections/etiology,immunology,microbiology
Virulence
Chemicals
Amino Acids
Antigens, Bacterial
colonization factor antigens
Fimbriae Proteins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Klemm P
Orskov I
Orskov F
References (17)
17 references, click to expand
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