Purification and characterization of type 1 fimbriae of Salmonella typhi

Microbiol Immunol. 1994;38(5):353-8. doi: 10.1111/j.1348-0421.1994.tb01790.x.


Type 1 fimbriae have been purified from a Salmonella typhi strain of clinical origin. Purified fimbriae retained their ability to bind to erythrocytes in a mannose-inhibitable fashion and, in doing so, behaved preferentially as a monovalent adhesin. SDS-PAGE analysis of the fimbrial preparation showed the presence of a 20-kDa major polypeptide component (fimbrillin) and of additional larger polypeptides present in smaller amounts. The amino-terminal sequence of fimbrillin was determined and turned out to be very similar but not identical to that of type 1 fimbrillins of other Salmonella serovars. A Western blot analysis of the purified fimbrial preparation using an antiserum raised against native fimbriae suggested that fimbrial proteins did not carry any major sequential epitope and that, in native fimbriae, conformational epitopes, possibly generated between different subunits, might provide for the major immunogenic epitopes. Analysis of different S. typhi clinical isolates using the anti-fimbrial antiserum showed an overall immunological similarity of these structures within this serovar.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Antibodies, Bacterial / immunology
  • Antigens, Bacterial / immunology
  • Bacterial Proteins / analysis
  • Electrophoresis, Polyacrylamide Gel
  • Fimbriae Proteins*
  • Fimbriae, Bacterial* / chemistry
  • Fimbriae, Bacterial* / immunology
  • Fimbriae, Bacterial* / ultrastructure
  • Molecular Sequence Data
  • Peptides / analysis
  • Protein Denaturation
  • Rabbits
  • Salmonella typhi / ultrastructure*
  • Sequence Homology, Amino Acid
  • Species Specificity


  • Antibodies, Bacterial
  • Antigens, Bacterial
  • Bacterial Proteins
  • Peptides
  • fimbrillin
  • Fimbriae Proteins