Molecular characterization of low-molecular-weight component protein, Flp, in Actinobacillus actinomycetemcomitans fimbriae

Tetsuyoshi Inoue, Ichiro Tanimoto, Hiroyuki Ohta, Keijiro Kato, Yoji Murayama, Kazuhiro Fukui

Research output: Contribution to journalArticle

60 Citations (Scopus)


Fimbriae preparation from Actinobacillus actinomycetemcomitans was found to contain an abundant low-molecular-weight protein (termed Flp) with an apparent molecular mass of approximately 6.5 kDa, in addition to a small amount of 54-kDa protein. Immunogold electron microscopy localized the Flp protein at the bacterial fimbriae but not at the cell surface. The DNA fragment including the flp gene was cloned from A. actinomycetemcomitans 304- a and its nucleotide sequence was determined. An open reading frame of the flp gene was composed of 225 bp encoding a protein of 75 amino acids. Comparison of the translated amino acid sequence with the sequence of native Flp determined by Edman degradation indicated that the N-terminal part of 26 amino acids is leader peptide. The N-terminal sequence of mature Flp exhibited some similarity to type-IV pilin. Furthermore, the processing site of premature Flp is also similar to that of type-IV prepilin, and a gene encoding a protein homologous to type-IV prepilin-like protein leader peptidase was found downstream of the flp gene. These findings indicate that Flp is the major component protein of A. actinomycetemcomitans fimbriae.

Original languageEnglish
Pages (from-to)253-258
Number of pages6
JournalMicrobiology and Immunology
Issue number4
Publication statusPublished - 1998



  • Actinobacillus actinomycetemcomitans
  • Fimbriae

ASJC Scopus subject areas

  • Immunology and Microbiology(all)
  • Microbiology (medical)
  • Microbiology

Cite this