Heterogeneous post-translational modification of Actinobacillus actinomycetemcomitans fimbrillin

Tetsuyoshi Inoue, Hiroyuki Ohta, Ichiro Tanimoto, Ryuji Shingaki, Kazuhiro Fukui

Research output: Contribution to journalArticlepeer-review

21 Citations (Scopus)


Fresh isolates of Actinobacillus actinomycetemcomitans produce bundle-forming fimbriae. The exact molecular mass of A. actinomycetemcomitans fimbrillin, a structural subunit of fimbriae, was determined by liquid chromatography-electrospray ionization mass spectrometry. Three major molecular species with 6,226.0, 6,366.0, and 6,513.0 Da were detected in a purified fimbrial fraction from the strain 310-a. These molecular masses were significantly higher than the molecular weight (5,118 Da) calculated from nucleotide sequence data of the fimbrillin gene, flp, suggesting that the fimbrial peptides were post-translationally modified. Modification of the fimbrial peptides was also suggested by an N-terminal amino acid sequence analysis of fimbrillin peptic fragments, with the modified amino acids being due to seven serine or asparagine residues located in the C-terminal region. A periodate oxidation/biotin-hydrazide labeling assay of fimbrillin suggested that it might be glycosylated.

Original languageEnglish
Pages (from-to)715-718
Number of pages4
Issue number8
Publication statusPublished - 2000
Externally publishedYes


  • Actinobacillus actinomycetemcomitans
  • Fimbrillin
  • Post-translational modification

ASJC Scopus subject areas

  • Microbiology
  • Immunology
  • Virology


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