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Heterogeneous Post‐Translational Modification of Actinobacillus actinomycetemcomitans Fimbrillin
Author(s) -
Inoue Tetsuyoshi,
Ohta Hiroyuki,
Tanimoto Ichiro,
Shingaki Ryuji,
Fukui Kazuhiro
Publication year - 2000
Publication title -
microbiology and immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.664
H-Index - 70
eISSN - 1348-0421
pISSN - 0385-5600
DOI - 10.1111/j.1348-0421.2000.tb02554.x
Subject(s) - biology , peptide sequence , biochemistry , electrospray ionization , molecular mass , amino acid , asparagine , serine , actinobacillus , nucleic acid sequence , fimbria , microbiology and biotechnology , mass spectrometry , gene , chemistry , chromatography , escherichia coli , bacteria , genetics , enzyme
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.