TY - JOUR
T1 - Heterogeneous post-translational modification of Actinobacillus actinomycetemcomitans fimbrillin
AU - Inoue, Tetsuyoshi
AU - Ohta, Hiroyuki
AU - Tanimoto, Ichiro
AU - Shingaki, Ryuji
AU - Fukui, Kazuhiro
PY - 2000
Y1 - 2000
N2 - 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.
AB - 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.
KW - Actinobacillus actinomycetemcomitans
KW - Fimbrillin
KW - Post-translational modification
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U2 - 10.1111/j.1348-0421.2000.tb02554.x
DO - 10.1111/j.1348-0421.2000.tb02554.x
M3 - Article
C2 - 11021403
AN - SCOPUS:0033859189
VL - 44
SP - 715
EP - 718
JO - Microbiology and Immunology
JF - Microbiology and Immunology
SN - 0385-5600
IS - 8
ER -