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

59 Citations (Scopus)

Abstract

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
Volume42
Issue number4
Publication statusPublished - 1998

Fingerprint

Molecular Weight
Aggregatibacter actinomycetemcomitans
Proteins
Genes
Bacterial Fimbriae
Fimbriae Proteins
Amino Acids
Staphylococcal Protein A
Protein Sorting Signals
Open Reading Frames
Bacteria Flp protein
Amino Acid Sequence
Electron Microscopy
DNA

Keywords

  • Actinobacillus actinomycetemcomitans
  • Fimbriae

ASJC Scopus subject areas

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

Cite this

Molecular characterization of low-molecular-weight component protein, Flp, in Actinobacillus actinomycetemcomitans fimbriae. / Inoue, Tetsuyoshi; Tanimoto, Ichiro; Ohta, Hiroyuki; Kato, Keijiro; Murayama, Yoji; Fukui, Kazuhiro.

In: Microbiology and Immunology, Vol. 42, No. 4, 1998, p. 253-258.

Research output: Contribution to journalArticle

Inoue, T, Tanimoto, I, Ohta, H, Kato, K, Murayama, Y & Fukui, K 1998, 'Molecular characterization of low-molecular-weight component protein, Flp, in Actinobacillus actinomycetemcomitans fimbriae', Microbiology and Immunology, vol. 42, no. 4, pp. 253-258.
Inoue, Tetsuyoshi ; Tanimoto, Ichiro ; Ohta, Hiroyuki ; Kato, Keijiro ; Murayama, Yoji ; Fukui, Kazuhiro. / Molecular characterization of low-molecular-weight component protein, Flp, in Actinobacillus actinomycetemcomitans fimbriae. In: Microbiology and Immunology. 1998 ; Vol. 42, No. 4. pp. 253-258.
@article{af89c682ada2469f8bd187d915deb047,
title = "Molecular characterization of low-molecular-weight component protein, Flp, in Actinobacillus actinomycetemcomitans fimbriae",
abstract = "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.",
keywords = "Actinobacillus actinomycetemcomitans, Fimbriae",
author = "Tetsuyoshi Inoue and Ichiro Tanimoto and Hiroyuki Ohta and Keijiro Kato and Yoji Murayama and Kazuhiro Fukui",
year = "1998",
language = "English",
volume = "42",
pages = "253--258",
journal = "Microbiology and Immunology",
issn = "0385-5600",
publisher = "Center for Academic Publications Japan",
number = "4",

}

TY - JOUR

T1 - Molecular characterization of low-molecular-weight component protein, Flp, in Actinobacillus actinomycetemcomitans fimbriae

AU - Inoue, Tetsuyoshi

AU - Tanimoto, Ichiro

AU - Ohta, Hiroyuki

AU - Kato, Keijiro

AU - Murayama, Yoji

AU - Fukui, Kazuhiro

PY - 1998

Y1 - 1998

N2 - 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.

AB - 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.

KW - Actinobacillus actinomycetemcomitans

KW - Fimbriae

UR - http://www.scopus.com/inward/record.url?scp=0031968738&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0031968738&partnerID=8YFLogxK

M3 - Article

C2 - 9623911

AN - SCOPUS:0031968738

VL - 42

SP - 253

EP - 258

JO - Microbiology and Immunology

JF - Microbiology and Immunology

SN - 0385-5600

IS - 4

ER -