Structural characterization of argingipain, a novel arginine-specific cysteine proteinase as a major periodontal pathogenic factor from porphyromonas gingivalis

Kuniaki Okamoto, Yoshio Misumi, Tomoko Kadowaki, Masahiro Yoneda, Kenji Yamamoto, Yukio Ikehara

Research output: Contribution to journalArticle

80 Citations (Scopus)

Abstract

Argingipain, so termed due to its peptide cleavage specificity at arginine residue, is a unique extracellular cysteine proteinase produced by the anaerobic rod Porphyromonas gingivalis, which is known as a major pathogenic factor of the progressive periodontal disease (T, Kadowaki, M. Yoneda, K. Okamoto, K. Maeda, and K, Yamamoto (1994) J. Biol. Chem. 269, 21371-21378), The catalytic specificity and functional importance of this enzyme prompted us to elucidate its structural features. A DNA fragment for argingipain was selectively amplified by polymerase chain reaction using mixed oligonucleotide primers designed from the NH2-terminal amino acid sequence of the purified enzyme. Although the extracellular mature enzyme was shown to have an apparent molecular mass of 44 kDa in gels, the nucleotide sequence of the isolated gene revealed a single gene coding for a 109-kDa precursor of argingipain. The deduced amino acid sequence exhibited no significant similarity to the sequences of representative members of the cysteine protease family. The precursor contained four functional domains: The NH2-terminal signal peptide required for the inner membrane transport; the NH2-terminal prosequence, which is assumed to stabilize the precursor structure; the proteinase domain; and the COOH-terminal hemagglutinin domain, which appears to be essential for extracellular secretion of the proteinase domain. Experiments involving the addition of the argingipain inhibitors to the culture medium of P. gingivalis suggested that the maturation of argingipain occurs intracellularly via an autocatalytic cleavage of the pro-argingipain propeptide.

Original languageEnglish
Pages (from-to)917-925
Number of pages9
JournalArchives of Biochemistry and Biophysics
Volume316
Issue number2
DOIs
Publication statusPublished - Feb 1 1995
Externally publishedYes

Fingerprint

Porphyromonas gingivalis
Cysteine Proteases
Arginine
Amino Acid Sequence
Peptide Hydrolases
Enzymes
Genes
Amino Acids
DNA Primers
Polymerase chain reaction
Hemagglutinins
Molecular mass
Periodontal Diseases
Protein Sorting Signals
Culture Media
Nucleotides
Gels
Membranes
Polymerase Chain Reaction
Peptides

Keywords

  • Argingipain
  • Arginine-specinc cysteine proteinases
  • Periodontitis
  • Porphyromonas gingivalis

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

Cite this

Structural characterization of argingipain, a novel arginine-specific cysteine proteinase as a major periodontal pathogenic factor from porphyromonas gingivalis. / Okamoto, Kuniaki; Misumi, Yoshio; Kadowaki, Tomoko; Yoneda, Masahiro; Yamamoto, Kenji; Ikehara, Yukio.

In: Archives of Biochemistry and Biophysics, Vol. 316, No. 2, 01.02.1995, p. 917-925.

Research output: Contribution to journalArticle

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