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 language | English |
|---|---|
| Pages (from-to) | 917-925 |
| Number of pages | 9 |
| Journal | Archives of Biochemistry and Biophysics |
| Volume | 316 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - Feb 1 1995 |
| Externally published | Yes |
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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 journal › Article
}
TY - JOUR
T1 - Structural characterization of argingipain, a novel arginine-specific cysteine proteinase as a major periodontal pathogenic factor from porphyromonas gingivalis
AU - Okamoto, Kuniaki
AU - Misumi, Yoshio
AU - Kadowaki, Tomoko
AU - Yoneda, Masahiro
AU - Yamamoto, Kenji
AU - Ikehara, Yukio
PY - 1995/2/1
Y1 - 1995/2/1
N2 - 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.
AB - 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.
KW - Argingipain
KW - Arginine-specinc cysteine proteinases
KW - Periodontitis
KW - Porphyromonas gingivalis
UR - http://www.scopus.com/inward/record.url?scp=0028931990&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0028931990&partnerID=8YFLogxK
U2 - 10.1006/abbi.1995.1123
DO - 10.1006/abbi.1995.1123
M3 - Article
VL - 316
SP - 917
EP - 925
JO - Archives of Biochemistry and Biophysics
JF - Archives of Biochemistry and Biophysics
SN - 0003-9861
IS - 2
ER -