Exopeptidases and gingipains in Porphyromonas gingivalis as prerequisites for its amino acid metabolism

Japanese Dental Science Review - Tập 52 - Trang 22-29 - 2016
Takayuki K. Nemoto1, Yuko Ohara-Nemoto1
1Department of Oral Molecular Biology, Course of Medical and Dental Sciences, Nagasaki University Graduate School of Biomedical Sciences, Japan

Tài liệu tham khảo

Slots, 1988, Bacteroides gingivalis, Bacteroides intermedius and Actinobacillus actinomycetemcomitans in human periodontal diseases, J Clin Periodontol, 15, 85, 10.1111/j.1600-051X.1988.tb00999.x White, 1981, Association of oral Bacteroides with gingivitis and adult periodontitis, J Periodontal Res, 16, 259, 10.1111/j.1600-0765.1981.tb00974.x Socransky, 2002, Periodontal microbial ecology, Periodontol 2000, 38, 135, 10.1111/j.1600-0757.2005.00107.x Iwai, 2005, Oral bacteria in the occluded arteries of patients with Buerger disease, J Vasc Surg, 42, 107, 10.1016/j.jvs.2005.03.016 Genco, 2010, Prevention: reducing the risk of CVD in patients with periodontitis, Nat Rev Cardiol, 7, 479, 10.1038/nrcardio.2010.120 Tabeta, 2014, Current evidence and biological plausibility linking periodontitis to atherosclerotic cardiovascular disease, Jpn Dent Sci Rev, 50, 55, 10.1016/j.jdsr.2014.03.001 Kshirsagar, 2007, Antibodies to periodontal organisms are associated with decreased kidney function: the dental atherosclerosis risk in communities study, Blood Purif, 25, 125, 10.1159/000096411 Detert, 2010, The association between rheumatoid arthritis and periodontal disease, Arthritis Res Ther, 12, 218, 10.1186/ar3106 Citron, 2007, Bacteroides, Porphyromonas, Prevotella, Fusobacterium, and other anaerobic Gram-negative rods, vol. 1, 911 Nelson, 2003, Complete genome sequence of the oral pathogenic bacterium Porphyromonas gingivalis strain W83, J Bacteriol, 185, 5591, 10.1128/JB.185.18.5591-5601.2003 Seshadri, 2004, Comparison of the genome of the oral pathogen Treponema denticols with other spirochete genomes, Proc Natl Acad Sci USA, 101, 5646, 10.1073/pnas.0307639101 Mayrand, 1988, Biology of asaccharolytic black-pigmented Bacteroides species, Microbiol Rev, 52, 134, 10.1128/MMBR.52.1.134-152.1988 Shah, 1990, Isolation and characterization of gingivain, a cysteine proteinase from Porphyromonas gingivalis strain W83, Biochem Soc Trans, 18, 578, 10.1042/bst0180578 Chen, 1992, Molecular cloning and structural characterization of the Arg-gingipain proteinase of Porphyromonas gingivalis. Biosynthesis as a proteinase-adhesin polyprotein, J Biol Chem, 267, 18896, 10.1016/S0021-9258(19)37045-0 Takahashi, 2000, Metabolic pathways for cytotoxic end product formation from glutamate- and aspartate-containing peptides by Porphyromonas gingivalis, J Bacteriol, 182, 4704, 10.1128/JB.182.17.4704-4710.2000 Takahashi, 2001, Preferential utilization of dipeptides by Porphyromonas gingivalis, J Dent Res, 80, 1425, 10.1177/00220345010800050801 Dashper, 2001, Sodium ion-driven serine/threonine transport in Porphyromonas gingivalis, J Bacteriol, 183, 4142, 10.1128/JB.183.14.4142-4148.2001 Abiko, 1985, Glycylprolyl dipeptidylaminopeptidase from Bacteroides gingivalis, J Dent Res, 64, 106, 10.1177/00220345850640020201 Banbula, 2000, Emerging family of proline-specific peptidases of Porphyromonas gingivalis: purification and characterization of serine dipeptidyl peptidase, a structural and functional homologue of mammalian prolyl dipeptidyl peptidase IV, Infect Immun, 68, 1176, 10.1128/IAI.68.3.1176-1182.2000 Banbula, 2001, Porphyromonas gingivalis DPP-7 represents a novel type of dipeptidylpeptidase, J Biol Chem, 276, 6299, 10.1074/jbc.M008789200 Banbula, 1999, Prolyl tripeptidyl peptidase from Porphyromonas gingivalis. A novel enzyme with possible pathological implications for the development of periodontitis, J Biol Chem, 274, 9246, 10.1074/jbc.274.14.9246 Mazumdar, 2009, Metabolic network model of a human oral pathogen, J Bacteriol, 191, 74, 10.1128/JB.01123-08 Ohara-Nemoto, 2011, Asp- and Glu-specific novel dipeptidyl peptidase 11 of Porphyromonas gingivalis ensures utilization of proteinaceous energy sources, J Biol Chem, 286, 38115, 10.1074/jbc.M111.278572 Ohara-Nemoto, 2014, Identification and characterization of prokaryotic dipeptidyl-peptidase 5 from Porphyromonas gingivalis, J Biol Chem, 289, 5436, 10.1074/jbc.M113.527333 Nemoto, 2014, Mechanism on oligomer–monomer transition of a novel peptidase from periodontopathic bacterium Shi, 1999, Genetic analyses of proteolysis, hemoglobin binding, and hemagglutination of Porphyromonas gingivalis. Construction of mutants with a combination of rgpA, rgpB, kgp, and hagA, J Biol Chem, 274, 17955, 10.1074/jbc.274.25.17955 O’Brien-Simpson, 2001, Role of RgpA, RgpB, and Kgp proteinases in virulence of Porphyromonas gingivalis W50 in a murine lesion model, Infect Immun, 69, 7527, 10.1128/IAI.69.12.7527-7534.2001 Potempa, 1997, Titration and mapping of the active site of cysteine proteases from Porphyromonas gingivalis (gingipains) using peptidyl chloromethanes, Biol Chem, 378, 223, 10.1515/bchm.1997.378.3-4.223 Imamura, 2003, The biphasic virulence activities of gingipains: activation and inactivation of host proteins, Curr Protein Pept Sci, 4, 443, 10.2174/1389203033487027 Kadowaki, 2007, A role for gingipains in cellular responses and bacterial survival in Porphyromonas gingivalis-infected cells, Front Biosci, 12, 4800, 10.2741/2428 Fitzpatrick, 2009, The gingipains: scissors and glue of the periodontal pathogen, Porphyromonas gingivalis, Future Microbiol, 4, 471, 10.2217/fmb.09.18 Rawlings, 2014, MEROPS: the database of proteolytic enzymes, their substrates and inhibitors, Nucleic Acids Res, 42, D503, 10.1093/nar/gkt953 Kadowaki, 1994, Purification and characterization of a novel arginine-specific cysteine proteinase (argingipain) involved in the pathogenesis of periodontal disease from the culture supernatant of Porphyromonas gingivalis, J Biol Chem, 269, 21371, 10.1016/S0021-9258(17)31972-5 Potempa, 1995, The multiple forms of trypsin-like activity present in various strains of Porphyromonas gingivalis are due to the presence of either Arg-gingipain or Lys-gingipain, Infect Immun, 63, 1176, 10.1128/IAI.63.4.1176-1182.1995 Fujimura, 1992, Comparative studies of three proteases of Porphyromonas gingivalis, Oral Microbiol Immunol, 7, 212, 10.1111/j.1399-302X.1992.tb00027.x Scott, 1993, Purification and characterization of a potent 70-kDa thiol lysyl-proteinase (Lys-gingipain) from Porphyromonas gingivalis that cleaves kininogens and fibrinogen, J Biol Chem, 268, 7935, 10.1016/S0021-9258(18)53048-9 Pavloff, 1997, Molecular cloning and characterization of Porphyromonas gingivalis lysine-specific gingipain. A new member of an emerging family of pathogenic bacterial cysteine proteinases, J Biol Chem, 272, 1595, 10.1074/jbc.272.3.1595 Singer, 1981, Butyrate and propionate: important components of toxic dental plaque extracts, Infect Immun, 32, 458, 10.1128/IAI.32.2.458-463.1981 Ho, 2007, Effects of a bacterial lipid byproduct on human pulp fibroblasts in vitro, J Endod, 33, 437, 10.1016/j.joen.2006.12.022 Kurita-Ochiai, 2008, Butyric acid induces apoptosis in inflamed fibroblasts, J Dent Res, 87, 51, 10.1177/154405910808700108 Kiyama, 1998, Sequence analysis of the Porphyromonas gingivalis dipeptidyl peptidase IV gene, Biochim Biophys Acta, 1396, 39, 10.1016/S0167-4781(97)00225-X Oda, 2009, Participation of the secreted dipeptidyl and tripeptidyl aminopeptidases in asaccharolytic growth of Porphyromonas gingivalis, J Priodontal Res, 44, 362, 10.1111/j.1600-0765.2008.01117.x Kumagai, 2005, Molecular mechanism for connective tissue destruction by dipeptidyl aminopeptidase IV produced by the periodontal pathogen Porphyromonas gingivalis, Infect Immun, 73, 2655, 10.1128/IAI.73.5.2655-2664.2005 Clais, 2014, Importance of biofilm formation and dipeptidyl peptidase IV for the pathogenicity of clinical Porphyromonas gingivalis isolates, Pathog Dis, 70, 408, 10.1111/2049-632X.12156 Beauvais, 1997, Biochemical and antigenic characterization of a new dipeptidyl-peptidase isolated from Aspergillus fumigatus, J Biol Chem, 7, 6238, 10.1074/jbc.272.10.6238 Monod, 2012, Dipeptidyl-peptidases IV and V of Aspergillus, 3392 Loussert, 2010, In vivo biofilm composition of Aspergillus fumigatus, Cell Microbiol, 12, 405, 10.1111/j.1462-5822.2009.01409.x Rouf, 2013, Phenylalanine664 of dipeptidyl peptidase (DPP) 7 and phenylalanine671 of DPP11 mediate preference for P2-position hydrophobic residues of a substrate, FEBS Open Bio, 3, 177, 10.1016/j.fob.2013.03.004 Kon, 2002, Pathogenic factors of Porphyromonas endodontalis, Dent J Iwate Med Univ, 27, 187 Nishimata, 2014, Identification of dipeptidyl-peptidase (DPP) 5 and DPP7 in Porphyromonas endodontalis, distinct from those in Porphyromonas gingivalis, PLOS ONE, 9, e114221, 10.1371/journal.pone.0114221 Rouf, 2013, Discrimination based on Gly and Arg/Ser at Position 673 between dipeptidyl-peptidase (DPP) 7 and DPP11, widely distributed DPPs in pathogenic and environmental Gram-negative bacteria, Biochimie, 95, 824, 10.1016/j.biochi.2012.11.019 Sakamoto, 2014, S46 peptidases are the first exopeptidases to be members of clan PA, Sci Rep, 15, 4977, 10.1038/srep04977 Underwood, 1999, Sequence, purification, and cloning of an intracellular serine protease, quiescent cell proline dipeptidase, J Biol Chem, 274, 34053, 10.1074/jbc.274.48.34053 Bezerra, 2012, Structures of human DPP7 reveal the molecular basis of specific inhibition and the architectural diversity of proline-specific peptidases, PLoS ONE, 7, e43019, 10.1371/journal.pone.0043019 Naito, 2008, Determination of the genome sequence of Porphyromonas gingivalis strain ATCC 33277 and genomic comparison with strain W83 revealed extensive genome rearrangements in P. gingivalis, DNA Res, 15, 215, 10.1093/dnares/dsn013 Ito, 2006, Crystal structure and mechanism of tripeptidyl activity of prolyl tripeptidyl aminopeptidase from Porphyromonas gingivalis, J Mol Biol, 362, 228, 10.1016/j.jmb.2006.06.083 Sato, 2010, A protein secretion system linked to bacteroidete gliding motility and pathogenesis, Proc Natl Acad Sci USA, 107, 276, 10.1073/pnas.0912010107 Veith, 2014, Porphyromonas gingivalis outer membrane vesicles exclusively contain outer membrane and periplasmic proteins and carry a cargo enriched with virulence factors, J Proteome Res, 13, 2420, 10.1021/pr401227e