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Volumn 11, Issue 9, 2015, Pages 1-31

Porphyromonas gingivalis Type IX Secretion Substrates Are Cleaved and Modified by a Sortase-Like Mechanism

Author keywords

[No Author keywords available]

Indexed keywords

SORTASE; AMINOACYLTRANSFERASE; BACTERIAL PROTEIN; BACTERIAL SECRETION SYSTEM; CYSTEINE PROTEINASE; PEPTIDE FRAGMENT; PROTEINASE K; RECOMBINANT PROTEIN; SIGNAL PEPTIDE;

EID: 84943556752     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1005152     Document Type: Article
Times cited : (84)

References (59)
  • 2
    • 84877078603 scopus 로고    scopus 로고
    • Periodontitis and atherosclerotic cardiovascular disease: consensus report of the Joint EFP/AAP Workshop on Periodontitis and Systemic Diseases
    • Tonetti MS, Van Dyke TE, Periodontitis and atherosclerotic cardiovascular disease: consensus report of the Joint EFP/AAP Workshop on Periodontitis and Systemic Diseases. J Periodontol. 2013;84: S24–29. doi: 10.1902/jop.2013.1340019 23631582
    • (2013) J Periodontol , vol.84 , pp. 24-29
    • Tonetti, M.S.1    Van Dyke, T.E.2
  • 3
    • 84877021027 scopus 로고    scopus 로고
    • Periodontal systemic associations: review of the evidence
    • Linden GJ, Lyons A, Scannapieco FA, Periodontal systemic associations: review of the evidence. J Periodontol. 2013;84: S8–S19. doi: 10.1902/jop.2013.1340010 23631586
    • (2013) J Periodontol , vol.84 , pp. 8-19
    • Linden, G.J.1    Lyons, A.2    Scannapieco, F.A.3
  • 4
    • 0031766801 scopus 로고    scopus 로고
    • Life below the gum line: pathogenic mechanisms of Porphyromonas gingivalis
    • Lamont RJ, Jenkinson HF, Life below the gum line: pathogenic mechanisms of Porphyromonas gingivalis. Microbiol Mol Biol Rev. 1998;62: 1244–1263. 9841671
    • (1998) Microbiol Mol Biol Rev , vol.62 , pp. 1244-1263
    • Lamont, R.J.1    Jenkinson, H.F.2
  • 5
    • 0035192014 scopus 로고    scopus 로고
    • Role of RgpA, RgpB, and Kgp proteinases in virulence of Porphyromonas gingivalis W50 in a murine lesion model
    • O'Brien-Simpson NM, Paolini RA, Hoffmann B, Slakeski N, Dashper SG, Reynolds EC, Role of RgpA, RgpB, and Kgp proteinases in virulence of Porphyromonas gingivalis W50 in a murine lesion model. Infect Immun. 2001;69: 7527–7534. 11705929
    • (2001) Infect Immun , vol.69 , pp. 7527-7534
    • O'Brien-Simpson, N.M.1    Paolini, R.A.2    Hoffmann, B.3    Slakeski, N.4    Dashper, S.G.5    Reynolds, E.C.6
  • 6
    • 24744447203 scopus 로고    scopus 로고
    • An immune response directed to proteinase and adhesin functional epitopes protects against Porphyromonas gingivalis-induced periodontal bone loss
    • O'Brien-Simpson NM, Pathirana RD, Paolini RA, Chen YY, Veith PD, Tam V, et al. An immune response directed to proteinase and adhesin functional epitopes protects against Porphyromonas gingivalis-induced periodontal bone loss. J Immunol. 2005;175: 3980–3989. 16148146
    • (2005) J Immunol , vol.175 , pp. 3980-3989
    • O'Brien-Simpson, N.M.1    Pathirana, R.D.2    Paolini, R.A.3    Chen, Y.Y.4    Veith, P.D.5    Tam, V.6
  • 7
    • 62449341627 scopus 로고    scopus 로고
    • Porphyromonas gingivalis RgpA-Kgp proteinase-adhesin complexes penetrate gingival tissue and induce proinflammatory cytokines or apoptosis in a concentration-dependent manner
    • O'Brien-Simpson NM, Pathirana RD, Walker GD, Reynolds EC, Porphyromonas gingivalis RgpA-Kgp proteinase-adhesin complexes penetrate gingival tissue and induce proinflammatory cytokines or apoptosis in a concentration-dependent manner. Infect Immun. 2009;77: 1246–1261. doi: 10.1128/IAI.01038-08 19114547
    • (2009) Infect Immun , vol.77 , pp. 1246-1261
    • O'Brien-Simpson, N.M.1    Pathirana, R.D.2    Walker, G.D.3    Reynolds, E.C.4
  • 8
    • 33749023323 scopus 로고    scopus 로고
    • The RgpB C-terminal domain has a role in attachment of RgpB to the outer membrane and belongs to a novel C-terminal-domain family found in Porphyromonas gingivalis
    • Seers CA, Slakeski N, Veith PD, Nikolof T, Chen YY, Dashper SG, et al. The RgpB C-terminal domain has a role in attachment of RgpB to the outer membrane and belongs to a novel C-terminal-domain family found in Porphyromonas gingivalis. J Bacteriol. 2006;188: 6376–6386. 16923905
    • (2006) J Bacteriol , vol.188 , pp. 6376-6386
    • Seers, C.A.1    Slakeski, N.2    Veith, P.D.3    Nikolof, T.4    Chen, Y.Y.5    Dashper, S.G.6
  • 9
    • 76249128306 scopus 로고    scopus 로고
    • A protein secretion system linked to bacteroidete gliding motility and pathogenesis
    • Sato K, Naito M, Yukitake H, Hirakawa H, Shoji M, McBride MJ, et al. A protein secretion system linked to bacteroidete gliding motility and pathogenesis. Proc Natl Acad Sci U S A. 2010;107: 276–281. doi: 10.1073/pnas.0912010107 19966289
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 276-281
    • Sato, K.1    Naito, M.2    Yukitake, H.3    Hirakawa, H.4    Shoji, M.5    McBride, M.J.6
  • 10
    • 84870908979 scopus 로고    scopus 로고
    • Identification of Porphyromonas gingivalis proteins secreted by the Por secretion system
    • Sato K, Yukitake H, Narita Y, Shoji M, Naito M, Nakayama K, Identification of Porphyromonas gingivalis proteins secreted by the Por secretion system. FEMS Microbiol Lett. 2013;338: 68–76. doi: 10.1111/1574-6968.12028 23075153
    • (2013) FEMS Microbiol Lett , vol.338 , pp. 68-76
    • Sato, K.1    Yukitake, H.2    Narita, Y.3    Shoji, M.4    Naito, M.5    Nakayama, K.6
  • 11
    • 84872151763 scopus 로고    scopus 로고
    • Gliding motility and Por secretion system genes are widespread among members of the phylum Bacteroidetes
    • McBride MJ, Zhu Y, Gliding motility and Por secretion system genes are widespread among members of the phylum Bacteroidetes. J Bacteriol. 2013;195: 270–278. doi: 10.1128/JB.01962-12 23123910
    • (2013) J Bacteriol , vol.195 , pp. 270-278
    • McBride, M.J.1    Zhu, Y.2
  • 12
    • 84885234044 scopus 로고    scopus 로고
    • Protein substrates of a novel secretion system are numerous in the Bacteroidetes phylum and have in common a cleavable C-terminal secretion signal, extensive post-translational modification, and cell-surface attachment
    • Veith PD, Nor Muhammad NA, Dashper SG, Likic VA, Gorasia DG, Chen D, et al. Protein substrates of a novel secretion system are numerous in the Bacteroidetes phylum and have in common a cleavable C-terminal secretion signal, extensive post-translational modification, and cell-surface attachment. J Proteome Res. 2013;12: 4449–4461. doi: 10.1021/pr400487b 24007199
    • (2013) J Proteome Res , vol.12 , pp. 4449-4461
    • Veith, P.D.1    Nor Muhammad, N.A.2    Dashper, S.G.3    Likic, V.A.4    Gorasia, D.G.5    Chen, D.6
  • 13
    • 0036533761 scopus 로고    scopus 로고
    • Major outer membrane proteins and proteolytic processing of RgpA and Kgp of Porphyromonas gingivalis W50
    • Veith PD, Talbo GH, Slakeski N, Dashper SG, Moore C, Paolini RA, et al. Major outer membrane proteins and proteolytic processing of RgpA and Kgp of Porphyromonas gingivalis W50. Biochem J. 2002;363: 105–115. 11903053
    • (2002) Biochem J , vol.363 , pp. 105-115
    • Veith, P.D.1    Talbo, G.H.2    Slakeski, N.3    Dashper, S.G.4    Moore, C.5    Paolini, R.A.6
  • 14
    • 0035726524 scopus 로고    scopus 로고
    • Structural analysis of the polysaccharide from the lipopolysaccharide of Porphyromonas gingivalis strain W50
    • Paramonov N, Bailey D, Rangarajan M, Hashim A, Kelly G, Curtis MA, et al. Structural analysis of the polysaccharide from the lipopolysaccharide of Porphyromonas gingivalis strain W50. Eur J Biochem. 2001;268: 4698–4707. 11532006
    • (2001) Eur J Biochem , vol.268 , pp. 4698-4707
    • Paramonov, N.1    Bailey, D.2    Rangarajan, M.3    Hashim, A.4    Kelly, G.5    Curtis, M.A.6
  • 15
    • 27444442409 scopus 로고    scopus 로고
    • Structural analysis of a novel anionic polysaccharide from Porphyromonas gingivalis strain W50 related to Arg-gingipain glycans
    • Paramonov N, Rangarajan M, Hashim A, Gallagher A, Aduse-Opoku J, Slaney JM, et al. Structural analysis of a novel anionic polysaccharide from Porphyromonas gingivalis strain W50 related to Arg-gingipain glycans. Mol Microbiol. 2005;58: 847–863. 16238632
    • (2005) Mol Microbiol , vol.58 , pp. 847-863
    • Paramonov, N.1    Rangarajan, M.2    Hashim, A.3    Gallagher, A.4    Aduse-Opoku, J.5    Slaney, J.M.6
  • 16
    • 41949128827 scopus 로고    scopus 로고
    • Identification of a second lipopolysaccharide in Porphyromonas gingivalis W50
    • Rangarajan M, Aduse-Opoku J, Paramonov N, Hashim A, Bostanci N, Fraser OP, et al. Identification of a second lipopolysaccharide in Porphyromonas gingivalis W50. J Bacteriol. 2008;190: 2920–2932. doi: 10.1128/JB.01868-07 18263730
    • (2008) J Bacteriol , vol.190 , pp. 2920-2932
    • Rangarajan, M.1    Aduse-Opoku, J.2    Paramonov, N.3    Hashim, A.4    Bostanci, N.5    Fraser, O.P.6
  • 17
    • 0032769105 scopus 로고    scopus 로고
    • Variable carbohydrate modifications to the catalytic chains of the RgpA and RgpB proteases of Porphyromonas gingivalis W50
    • Curtis MA, Thickett A, Slaney JM, Rangarajan M, Aduse-Opoku J, Shepherd P, et al. Variable carbohydrate modifications to the catalytic chains of the RgpA and RgpB proteases of Porphyromonas gingivalis W50. Infect Immun. 1999;67: 3816–3823. 10417143
    • (1999) Infect Immun , vol.67 , pp. 3816-3823
    • Curtis, M.A.1    Thickett, A.2    Slaney, J.M.3    Rangarajan, M.4    Aduse-Opoku, J.5    Shepherd, P.6
  • 18
    • 0036232069 scopus 로고    scopus 로고
    • Construction and characterization of a nonpigmented mutant of Porphyromonas gingivalis: cell surface polysaccharide as an anchorage for gingipains
    • Shoji M, Ratnayake DB, Shi Y, Kadowaki T, Yamamoto K, Yoshimura F, et al. Construction and characterization of a nonpigmented mutant of Porphyromonas gingivalis: cell surface polysaccharide as an anchorage for gingipains. Microbiology. 2002;148: 1183–1191. 11932462
    • (2002) Microbiology , vol.148 , pp. 1183-1191
    • Shoji, M.1    Ratnayake, D.B.2    Shi, Y.3    Kadowaki, T.4    Yamamoto, K.5    Yoshimura, F.6
  • 19
    • 84863806174 scopus 로고    scopus 로고
    • PG0026 is the C-terminal signal peptidase of a novel secretion system of Porphyromonas gingivalis
    • Glew MD, Veith PD, Peng B, Chen YY, Gorasia DG, Yang Q, et al. PG0026 is the C-terminal signal peptidase of a novel secretion system of Porphyromonas gingivalis. J Biol Chem. 2012;287: 24605–24617. doi: 10.1074/jbc.M112.369223 22593568
    • (2012) J Biol Chem , vol.287 , pp. 24605-24617
    • Glew, M.D.1    Veith, P.D.2    Peng, B.3    Chen, Y.Y.4    Gorasia, D.G.5    Yang, Q.6
  • 20
    • 20144366153 scopus 로고    scopus 로고
    • Identification of a new membrane-associated protein that influences transport/maturation of gingipains and adhesins of Porphyromonas gingivalis
    • Sato K, Sakai E, Veith PD, Shoji M, Kikuchi Y, Yukitake H, et al. Identification of a new membrane-associated protein that influences transport/maturation of gingipains and adhesins of Porphyromonas gingivalis. J Biol Chem. 2005;280: 8668–8677. 15634642
    • (2005) J Biol Chem , vol.280 , pp. 8668-8677
    • Sato, K.1    Sakai, E.2    Veith, P.D.3    Shoji, M.4    Kikuchi, Y.5    Yukitake, H.6
  • 21
    • 79951811721 scopus 로고    scopus 로고
    • The outer membrane protein LptO is essential for the O-deacylation of LPS and the co-ordinated secretion and attachment of A-LPS and CTD proteins in Porphyromonas gingivalis
    • Chen YY, Peng B, Yang Q, Glew MD, Veith PD, Cross KJ, et al. The outer membrane protein LptO is essential for the O-deacylation of LPS and the co-ordinated secretion and attachment of A-LPS and CTD proteins in Porphyromonas gingivalis. Mol Microbiol. 2011;79: 1380–1401. doi: 10.1111/j.1365-2958.2010.07530.x 21244528
    • (2011) Mol Microbiol , vol.79 , pp. 1380-1401
    • Chen, Y.Y.1    Peng, B.2    Yang, Q.3    Glew, M.D.4    Veith, P.D.5    Cross, K.J.6
  • 22
    • 60349097303 scopus 로고    scopus 로고
    • PG27 is a novel membrane protein essential for a Porphyromonas gingivalis protease secretion system
    • Ishiguro I, Saiki K, Konishi K, PG27 is a novel membrane protein essential for a Porphyromonas gingivalis protease secretion system. FEMS Microbiol Lett. 2009;292: 261–267. doi: 10.1111/j.1574-6968.2009.01489.x 19187201
    • (2009) FEMS Microbiol Lett , vol.292 , pp. 261-267
    • Ishiguro, I.1    Saiki, K.2    Konishi, K.3
  • 23
    • 34249023943 scopus 로고    scopus 로고
    • Identification of a Porphyromonas gingivalis novel protein sov required for the secretion of gingipains
    • Saiki K, Konishi K, Identification of a Porphyromonas gingivalis novel protein sov required for the secretion of gingipains. Microbiol Immunol. 2007;51: 483–491. 17579257
    • (2007) Microbiol Immunol , vol.51 , pp. 483-491
    • Saiki, K.1    Konishi, K.2
  • 24
    • 84897923160 scopus 로고    scopus 로고
    • Identification of an O-antigen chain length regulator, WzzP, in Porphyromonas gingivalis
    • Shoji M, Yukitake H, Sato K, Shibata Y, Naito M, Aduse-Opoku J, et al. Identification of an O-antigen chain length regulator, WzzP, in Porphyromonas gingivalis. Microbiologyopen. 2013;2: 383–401. doi: 10.1002/mbo3.84 23509024
    • (2013) Microbiologyopen , vol.2 , pp. 383-401
    • Shoji, M.1    Yukitake, H.2    Sato, K.3    Shibata, Y.4    Naito, M.5    Aduse-Opoku, J.6
  • 25
    • 67749117911 scopus 로고    scopus 로고
    • Structural analysis of the core region of O-lipopolysaccharide of Porphyromonas gingivalis from mutants defective in O-antigen ligase and O-antigen polymerase
    • Paramonov NA, Aduse-Opoku J, Hashim A, Rangarajan M, Curtis MA, Structural analysis of the core region of O-lipopolysaccharide of Porphyromonas gingivalis from mutants defective in O-antigen ligase and O-antigen polymerase. J Bacteriol. 2009;191: 5272–5282. doi: 10.1128/JB.00019-09 19525343
    • (2009) J Bacteriol , vol.191 , pp. 5272-5282
    • Paramonov, N.A.1    Aduse-Opoku, J.2    Hashim, A.3    Rangarajan, M.4    Curtis, M.A.5
  • 26
    • 77956633373 scopus 로고    scopus 로고
    • A Porphyromonas gingivalis mutant defective in a putative glycosyltransferase exhibits defective biosynthesis of the polysaccharide portions of lipopolysaccharide, decreased gingipain activities, strong autoaggregation, and increased biofilm formation
    • Yamaguchi M, Sato K, Yukitake H, Noiri Y, Ebisu S, Nakayama K, A Porphyromonas gingivalis mutant defective in a putative glycosyltransferase exhibits defective biosynthesis of the polysaccharide portions of lipopolysaccharide, decreased gingipain activities, strong autoaggregation, and increased biofilm formation. Infect Immun. 2010;78: 3801–3812. doi: 10.1128/IAI.00071-10 20624909
    • (2010) Infect Immun , vol.78 , pp. 3801-3812
    • Yamaguchi, M.1    Sato, K.2    Yukitake, H.3    Noiri, Y.4    Ebisu, S.5    Nakayama, K.6
  • 27
    • 21544450833 scopus 로고    scopus 로고
    • Inactivation of vimF, a putative glycosyltransferase gene downstream of vimE, alters glycosylation and activation of the gingipains in Porphyromonas gingivalis W83
    • Vanterpool E, Roy F, Fletcher HM, Inactivation of vimF, a putative glycosyltransferase gene downstream of vimE, alters glycosylation and activation of the gingipains in Porphyromonas gingivalis W83. Infect Immun. 2005;73: 3971–3982. 15972484
    • (2005) Infect Immun , vol.73 , pp. 3971-3982
    • Vanterpool, E.1    Roy, F.2    Fletcher, H.M.3
  • 28
    • 15544371631 scopus 로고    scopus 로고
    • Altered gingipain maturation in vimA- and vimE-defective isogenic mutants of Porphyromonas gingivalis
    • Vanterpool E, Roy F, Sandberg L, Fletcher HM, Altered gingipain maturation in vimA- and vimE-defective isogenic mutants of Porphyromonas gingivalis. Infect Immun. 2005;73: 1357–1366. 15731033
    • (2005) Infect Immun , vol.73 , pp. 1357-1366
    • Vanterpool, E.1    Roy, F.2    Sandberg, L.3    Fletcher, H.M.4
  • 29
    • 33748078137 scopus 로고    scopus 로고
    • Mechanisms of resistance of Porphyromonas gingivalis to killing by serum complement
    • Slaney JM, Gallagher A, Aduse-Opoku J, Pell K, Curtis MA, Mechanisms of resistance of Porphyromonas gingivalis to killing by serum complement. Infect Immun. 2006;74: 5352–5361. 16926430
    • (2006) Infect Immun , vol.74 , pp. 5352-5361
    • Slaney, J.M.1    Gallagher, A.2    Aduse-Opoku, J.3    Pell, K.4    Curtis, M.A.5
  • 30
    • 33750435921 scopus 로고    scopus 로고
    • Porphyromonas gingivalis galE is involved in lipopolysaccharide O-antigen synthesis and biofilm formation
    • Nakao R, Senpuku H, Watanabe H, Porphyromonas gingivalis galE is involved in lipopolysaccharide O-antigen synthesis and biofilm formation. Infect Immun. 2006;74: 6145–6153. 16954395
    • (2006) Infect Immun , vol.74 , pp. 6145-6153
    • Nakao, R.1    Senpuku, H.2    Watanabe, H.3
  • 32
    • 0033121176 scopus 로고    scopus 로고
    • Characterization of a Porphyromonas gingivalis gene prtK that encodes a lysine-specific cysteine proteinase and three sequence-related adhesins
    • Slakeski N, Cleal SM, Bhogal PS, Reynolds EC, Characterization of a Porphyromonas gingivalis gene prtK that encodes a lysine-specific cysteine proteinase and three sequence-related adhesins. Oral Microbiol Immunol. 1999;14: 92–97. 10219167
    • (1999) Oral Microbiol Immunol , vol.14 , pp. 92-97
    • Slakeski, N.1    Cleal, S.M.2    Bhogal, P.S.3    Reynolds, E.C.4
  • 34
    • 63449142077 scopus 로고    scopus 로고
    • Response of Porphyromonas gingivalis to heme limitation in continuous culture
    • Dashper SG, Ang CS, Veith PD, Mitchell HL, Lo AW, Seers CA, et al. Response of Porphyromonas gingivalis to heme limitation in continuous culture. J Bacteriol. 2009;191: 1044–1055. doi: 10.1128/JB.01270-08 19028886
    • (2009) J Bacteriol , vol.191 , pp. 1044-1055
    • Dashper, S.G.1    Ang, C.S.2    Veith, P.D.3    Mitchell, H.L.4    Lo, A.W.5    Seers, C.A.6
  • 35
    • 84899842537 scopus 로고    scopus 로고
    • Porphyromonas gingivalis outer membrane vesicles exclusively contain outer membrane and periplasmic proteins and carry a cargo enriched with virulence factors
    • Veith PD, Chen YY, Gorasia DG, Chen D, Glew MD, O'Brien-Simpson NM, et al. Porphyromonas gingivalis outer membrane vesicles exclusively contain outer membrane and periplasmic proteins and carry a cargo enriched with virulence factors. J Proteome Res. 2014.
    • (2014) J Proteome Res
    • Veith, P.D.1    Chen, Y.Y.2    Gorasia, D.G.3    Chen, D.4    Glew, M.D.5    O'Brien-Simpson, N.M.6
  • 37
    • 77949587649 scopus 로고    scopus 로고
    • Fast and accurate long-read alignment with Burrows-Wheeler transform
    • Li H, Durbin R, Fast and accurate long-read alignment with Burrows-Wheeler transform. Bioinformatics. 2010;26: 589–595. doi: 10.1093/bioinformatics/btp698 20080505
    • (2010) Bioinformatics , vol.26 , pp. 589-595
    • Li, H.1    Durbin, R.2
  • 38
    • 68549104404 scopus 로고    scopus 로고
    • The Sequence Alignment/Map format and SAMtools
    • Li H, Handsaker B, Wysoker A, Fennell T, Ruan J, Homer N, et al. The Sequence Alignment/Map format and SAMtools. Bioinformatics. 2009;25: 2078–2079. doi: 10.1093/bioinformatics/btp352 19505943
    • (2009) Bioinformatics , vol.25 , pp. 2078-2079
    • Li, H.1    Handsaker, B.2    Wysoker, A.3    Fennell, T.4    Ruan, J.5    Homer, N.6
  • 39
    • 84943518295 scopus 로고    scopus 로고
    • Garrison E, Marth, G. Haplotype-based variant detection from short-read sequencing2012.
  • 40
    • 77955801615 scopus 로고    scopus 로고
    • Galaxy: a comprehensive approach for supporting accessible, reproducible, and transparent computational research in the life sciences
    • Goecks J, Nekrutenko A, Taylor J, Galaxy: a comprehensive approach for supporting accessible, reproducible, and transparent computational research in the life sciences. Genome Biol. 2010;11: R86. doi: 10.1186/gb-2010-11-8-r86 20738864
    • (2010) Genome Biol , vol.11 , pp. 86
    • Goecks, J.1    Nekrutenko, A.2    Taylor, J.3
  • 43
    • 0026733421 scopus 로고
    • A comparison between low background silver diammine and silver nitrate protein stains
    • Rabilloud T, A comparison between low background silver diammine and silver nitrate protein stains. Electrophoresis. 1992;13: 429–439. 1425556
    • (1992) Electrophoresis , vol.13 , pp. 429-439
    • Rabilloud, T.1
  • 44
    • 0028603364 scopus 로고
    • Sample application by in-gel rehydration improves the resolution of two-dimensional electrophoresis with immobilized pH gradients in the first dimension
    • Rabilloud T, Valette C, Lawrence JJ, Sample application by in-gel rehydration improves the resolution of two-dimensional electrophoresis with immobilized pH gradients in the first dimension. Electrophoresis. 1994;15: 1552–1558. 7536671
    • (1994) Electrophoresis , vol.15 , pp. 1552-1558
    • Rabilloud, T.1    Valette, C.2    Lawrence, J.J.3
  • 45
    • 84875123279 scopus 로고    scopus 로고
    • Liquid chromatography quadrupole time-of-flight mass spectrometry characterization of metabolites guided by the METLIN database
    • Zhu ZJ, Schultz AW, Wang J, Johnson CH, Yannone SM, Patti GJ, et al. Liquid chromatography quadrupole time-of-flight mass spectrometry characterization of metabolites guided by the METLIN database. Nat Protoc. 2013;8: 451–460. doi: 10.1038/nprot.2013.004 23391889
    • (2013) Nat Protoc , vol.8 , pp. 451-460
    • Zhu, Z.J.1    Schultz, A.W.2    Wang, J.3    Johnson, C.H.4    Yannone, S.M.5    Patti, G.J.6
  • 46
    • 0030925556 scopus 로고    scopus 로고
    • Biochemical characterization of the arginine-specific proteases of Porphyromonas gingivalis W50 suggests a common precursor
    • Rangarajan M, Smith SJ, U S, Curtis MA, Biochemical characterization of the arginine-specific proteases of Porphyromonas gingivalis W50 suggests a common precursor. Biochem J. 1997;323 (Pt 3): 701–709. 9169603
    • (1997) Biochem J , vol.323 , pp. 701-709
    • Rangarajan, M.1    Smith, S.J.2    Curtis, M.A.3
  • 47
    • 0032080290 scopus 로고    scopus 로고
    • The periodontopathogen Porphyromonas gingivalis binds iron protoporphyrin IX in the mu-oxo dimeric form: an oxidative buffer and possible pathogenic mechanism
    • Smalley JW, Silver J, Marsh PJ, Birss AJ, The periodontopathogen Porphyromonas gingivalis binds iron protoporphyrin IX in the mu-oxo dimeric form: an oxidative buffer and possible pathogenic mechanism. Biochem J. 1998;331 (Pt 3): 681–685. 9560292
    • (1998) Biochem J , vol.331 , pp. 681-685
    • Smalley, J.W.1    Silver, J.2    Marsh, P.J.3    Birss, A.J.4
  • 48
    • 2542570174 scopus 로고    scopus 로고
    • A combination of both arginine- and lysine-specific gingipain activity of Porphyromonas gingivalis is necessary for the generation of the micro-oxo bishaem-containing pigment from haemoglobin
    • Smalley JW, Thomas MF, Birss AJ, Withnall R, Silver J, A combination of both arginine- and lysine-specific gingipain activity of Porphyromonas gingivalis is necessary for the generation of the micro-oxo bishaem-containing pigment from haemoglobin. Biochem J. 2004;379: 833–840. 14741050
    • (2004) Biochem J , vol.379 , pp. 833-840
    • Smalley, J.W.1    Thomas, M.F.2    Birss, A.J.3    Withnall, R.4    Silver, J.5
  • 49
    • 84901370340 scopus 로고    scopus 로고
    • Involvement of the Wbp pathway in the biosynthesis of Porphyromonas gingivalis lipopolysaccharide with anionic polysaccharide
    • Shoji M, Sato K, Yukitake H, Naito M, Nakayama K, Involvement of the Wbp pathway in the biosynthesis of Porphyromonas gingivalis lipopolysaccharide with anionic polysaccharide. Sci Rep. 2014;4: 5056. doi: 10.1038/srep05056 24852504
    • (2014) Sci Rep , vol.4 , pp. 5056
    • Shoji, M.1    Sato, K.2    Yukitake, H.3    Naito, M.4    Nakayama, K.5
  • 50
    • 0033607265 scopus 로고    scopus 로고
    • Purification and characterization of sortase, the transpeptidase that cleaves surface proteins of Staphylococcus aureus at the LPXTG motif
    • Ton-That H, Liu G, Mazmanian SK, Faull KF, Schneewind O, Purification and characterization of sortase, the transpeptidase that cleaves surface proteins of Staphylococcus aureus at the LPXTG motif. Proc Natl Acad Sci U S A. 1999;96: 12424–12429. 10535938
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 12424-12429
    • Ton-That, H.1    Liu, G.2    Mazmanian, S.K.3    Faull, K.F.4    Schneewind, O.5
  • 51
    • 84883181202 scopus 로고    scopus 로고
    • Sequence-independent processing site of the C-terminal domain (CTD) influences maturation of the RgpB protease from Porphyromonas gingivalis
    • Zhou XY, Gao JL, Hunter N, Potempa J, Nguyen KA, Sequence-independent processing site of the C-terminal domain (CTD) influences maturation of the RgpB protease from Porphyromonas gingivalis. Mol Microbiol. 2013;89: 903–917. doi: 10.1111/mmi.12319 23869473
    • (2013) Mol Microbiol , vol.89 , pp. 903-917
    • Zhou, X.Y.1    Gao, J.L.2    Hunter, N.3    Potempa, J.4    Nguyen, K.A.5
  • 52
    • 79959385024 scopus 로고    scopus 로고
    • Por secretion system-dependent secretion and glycosylation of Porphyromonas gingivalis hemin-binding protein 35
    • Shoji M, Sato K, Yukitake H, Kondo Y, Narita Y, Kadowaki T, et al. Por secretion system-dependent secretion and glycosylation of Porphyromonas gingivalis hemin-binding protein 35. PLoS One. 2011;6: e21372. doi: 10.1371/journal.pone.0021372 21731719
    • (2011) PLoS One , vol.6
    • Shoji, M.1    Sato, K.2    Yukitake, H.3    Kondo, Y.4    Narita, Y.5    Kadowaki, T.6
  • 53
    • 0032969566 scopus 로고    scopus 로고
    • Surface proteins of gram-positive bacteria and mechanisms of their targeting to the cell wall envelope
    • Navarre WW, Schneewind O, Surface proteins of gram-positive bacteria and mechanisms of their targeting to the cell wall envelope. Microbiol Mol Biol Rev. 1999;63: 174–229. 10066836
    • (1999) Microbiol Mol Biol Rev , vol.63 , pp. 174-229
    • Navarre, W.W.1    Schneewind, O.2
  • 54
    • 0027992980 scopus 로고
    • Proteolytic cleavage and cell wall anchoring at the LPXTG motif of surface proteins in gram-positive bacteria
    • Navarre WW, Schneewind O, Proteolytic cleavage and cell wall anchoring at the LPXTG motif of surface proteins in gram-positive bacteria. Mol Microbiol. 1994;14: 115–121. 7830549
    • (1994) Mol Microbiol , vol.14 , pp. 115-121
    • Navarre, W.W.1    Schneewind, O.2
  • 55
    • 84928539002 scopus 로고    scopus 로고
    • Identification of the linkage between A-polysaccharide and the core in the A-lipopolysaccharide of Porphyromonas gingivalis W50
    • Paramonov N, Aduse-Opoku J, Hashim A, Rangarajan M, Curtis MA, Identification of the linkage between A-polysaccharide and the core in the A-lipopolysaccharide of Porphyromonas gingivalis W50. J Bacteriol. 2015;197: 1735–1746. doi: 10.1128/JB.02562-14 25733619
    • (2015) J Bacteriol , vol.197 , pp. 1735-1746
    • Paramonov, N.1    Aduse-Opoku, J.2    Hashim, A.3    Rangarajan, M.4    Curtis, M.A.5
  • 56
    • 0033570275 scopus 로고    scopus 로고
    • Crystal structure of gingipain R: an Arg-specific bacterial cysteine proteinase with a caspase-like fold
    • Eichinger A, Beisel HG, Jacob U, Huber R, Medrano FJ, Banbula A, et al. Crystal structure of gingipain R: an Arg-specific bacterial cysteine proteinase with a caspase-like fold. EMBO J. 1999;18: 5453–5462. 10523290
    • (1999) EMBO J , vol.18 , pp. 5453-5462
    • Eichinger, A.1    Beisel, H.G.2    Jacob, U.3    Huber, R.4    Medrano, F.J.5    Banbula, A.6
  • 57
    • 3543073805 scopus 로고    scopus 로고
    • Crystal structures of Staphylococcus aureus sortase A and its substrate complex
    • Zong Y, Bice TW, Ton-That H, Schneewind O, Narayana SV, Crystal structures of Staphylococcus aureus sortase A and its substrate complex. J Biol Chem. 2004;279: 31383–31389. 15117963
    • (2004) J Biol Chem , vol.279 , pp. 31383-31389
    • Zong, Y.1    Bice, T.W.2    Ton-That, H.3    Schneewind, O.4    Narayana, S.V.5
  • 58
    • 84883428060 scopus 로고    scopus 로고
    • Site-specific C-terminal and internal loop labeling of proteins using sortase-mediated reactions
    • Guimaraes CP, Witte MD, Theile CS, Bozkurt G, Kundrat L, Blom AE, et al. Site-specific C-terminal and internal loop labeling of proteins using sortase-mediated reactions. Nat Protoc. 2013;8: 1787–1799. doi: 10.1038/nprot.2013.101 23989673
    • (2013) Nat Protoc , vol.8 , pp. 1787-1799
    • Guimaraes, C.P.1    Witte, M.D.2    Theile, C.S.3    Bozkurt, G.4    Kundrat, L.5    Blom, A.E.6
  • 59
    • 0034737451 scopus 로고    scopus 로고
    • Anchoring of surface proteins to the cell wall of Staphylococcus aureus. Sortase catalyzed in vitro transpeptidation reaction using LPXTG peptide and NH(2)-Gly(3) substrates
    • Ton-That H, Mazmanian SK, Faull KF, Schneewind O, Anchoring of surface proteins to the cell wall of Staphylococcus aureus. Sortase catalyzed in vitro transpeptidation reaction using LPXTG peptide and NH(2)-Gly(3) substrates. J Biol Chem. 2000;275: 9876–9881. 10734144
    • (2000) J Biol Chem , vol.275 , pp. 9876-9881
    • Ton-That, H.1    Mazmanian, S.K.2    Faull, K.F.3    Schneewind, O.4


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