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Volumn 17, Issue 10, 2013, Pages 527-535

Extracellular Proteome Analysis of Leptospira interrogans serovar Lai

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; PROTEOME;

EID: 84884768623     PISSN: 15362310     EISSN: 15578100     Source Type: Journal    
DOI: 10.1089/omi.2013.0043     Document Type: Article
Times cited : (26)

References (57)
  • 1
    • 80052541260 scopus 로고    scopus 로고
    • Pathogenesis of leptospirosis: The influence of genomics
    • Adler B, Lo M, Seemann T, and Murray GL. (2011). Pathogenesis of leptospirosis: The influence of genomics. Vet Microbiol 153, 73-81.
    • (2011) Vet Microbiol , vol.153 , pp. 73-81
    • Adler, B.1    Lo, M.2    Seemann, T.3    Murray, G.L.4
  • 4
    • 0018181089 scopus 로고
    • Protein-free and low-protein media for the cultivation of Leptospira
    • Bey RF, and Johnson RC. (1978). Protein-free and low-protein media for the cultivation of Leptospira. Infect Immun 19, 562-569. (Pubitemid 8291075)
    • (1978) Infection and Immunity , vol.19 , Issue.2 , pp. 562-569
    • Bey, R.F.1    Johnson, R.C.2
  • 6
    • 76449114765 scopus 로고    scopus 로고
    • High-coverage proteome analysis reveals the first insight of protein modification systems in the pathogenic spirochete Leptospira interrogans
    • Cao XJ, Dai J, Xu H, et al. (2010). High-coverage proteome analysis reveals the first insight of protein modification systems in the pathogenic spirochete Leptospira interrogans. Cell Res 20, 197-210.
    • (2010) Cell Res , vol.20 , pp. 197-210
    • Cao, X.J.1    Dai, J.2    Xu, H.3
  • 7
    • 80052542448 scopus 로고    scopus 로고
    • Identification of candidate host proteins that interact with LipL32, the major outer membrane protein of pathogenic Leptospira, by random phage display peptide library
    • Chaemchuen S, Rungpragayphan S, Poovorawan Y, and Patarakul K. (2011). Identification of candidate host proteins that interact with LipL32, the major outer membrane protein of pathogenic Leptospira, by random phage display peptide library. Vet Microbiol 153, 178-185.
    • (2011) Vet Microbiol , vol.153 , pp. 178-185
    • Chaemchuen, S.1    Rungpragayphan, S.2    Poovorawan, Y.3    Patarakul, K.4
  • 8
    • 38749140290 scopus 로고    scopus 로고
    • Peroxiredoxins in bacterial antioxidant defense
    • Dubbs JM, and Mongkolsuk S. (2007). Peroxiredoxins in bacterial antioxidant defense. SubCell Biochem 44, 143-193.
    • (2007) SubCell Biochem , vol.44 , pp. 143-193
    • Dubbs, J.M.1    Mongkolsuk, S.2
  • 9
    • 0004169519 scopus 로고
    • 1st ed. CRC Press, the Chemical Rubber Company Press, Boca Raton, FL)
    • Faine S. (1994). Leptospira and Leptospirosis. 1st ed. (CRC Press, the Chemical Rubber Company Press, Boca Raton, FL).
    • (1994) Leptospira and Leptospirosis
    • Faine, S.1
  • 11
    • 0034918895 scopus 로고    scopus 로고
    • Stress-induced ClpP serine protease of Listeria monocytogenes is essential for induction of listeriolysin O-dependent protective immunity
    • DOI 10.1128/IAI.69.8.4938-4943.2001
    • Gaillot O, Bregenholt S, Jaubert F, Di Santo JP, and Berche P. (2001). Stress-induced ClpP serine protease of Listeria monocytogenes is essential for induction of listeriolysin Odependent protective immunity. Infect Immun 69, 4938-4943. (Pubitemid 32674476)
    • (2001) Infection and Immunity , vol.69 , Issue.8 , pp. 4938-4943
    • Gaillot, O.1    Bregenholt, S.2    Jaubert, F.3    Di Santo, J.P.4    Berche, P.5
  • 13
    • 0036716467 scopus 로고    scopus 로고
    • Characterization of the leptospiral outer membrane and description of three novel leptospiral membrane proteins
    • Haake DA, and Matsunaga J. (2002). Characterization of the leptospiral outer membrane and description of three novel leptospiral membrane proteins. Infect Immun 70, 4936-4945.
    • (2002) Infect Immun , vol.70 , pp. 4936-4945
    • Haake, D.A.1    Matsunaga, J.2
  • 14
    • 78149443620 scopus 로고    scopus 로고
    • Bacterial contactdependent delivery systems
    • Hayes CS, Aoki SK, and Low DA. (2010). Bacterial contactdependent delivery systems. Annu Rev Genet 44, 71-90.
    • (2010) Annu Rev Genet , vol.44 , pp. 71-90
    • Hayes, C.S.1    Aoki, S.K.2    Low, D.A.3
  • 15
    • 85085674550 scopus 로고    scopus 로고
    • Recognizing risks and potential promise of germline engineering
    • Hesterlee SE. (2001). Recognizing risks and potential promise of germline engineering. Nature 414, 15.
    • (2001) Nature , vol.414 , pp. 15
    • Hesterlee, S.E.1
  • 16
    • 42949159838 scopus 로고    scopus 로고
    • LipL32 is an extracellular matrix-interacting protein of Leptospira spp. and Pseudoalteromonas tunicata
    • DOI 10.1128/IAI.01643-07
    • Hoke DE, Egan S, Cullen PA, and Adler B. (2008). LipL32 is an extracellular matrix-interacting protein of Leptospira spp. and Pseudoalteromonas tunicata. Infect Immun 76, 2063-2069. (Pubitemid 351656139)
    • (2008) Infection and Immunity , vol.76 , Issue.5 , pp. 2063-2069
    • Hoke, D.E.1    Egan, S.2    Cullen, P.A.3    Adler, B.4
  • 17
    • 59449110078 scopus 로고    scopus 로고
    • SOSUI-GramN: High performance prediction for sub-cellular localization of proteins in gram-negative bacteria
    • Imai K, Asakawa N, Tsuji T, et al. (2008). SOSUI-GramN: High performance prediction for sub-cellular localization of proteins in gram-negative bacteria. Bioinformation 2, 417-421.
    • (2008) Bioinformation , vol.2 , pp. 417-421
    • Imai, K.1    Asakawa, N.2    Tsuji, T.3
  • 18
    • 0041341888 scopus 로고    scopus 로고
    • Prediction of lipoprotein signal peptides in Gram-negative bacteria
    • DOI 10.1110/ps.0303703
    • Juncker AS, Willenbrock H, Von Heijne G, Brunak S, Nielsen H, and Krogh A. (2003). Prediction of lipoprotein signal peptides in Gram-negative bacteria. Protein Sci 12, 1652-1662. (Pubitemid 36910046)
    • (2003) Protein Science , vol.12 , Issue.8 , pp. 1652-1662
    • Juncker, A.S.1    Willenbrock, H.2    Von Heijne, G.3    Brunak, S.4    Nielsen, H.5    Krogh, A.6
  • 20
    • 0034442652 scopus 로고    scopus 로고
    • Identification and immunogenicity of group A Streptococcus culture supernatant proteins
    • DOI 10.1128/IAI.68.12.6807-6818.2000
    • Lei B, Mackie S, Lukomski S, and Musser JM. (2000). Identification and immunogenicity of group A Streptococcus culture supernatant proteins. Infect Immun 68, 6807-6818. (Pubitemid 32463388)
    • (2000) Infection and Immunity , vol.68 , Issue.12 , pp. 6807-6818
    • Lei, B.1    Mackie, S.2    Lukomski, S.3    Musser, J.M.4
  • 21
    • 58149203237 scopus 로고    scopus 로고
    • CDD: Specific functional annotation with the Conserved Domain Database
    • Marchler-Bauer A, Anderson JB, Chitsaz F, et al. (2009). CDD: Specific functional annotation with the Conserved Domain Database. Nucleic Acids Res 37, D205-210.
    • (2009) Nucleic Acids Res , vol.37
    • Marchler-Bauer, A.1    Anderson, J.B.2    Chitsaz, F.3
  • 22
    • 3242887157 scopus 로고    scopus 로고
    • CD-Search: Protein domain annotations on the fly
    • DOI 10.1093/nar/gkh454
    • Marchler-Bauer A, and Bryant SH. (2004). CD-Search: Protein domain annotations on the fly. Nucleic Acids Res 32, W327-331. (Pubitemid 38997352)
    • (2004) Nucleic Acids Research , vol.32 , Issue.WEB SERVER ISSUE
    • Marchler-Bauer, A.1    Bryant, S.H.2
  • 23
    • 78651285748 scopus 로고    scopus 로고
    • CDD: A Conserved Domain Database for the functional annotation of proteins
    • Marchler-Bauer A, Lu S, Anderson JB, et al. (2011). CDD: A Conserved Domain Database for the functional annotation of proteins. Nucleic Acids Res 39, D225-229.
    • (2011) Nucleic Acids Res , vol.39
    • Marchler-Bauer, A.1    Lu, S.2    Anderson, J.B.3
  • 24
    • 84866175144 scopus 로고    scopus 로고
    • Differential in vivo gene expression of major Leptospira proteins in resistant or susceptible animal models
    • Matsui M, Soupe ME, Becam J, and Goarant C. (2012). Differential in vivo gene expression of major Leptospira proteins in resistant or susceptible animal models. Appl Environ Microbiol 78, 6372-6376.
    • (2012) Appl Environ Microbiol , vol.78 , pp. 6372-6376
    • Matsui, M.1    Soupe, M.E.2    Becam, J.3    Goarant, C.4
  • 26
    • 62449313550 scopus 로고    scopus 로고
    • Major surface protein LipL32 is not required for either acute or chronic infection with Leptospira interrogans
    • Murray GL, Srikram A, Hoke DE, et al. (2009). Major surface protein LipL32 is not required for either acute or chronic infection with Leptospira interrogans. Infect Immun 77, 952-958.
    • (2009) Infect Immun , vol.77 , pp. 952-958
    • Murray, G.L.1    Srikram, A.2    Hoke, D.E.3
  • 27
    • 80054745109 scopus 로고    scopus 로고
    • Comparative proteomic analysis of differentially expressed proteins in the urine of reservoir hosts of leptospirosis
    • Nally JE, Monahan AM, Miller IS, Bonilla-Santiago R, Souda P, and Whitelegge JP. (2011). Comparative proteomic analysis of differentially expressed proteins in the urine of reservoir hosts of leptospirosis. PLoS ONE 6, e26046.
    • (2011) PLoS ONE , vol.6
    • Nally, J.E.1    Monahan, A.M.2    Miller, I.S.3    Bonilla-Santiago, R.4    Souda, P.5    Whitelegge, J.P.6
  • 28
    • 0035158941 scopus 로고    scopus 로고
    • Temperature-regulated protein synthesis by Leptospira interrogans
    • DOI 10.1128/IAI.69.1.400-404.2001
    • Nally JE, Timoney JF, and Stevenson B. (2001). Temperatureregulated protein synthesis by Leptospira interrogans. Infect Immun 69, 400-404. (Pubitemid 32038338)
    • (2001) Infection and Immunity , vol.69 , Issue.1 , pp. 400-404
    • Nally, J.E.1    Timoney, J.F.2    Stevenson, B.3
  • 30
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen H, Engelbrecht J, Brunak S, and Von Heijne G. (1997). Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng 10, 1-6.
    • (1997) Protein Eng , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    Von Heijne, G.4
  • 31
    • 78650027203 scopus 로고    scopus 로고
    • The critical role of S-lactoylglutathione formation during methylglyoxal detoxification in Escherichia coli
    • Ozyamak E, Black SS, Walker CA, et al. (2010). The critical role of S-lactoylglutathione formation during methylglyoxal detoxification in Escherichia coli. Mol Microbiol 78, 1577-1590.
    • (2010) Mol Microbiol , vol.78 , pp. 1577-1590
    • Ozyamak, E.1    Black, S.S.2    Walker, C.A.3
  • 32
    • 43249088695 scopus 로고    scopus 로고
    • Genome sequence of the saprophyte Leptospira biflexa provides insights into the evolution of Leptospira and the pathogenesis of leptospirosis
    • Picardeau M, Bulach DM, Bouchier C, et al. (2008). Genome sequence of the saprophyte Leptospira biflexa provides insights into the evolution of Leptospira and the pathogenesis of leptospirosis. PLoS ONE 3, e1607.
    • (2008) PLoS ONE , vol.3
    • Picardeau, M.1    Bulach, D.M.2    Bouchier, C.3
  • 33
    • 78149244223 scopus 로고    scopus 로고
    • The OmpL37 surface-exposed protein is expressed by pathogenic Leptospira during infection and binds skin and vascular elastin
    • Pinne M, Choy HA, and Haake DA. (2010). The OmpL37 surface-exposed protein is expressed by pathogenic Leptospira during infection and binds skin and vascular elastin. PLoS Negl Trop Dis 4, e815.
    • (2010) PLoS Negl Trop Dis , vol.4
    • Pinne, M.1    Choy, H.A.2    Haake, D.A.3
  • 34
    • 84860561026 scopus 로고    scopus 로고
    • Detection of Helicobacter pylori in bovine, buffalo, camel, ovine, and caprine milk in Iran
    • Rahimi E, and Kheirabadi EK. (2012). Detection of Helicobacter pylori in bovine, buffalo, camel, ovine, and caprine milk in Iran. Foodborne Pathog Dis 9, 453-456.
    • (2012) Foodborne Pathog Dis , vol.9 , pp. 453-456
    • Rahimi, E.1    Kheirabadi, E.K.2
  • 36
    • 34547645283 scopus 로고    scopus 로고
    • The OmpAlike protein Loa22 is essential for Leptospiral virulence
    • Ristow P, Bourhy P, McBride FWDC, et al. (2007). The OmpAlike protein Loa22 is essential for Leptospiral virulence. PLoS Pathogens 3, e97.
    • (2007) PLoS Pathogens , vol.3
    • Ristow, P.1    Bourhy, P.2    Fwdc, M.3
  • 37
    • 84858049415 scopus 로고    scopus 로고
    • Post-translational modifications of host proteins by Legionella pneumophila: A sophisticated survival strategy
    • Rolando M, and Buchrieser C. (2012). Post-translational modifications of host proteins by Legionella pneumophila: A sophisticated survival strategy. Future Microbiol 7, 369-381.
    • (2012) Future Microbiol , vol.7 , pp. 369-381
    • Rolando, M.1    Buchrieser, C.2
  • 38
    • 34447116519 scopus 로고    scopus 로고
    • Protein secretion and membrane insertion systems in gram-negative bacteria
    • DOI 10.1007/s00232-006-0049-7
    • Saier MH, Jr. (2006). Protein secretion and membrane insertion systems in gram-negative bacteria. J Memb Biol 214, 75-90. (Pubitemid 47036671)
    • (2006) Journal of Membrane Biology , vol.214 , Issue.1-2 , pp. 75-90
    • Saier Jr., M.H.1
  • 40
    • 41649095188 scopus 로고    scopus 로고
    • Immune responses induced by spirochetal outer membrane lipoproteins and glycolipids
    • DOI 10.1016/j.imbio.2007.11.003, PII S0171298507001404
    • Schroder NW, Eckert J, Stubs G, and Schumann RR. (2008). Immune responses induced by spirochetal outer membrane lipoproteins and glycolipids. Immunobiology 213, 329-340. (Pubitemid 351479861)
    • (2008) Immunobiology , vol.213 , Issue.3-4 , pp. 329-340
    • Schroder, N.W.J.1    Eckert, J.2    Stubs, G.3    Schumann, R.R.4
  • 41
    • 30744477217 scopus 로고    scopus 로고
    • Lipoprotein computational prediction in spirochaetal genomes
    • DOI 10.1099/mic.0.28317-0
    • Setubal JC, Reis M, Matsunaga J, and Haake DA. (2006). Lipoprotein computational prediction in spirochaetal genomes. Microbiology 152, 113-121. (Pubitemid 43092399)
    • (2006) Microbiology , vol.152 , Issue.1 , pp. 113-121
    • Setubal, J.C.1    Reis, M.2    Matsunaga, J.3    Haake, D.A.4
  • 42
    • 84860587543 scopus 로고    scopus 로고
    • Bacterial effector interplay: A new way to view effector function
    • Shames SR, and Finlay BB. (2012). Bacterial effector interplay: A new way to view effector function. Trends Microbiol 20, 214-219.
    • (2012) Trends Microbiol , vol.20 , pp. 214-219
    • Shames, S.R.1    Finlay, B.B.2
  • 43
    • 0033842544 scopus 로고    scopus 로고
    • Secretion of virulence determinants by the general secretory pathway in Gram-negative pathogens: An evolving story
    • DOI 10.1016/S1286-4579(00)01260-0
    • Stathopoulos C, Hendrixson DR, Thanassi DG, Hultgren SJ, St Geme JW, 3rd, and Curtiss R, 3rd. (2000). Secretion of virulence determinants by the general secretory pathway in gramnegative pathogens: An evolving story. Microbes Infect 2, 1061-1072. (Pubitemid 30664220)
    • (2000) Microbes and Infection , vol.2 , Issue.9 , pp. 1061-1072
    • Stathopoulos, C.1    Hendrixson, D.R.2    Thanassi, D.G.3    Hultgren, S.J.4    St. Geme III, J.W.5    Curtiss III, R.6
  • 44
    • 43149110212 scopus 로고    scopus 로고
    • Leptospira interrogans endostatin-like outer membrane proteins bind host fibronectin, laminin and regulators of complement
    • Stevenson B, Choy HA, Pinne M, et al. (2007). Leptospira interrogans endostatin-like outer membrane proteins bind host fibronectin, laminin and regulators of complement. PLoS One 2, e1188.
    • (2007) PLoS One , vol.2
    • Stevenson, B.1    Choy, H.A.2    Pinne, M.3
  • 45
    • 0036736598 scopus 로고    scopus 로고
    • ClpP is involved in the stress response and degradation of misfolded proteins in Salmonella enterica serovar Typhimurium
    • Thomsen LE, Olsen JE, Foster JW, and Ingmer H. (2002). ClpP is involved in the stress response and degradation of misfolded proteins in Salmonella enterica serovar Typhimurium. Microbiology 148, 2727-2733.
    • (2002) Microbiology , vol.148 , pp. 2727-2733
    • Thomsen, L.E.1    Olsen, J.E.2    Foster, J.W.3    Ingmer, H.4
  • 46
    • 67651238379 scopus 로고    scopus 로고
    • Analysis of differential proteomes in pathogenic and non-pathogenic Leptospira: Potential pathogenic and virulence factors
    • Thongboonkerd V, Chiangjong W, Saetun P, Sinchaikul S, Chen ST, and Kositanont U. (2009). Analysis of differential proteomes in pathogenic and non-pathogenic Leptospira: potential pathogenic and virulence factors. Proteomics 9, 3522-3534.
    • (2009) Proteomics , vol.9 , pp. 3522-3534
    • Thongboonkerd, V.1    Chiangjong, W.2    Saetun, P.3    Sinchaikul, S.4    Chen, S.T.5    Kositanont, U.6
  • 48
    • 62949245620 scopus 로고    scopus 로고
    • Peroxiredoxins: A less studied component of hydrogen peroxide detoxification in photosynthetic organisms
    • Tripathi BN, Bhatt I, and Dietz KJ. (2009). Peroxiredoxins: A less studied component of hydrogen peroxide detoxification in photosynthetic organisms. Protoplasma 235, 3-15.
    • (2009) Protoplasma , vol.235 , pp. 3-15
    • Tripathi, B.N.1    Bhatt, I.2    Dietz, K.J.3
  • 49
    • 60849116153 scopus 로고    scopus 로고
    • Protein secretion systems in bacterial-host associations, and their description in the Gene Ontology
    • Tseng TT, Tyler BM, and Setubal JC. (2009). Protein secretion systems in bacterial-host associations, and their description in the Gene Ontology. BMC Microbiol 9 Suppl 1, S2.
    • (2009) BMC Microbiol , vol.9 , Issue.SUPPL. 1
    • Tseng, T.T.1    Tyler, B.M.2    Setubal, J.C.3
  • 50
    • 84860479449 scopus 로고    scopus 로고
    • SseF, a type III effector protein from the mammalian pathogen Salmonella enterica, requires resistance-gene-mediated signalling to activate cell death in the model plant Nicotiana benthamiana
    • Ustun S, Muller P, Palmisano R, Hensel M, and Bornke F. (2012). SseF, a type III effector protein from the mammalian pathogen Salmonella enterica, requires resistance-gene-mediated signalling to activate cell death in the model plant Nicotiana benthamiana. New Phytol 194, 1046-1060.
    • (2012) New Phytol , vol.194 , pp. 1046-1060
    • Ustun, S.1    Muller, P.2    Palmisano, R.3    Hensel, M.4    Bornke, F.5
  • 52
    • 44149120513 scopus 로고    scopus 로고
    • Genome-wide subcellular localization of putative outer membrane and extracellular proteins in Leptospira interrogans serovar Lai genome using bioinformatics approaches
    • Viratyosin W, Ingsriswang S, Pacharawongsakda E, and Palittapongarnpim P. (2008). Genome-wide subcellular localization of putative outer membrane and extracellular proteins in Leptospira interrogans serovar Lai genome using bioinformatics approaches. BMC Genom 9, 181.
    • (2008) BMC Genom , vol.9 , pp. 181
    • Viratyosin, W.1    Ingsriswang, S.2    Pacharawongsakda, E.3    Palittapongarnpim, P.4
  • 53
    • 78449242700 scopus 로고    scopus 로고
    • Transcriptional responses of Leptospira interrogans to host innate immunity: Significant changes in metabolism, oxygen tolerance, and outer membrane
    • Xue F, Dong H, Wu J, et al. (2010). Transcriptional responses of Leptospira interrogans to host innate immunity: Significant changes in metabolism, oxygen tolerance, and outer membrane. PLoS Negl Trop Dis 4, e857.
    • (2010) PLoS Negl Trop Dis , vol.4
    • Xue, F.1    Dong, H.2    Wu, J.3
  • 54
    • 62949134757 scopus 로고    scopus 로고
    • Evolution and pathogenesis of Leptospira spp.: Lessons learned from the genomes
    • Xue F, Yan J, and Picardeau M. (2009). Evolution and pathogenesis of Leptospira spp.: Lessons learned from the genomes. Microbes Infect 11, 328-333.
    • (2009) Microbes Infect , vol.11 , pp. 328-333
    • Xue, F.1    Yan, J.2    Picardeau, M.3
  • 55
    • 1942505330 scopus 로고    scopus 로고
    • Predicting subcellular localization of proteins for Gram-negative bacteria by support vector machines based on n-peptide compositions
    • Yu CS, Lin CJ, and Hwang JK. (2004). Predicting subcellular localization of proteins for Gram-negative bacteria by support vector machines based on n-peptide compositions. Protein Sci 13, 1402-1406.
    • (2004) Protein Sci , vol.13 , pp. 1402-1406
    • Yu, C.S.1    Lin, C.J.2    Hwang, J.K.3
  • 56
    • 77954199597 scopus 로고    scopus 로고
    • PSORTb 3.0: Improved protein subcellular localization prediction with refined localization subcategories and predictive capabilities for all prokaryotes
    • Yu NY, Wagner JR, Laird MR, et al. (2010). PSORTb 3.0: Improved protein subcellular localization prediction with refined localization subcategories and predictive capabilities for all prokaryotes. Bioinformatics 26, 1608-1615.
    • (2010) Bioinformatics , vol.26 , pp. 1608-1615
    • Yu, N.Y.1    Wagner, J.R.2    Laird, M.R.3
  • 57
    • 79961209179 scopus 로고    scopus 로고
    • Comparative proteogenomic analysis of the Leptospira interrogans virulenceattenuated strain IPAV against the pathogenic strain 56601
    • Zhong Y, Chang X, Cao XJ, et al. (2011). Comparative proteogenomic analysis of the Leptospira interrogans virulenceattenuated strain IPAV against the pathogenic strain 56601. Cell Res 21, 1210-1229.
    • (2011) Cell Res , vol.21 , pp. 1210-1229
    • Zhong, Y.1    Chang, X.2    Cao, X.J.3


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