메뉴 건너뛰기




Volumn 82, Issue 3, 2014, Pages 1123-1131

High-temperature protein G is an essential virulence factor of Leptospira interrogans

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALS; BACTERIAL PROTEINS; COMPUTATIONAL BIOLOGY; FEMALE; HSP90 HEAT-SHOCK PROTEINS; IMMUNITY, INNATE; LEPTOSPIRA INTERROGANS; LEPTOSPIROSIS; MALE; MESOCRICETUS; MUTATION; OSMOTIC PRESSURE; OXIDATIVE STRESS; TEMPERATURE; VIRULENCE FACTORS;

EID: 84894278483     PISSN: 00199567     EISSN: 10985522     Source Type: Journal    
DOI: 10.1128/IAI.01546-13     Document Type: Article
Times cited : (42)

References (69)
  • 1
    • 73949084950 scopus 로고    scopus 로고
    • Leptospira and leptospirosis
    • Adler B, de la Peña Moctezuma A. 2010. Leptospira and leptospirosis. Vet. Microbiol. 140:287-296. http://dx.doi.org/10.1016/j.vetmic.2009.03 .012.
    • (2010) Vet. Microbiol. , vol.140 , pp. 287-296
    • Adler, B.1    de la Peña Moctezuma, A.2
  • 6
    • 85047688053 scopus 로고    scopus 로고
    • FlaA proteins in Leptospira interrogans are essential for motility and virulence but are not required for formation of the flagellum sheath
    • Lambert A, Picardeau M, Haake DA, Sermswan RW, Srikram A, Adler B, Murray GL. 2012. FlaA proteins in Leptospira interrogans are essential for motility and virulence but are not required for formation of the flagellum sheath. Infect. Immun. 80:2019-2025. http://dx.doi.org/10.1128/IAI .00131-12.
    • (2012) Infect. Immun. , vol.80 , pp. 2019-2025
    • Lambert, A.1    Picardeau, M.2    Haake, D.A.3    Sermswan, R.W.4    Srikram, A.5    Adler, B.6    Murray, G.L.7
  • 7
    • 73449089074 scopus 로고    scopus 로고
    • Inactivation of the fliY gene encoding a flagellar motor switch protein attenuates mobility and virulence of Leptospira interrogans strain Lai
    • Liao S, Sun A, Ojcius DM, Wu S, Zhao J, Yan J. 2009. Inactivation of the fliY gene encoding a flagellar motor switch protein attenuates mobility and virulence of Leptospira interrogans strain Lai. BMC Microbiol. 9:253. http://dx.doi.org/10.1186/1471-2180-9-253.
    • (2009) BMC Microbiol. , vol.9 , pp. 253
    • Liao, S.1    Sun, A.2    Ojcius, D.M.3    Wu, S.4    Zhao, J.5    Yan, J.6
  • 8
    • 80052307960 scopus 로고    scopus 로고
    • Inactivation of clpB in the pathogen Leptospira interrogans reduces virulence and resistance to stress conditions
    • Lourdault K, Cerqueira GM, Wunder EA, Picardeau M. 2011. Inactivation of clpB in the pathogen Leptospira interrogans reduces virulence and resistance to stress conditions. Infect. Immun. 79:3711-3717. http://dx .doi.org/10.1128/IAI.05168-11.
    • (2011) Infect. Immun. , vol.79 , pp. 3711-3717
    • Lourdault, K.1    Cerqueira, G.M.2    Wunder, E.A.3    Picardeau, M.4
  • 9
    • 77958584406 scopus 로고    scopus 로고
    • Mutations affecting Leptospira interrogans lipopolysaccharide attenuate virulence
    • Murray GL, Srikram A, Henry R, Hartskeerl RA, Sermswan RW, Adler B. 2010. Mutations affecting Leptospira interrogans lipopolysaccharide attenuate virulence. Mol. Microbiol. 78:701-709. http://dx.doi.org/10.1111 /j.1365-2958.2010.07360.x.
    • (2010) Mol. Microbiol. , vol.78 , pp. 701-709
    • Murray, G.L.1    Srikram, A.2    Henry, R.3    Hartskeerl, R.A.4    Sermswan, R.W.5    Adler, B.6
  • 10
    • 61449095457 scopus 로고    scopus 로고
    • Leptospira interrogans requires heme oxygenase for disease pathogenesis
    • Murray GL, Srikram A, Henry R, Puapairoj A, Sermswan RW, Adler B.2009. Leptospira interrogans requires heme oxygenase for disease pathogenesis. Microbes Infect. 11:311-314. http://dx.doi.org/10.1016/j.micinf .2008.11.014.
    • (2009) Microbes Infect. , vol.11 , pp. 311-314
    • Murray, G.L.1    Srikram, A.2    Henry, R.3    Puapairoj, A.4    Sermswan, R.W.5    Adler, B.6
  • 12
    • 84862795039 scopus 로고    scopus 로고
    • The mammalian cell entry (Mce) protein of pathogenic Leptospira species is responsible for RGD motif-dependent infection of cells and animals
    • Zhang L, Zhang C, Ojcius DM, Sun D, Zhao J, Lin X, Li L, Li L, Yan J. 2012. The mammalian cell entry (Mce) protein of pathogenic Leptospira species is responsible for RGD motif-dependent infection of cells and animals. Mol. Microbiol. 83:1006-1023. http://dx.doi.org/10.1111/j.1365-2958.2012.07985.x.
    • (2012) Mol. Microbiol. , vol.83 , pp. 1006-1023
    • Zhang, L.1    Zhang, C.2    Ojcius, D.M.3    Sun, D.4    Zhao, J.5    Lin, X.6    Li, L.7    Li, L.8    Yan, J.9
  • 13
    • 17644368883 scopus 로고    scopus 로고
    • Random insertional mutagenesis of Leptospira interrogans, the agent of leptospirosis, using a mariner transposon
    • Bourhy P, Louvel H, Saint Girons I, Picardeau M. 2005. Random insertional mutagenesis of Leptospira interrogans, the agent of leptospirosis, using a mariner transposon. J. Bacteriol. 187:3255-3258. http://dx.doi .org/10.1128/JB.187.9.3255-3258.2005.
    • (2005) J. Bacteriol. , vol.187 , pp. 3255-3258
    • Bourhy, P.1    Louvel, H.2    Saint Girons, I.3    Picardeau, M.4
  • 15
    • 33746364784 scopus 로고    scopus 로고
    • Structure and mechanism of the Hsp90 molecular chaperone machinery
    • Pearl LH, Prodromou C. 2006. Structure and mechanism of the Hsp90 molecular chaperone machinery. Annu. Rev. Biochem. 75:271-294. http: //dx.doi.org/10.1146/annurev.biochem.75.103004.142738.
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 271-294
    • Pearl, L.H.1    Prodromou, C.2
  • 16
    • 2942533020 scopus 로고    scopus 로고
    • The crystal structure of the carboxy-terminal dimerization domain of htpG, the Escherichia coli Hsp90, reveals a potential substrate binding site
    • Harris SF, Shiau AK, Agard DA. 2004. The crystal structure of the carboxy-terminal dimerization domain of htpG, the Escherichia coli Hsp90, reveals a potential substrate binding site. Structure 12:1087-1097. http://dx.doi.org/10.1016/j.str.2004.03.020.
    • (2004) Structure , vol.12 , pp. 1087-1097
    • Harris, S.F.1    Shiau, A.K.2    Agard, D.A.3
  • 17
    • 0031444238 scopus 로고    scopus 로고
    • Identification and structural characterization of the ATP/ADPbinding site in the Hsp90 molecular chaperone
    • Prodromou C, Roe SM, O'Brien R, Ladbury JE, Piper PW, Pearl LH.1997. Identification and structural characterization of the ATP/ADPbinding site in the Hsp90 molecular chaperone. Cell 90:65-75. http://dx .doi.org/10.1016/S0092-8674(00)80314-1.
    • (1997) Cell , vol.90 , pp. 65-75
    • Prodromou, C.1    Roe, S.M.2    O'Brien, R.3    Ladbury, J.E.4    Piper, P.W.5    Pearl, L.H.6
  • 18
    • 49649117517 scopus 로고    scopus 로고
    • The Hsp90 chaperone machinery
    • Wandinger SK, Richter K, Buchner J. 2008. The Hsp90 chaperone machinery. J. Biol. Chem. 283:18473-18477. http://dx.doi.org/10.1074/jbc .R800007200.
    • (2008) J. Biol. Chem. , vol.283 , pp. 18473-18477
    • Wandinger, S.K.1    Richter, K.2    Buchner, J.3
  • 19
    • 17044403753 scopus 로고    scopus 로고
    • Structures of the N-terminal and middle domains of E. coli Hsp90 and conformation changes upon ADP binding
    • Huai Q, Wang H, Liu Y, Kim H-Y, Toft D, Ke H. 2005. Structures of the N-terminal and middle domains of E. coli Hsp90 and conformation changes upon ADP binding. Structure 13:579-590. http://dx.doi.org/10 .1016/j.str.2004.12.018.
    • (2005) Structure , vol.13 , pp. 579-590
    • Huai, Q.1    Wang, H.2    Liu, Y.3    Kim, H.-Y.4    Toft, D.5    Ke, H.6
  • 20
    • 0037352446 scopus 로고    scopus 로고
    • Structural and functional analysis of the middle segment of Hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions
    • Meyer P, Prodromou C, Hu B, Vaughan C, Roe SM, Panaretou B, Piper PW, Pearl LH. 2003. Structural and functional analysis of the middle segment of Hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions. Mol. Cell 11:647-658. http://dx.doi.org/10 .1016/S1097-2765(03)00065-0.
    • (2003) Mol. Cell , vol.11 , pp. 647-658
    • Meyer, P.1    Prodromou, C.2    Hu, B.3    Vaughan, C.4    Roe, S.M.5    Panaretou, B.6    Piper, P.W.7    Pearl, L.H.8
  • 21
    • 0028848373 scopus 로고
    • Mechanism of dimer formation of the 90-kDa heat-shock protein
    • Nemoto T, Ohara-Nemoto Y, Ota M, Takagi T, Yokoyama K. 1995. Mechanism of dimer formation of the 90-kDa heat-shock protein. Eur. J. Biochem. 233:1-8. http://dx.doi.org/10.1111/j.1432-1033.1995.001_1.x.
    • (1995) Eur. J. Biochem. , vol.233 , pp. 1-8
    • Nemoto, T.1    Ohara-Nemoto, Y.2    Ota, M.3    Takagi, T.4    Yokoyama, K.5
  • 23
    • 77951601227 scopus 로고    scopus 로고
    • Bacterial Hsp90-desperately seeking clients
    • Buchner J. 2010. Bacterial Hsp90-desperately seeking clients. Mol. Microbiol. 76:540-544. http://dx.doi.org/10.1111/j.1365-2958.2010.07140.x.
    • (2010) Mol. Microbiol. , vol.76 , pp. 540-544
    • Buchner, J.1
  • 24
    • 77951610740 scopus 로고    scopus 로고
    • HtpG, the prokaryotic homologue of Hsp90, stabilizes a phycobilisome protein in the cyanobacterium Synechococcus elongatus PCC 7942
    • Sato T, Minagawa S, Kojima E, Okamoto N, Nakamoto H. 2010. HtpG, the prokaryotic homologue of Hsp90, stabilizes a phycobilisome protein in the cyanobacterium Synechococcus elongatus PCC 7942. Mol. Microbiol. 76:576-589. http://dx.doi.org/10.1111/j.1365-2958.2010.07139.x.
    • (2010) Mol. Microbiol. , vol.76 , pp. 576-589
    • Sato, T.1    Minagawa, S.2    Kojima, E.3    Okamoto, N.4    Nakamoto, H.5
  • 25
    • 0034924812 scopus 로고    scopus 로고
    • Folding of newly translated proteins in vivo: the role of molecular chaperones
    • Frydman J. 2001. Folding of newly translated proteins in vivo: the role of molecular chaperones. Annu. Rev. Biochem. 70:603-648. http://dx.doi .org/10.1146/annurev.biochem.70.1.603.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 603-648
    • Frydman, J.1
  • 26
    • 84865801441 scopus 로고    scopus 로고
    • Identification of the Vibrio vulnificus htpG gene and its influence on cold shock recovery
    • Choi S, Jang K, Yun HJ, Kang DH. 2012. Identification of the Vibrio vulnificus htpG gene and its influence on cold shock recovery. J. Microbiol. 50:707-711. http://dx.doi.org/10.1007/s12275-012-2294-z.
    • (2012) J. Microbiol. , vol.50 , pp. 707-711
    • Choi, S.1    Jang, K.2    Yun, H.J.3    Kang, D.H.4
  • 27
    • 80051806193 scopus 로고    scopus 로고
    • HtpG is involved in the pathogenesis of Edwardsiella tarda
    • Dang W, Hu YH, Sun L. 2011. HtpG is involved in the pathogenesis of Edwardsiella tarda. Vet. Microbiol. 152:394-400. http://dx.doi.org/10 .1016/j.vetmic.2011.05.030.
    • (2011) Vet. Microbiol. , vol.152 , pp. 394-400
    • Dang, W.1    Hu, Y.H.2    Sun, L.3
  • 28
    • 0032840055 scopus 로고    scopus 로고
    • HtpG is essential for the thermal stress management in cyanobacteria
    • Tanaka N, Nakamoto H. 1999. HtpG is essential for the thermal stress management in cyanobacteria. FEBS Lett. 458:117-123. http://dx.doi.org /10.1016/S0014-5793(99)01134-5.
    • (1999) FEBS Lett. , vol.458 , pp. 117-123
    • Tanaka, N.1    Nakamoto, H.2
  • 29
    • 0033045319 scopus 로고    scopus 로고
    • The Bacillus subtilis htpG gene is not involved in thermal stress management
    • Versteeg S, Mogk A, Schumann W. 1999. The Bacillus subtilis htpG gene is not involved in thermal stress management. Mol. Gen. Genet. 261:582-588. http://dx.doi.org/10.1007/s004380051004.
    • (1999) Mol. Gen. Genet. , vol.261 , pp. 582-588
    • Versteeg, S.1    Mogk, A.2    Schumann, W.3
  • 30
  • 31
    • 84884491909 scopus 로고    scopus 로고
    • Use of a high-throughput screen to identify Leptospira mutants unable to colonize the carrier host or cause disease in the acute model of infection
    • Marcsisin RA, Bartpho T, Bulach DM, Srikram A, Sermswan RW, Adler B, Murray GL. 2013. Use of a high-throughput screen to identify Leptospira mutants unable to colonize the carrier host or cause disease in the acute model of infection. J. Med. Microbiol. 62:1601-1608. http://dx.doi .org/10.1099/jmm.0.058586-0.
    • (2013) J. Med. Microbiol. , vol.62 , pp. 1601-1608
    • Marcsisin, R.A.1    Bartpho, T.2    Bulach, D.M.3    Srikram, A.4    Sermswan, R.W.5    Adler, B.6    Murray, G.L.7
  • 32
    • 45849127235 scopus 로고    scopus 로고
    • Leptospira interrogans requires a functional heme oxygenase to scavenge iron from hemoglobin
    • Murray GL, Ellis KM, Lo M, Adler B. 2008. Leptospira interrogans requires a functional heme oxygenase to scavenge iron from hemoglobin. Microbes Infect. 10:791-797. http://dx.doi.org/10.1016/j.micinf.2008.04 .010.
    • (2008) Microbes Infect. , vol.10 , pp. 791-797
    • Murray, G.L.1    Ellis, K.M.2    Lo, M.3    Adler, B.4
  • 33
    • 37849041601 scopus 로고    scopus 로고
    • Conjugative transfer between Escherichia coli and Leptospira spp. as a new genetic tool
    • Picardeau M. 2008. Conjugative transfer between Escherichia coli and Leptospira spp. as a new genetic tool. Appl. Environ. Microbiol. 74:319-322. http://dx.doi.org/10.1128/AEM.02172-07.
    • (2008) Appl. Environ. Microbiol. , vol.74 , pp. 319-322
    • Picardeau, M.1
  • 34
    • 67650473254 scopus 로고    scopus 로고
    • Use of quantitative real-time PCR for studying the dissemination of Leptospira interrogans in the guinea pig infection model of leptospirosis
    • Lourdault K, Aviat F, Picardeau M. 2009. Use of quantitative real-time PCR for studying the dissemination of Leptospira interrogans in the guinea pig infection model of leptospirosis. J. Med. Microbiol. 58:648-655. http: //dx.doi.org/10.1099/jmm.0.008169-0.
    • (2009) J. Med. Microbiol. , vol.58 , pp. 648-655
    • Lourdault, K.1    Aviat, F.2    Picardeau, M.3
  • 35
    • 67349163028 scopus 로고    scopus 로고
    • Detection of pathogenic Leptospira spp. through TaqMan polymerase chain reaction targeting the LipL32 gene
    • Stoddard RA, Gee JE, Wilkins PP, McCaustland K, Hoffmaster AR.2009. Detection of pathogenic Leptospira spp. through TaqMan polymerase chain reaction targeting the LipL32 gene. Diagn. Microbiol. Infect. Dis. 64:247-255. http://dx.doi.org/10.1016/j.diagmicrobio.2009.03.014.
    • (2009) Diagn. Microbiol. Infect. Dis. , vol.64 , pp. 247-255
    • Stoddard, R.A.1    Gee, J.E.2    Wilkins, P.P.3    McCaustland, K.4    Hoffmaster, A.R.5
  • 36
    • 0036121913 scopus 로고    scopus 로고
    • Global analysis of outer membrane proteins from Leptospira interrogans serovar Lai
    • Cullen PA, Cordwell SJ, Bulach DM, Haake DA, Adler B. 2002. Global analysis of outer membrane proteins from Leptospira interrogans serovar Lai. Infect. Immun. 70:2311-2318. http://dx.doi.org/10.1128/IAI.70.5 .2311-2318.2002.
    • (2002) Infect. Immun. , vol.70 , pp. 2311-2318
    • Cullen, P.A.1    Cordwell, S.J.2    Bulach, D.M.3    Haake, D.A.4    Adler, B.5
  • 37
    • 0242417007 scopus 로고    scopus 로고
    • LipL21 is a novel surface-exposed lipoprotein of pathogenic Leptospira species
    • Cullen PA, Haake DA, Bulach DM, Zuerner RL, Adler B. 2003. LipL21 is a novel surface-exposed lipoprotein of pathogenic Leptospira species. Infect. Immun. 71:2414-2421. http://dx.doi.org/10.1128/IAI.71.5.2414-2421.2003.
    • (2003) Infect. Immun. , vol.71 , pp. 2414-2421
    • Cullen, P.A.1    Haake, D.A.2    Bulach, D.M.3    Zuerner, R.L.4    Adler, B.5
  • 38
    • 0142043304 scopus 로고    scopus 로고
    • Construction and characterization of a Porphyromonas gingivalis htpG disruption mutant
    • Sweier DG, Combs A, Shelburne CE, Fenno JC, Lopatin DE. 2003. Construction and characterization of a Porphyromonas gingivalis htpG disruption mutant. FEMS Microbiol. Lett. 225:101-106. http://dx.doi.org/10 .1016/S0378-1097(03)00506-8.
    • (2003) FEMS Microbiol. Lett. , vol.225 , pp. 101-106
    • Sweier, D.G.1    Combs, A.2    Shelburne, C.E.3    Fenno, J.C.4    Lopatin, D.E.5
  • 39
    • 77952910249 scopus 로고    scopus 로고
    • Use of luminescent Leptospira interrogans for enumeration in biological assays
    • Murray GL, King AM, Srikram A, Sermswan RW, Adler B. 2010. Use of luminescent Leptospira interrogans for enumeration in biological assays. J. Clin. Microbiol. 48:2037-2042. http://dx.doi.org/10.1128/JCM.02541-09.
    • (2010) J. Clin. Microbiol. , vol.48 , pp. 2037-2042
    • Murray, G.L.1    King, A.M.2    Srikram, A.3    Sermswan, R.W.4    Adler, B.5
  • 40
    • 80054112939 scopus 로고    scopus 로고
    • Characteristic features of intracellular pathogenic Leptospira in infected murine macrophages
    • Toma C, Okura N, Takayama C, Suzuki T. 2011. Characteristic features of intracellular pathogenic Leptospira in infected murine macrophages. Cell. Microbiol. 13:1783-1792. http://dx.doi.org/10.1111/j.1462-5822 .2011.01660.x.
    • (2011) Cell. Microbiol. , vol.13 , pp. 1783-1792
    • Toma, C.1    Okura, N.2    Takayama, C.3    Suzuki, T.4
  • 45
    • 84864380055 scopus 로고    scopus 로고
    • Novel structural and functional insights into the MoxR family of AAA+ATPases
    • Wong KS, Houry WA. 2012. Novel structural and functional insights into the MoxR family of AAA+ATPases. J. Struct. Biol. 179:211-221. http://dx .doi.org/10.1016/j.jsb.2012.03.010.
    • (2012) J. Struct. Biol. , vol.179 , pp. 211-221
    • Wong, K.S.1    Houry, W.A.2
  • 46
    • 0032589120 scopus 로고    scopus 로고
    • Characterization of the BatI (Bacteroides aerotolerance) operon in Bacteroides fragilis: isolation of a B. fragilis mutant with reduced aerotolerance and impaired growth in in vivo model systems
    • Tang YP, Dallas MM, Malamy MH. 1999. Characterization of the BatI (Bacteroides aerotolerance) operon in Bacteroides fragilis: isolation of a B. fragilis mutant with reduced aerotolerance and impaired growth in in vivo model systems. Mol. Microbiol. 32:139-149. http://dx.doi.org/10.1046/j .1365-2958.1999.01337.x.
    • (1999) Mol. Microbiol. , vol.32 , pp. 139-149
    • Tang, Y.P.1    Dallas, M.M.2    Malamy, M.H.3
  • 47
  • 48
    • 34247566179 scopus 로고    scopus 로고
    • Computer-assisted protein domain boundary prediction using the DomPred server
    • Bryson K, Cozzetto D, Jones DT. 2007. Computer-assisted protein domain boundary prediction using the DomPred server. Curr. Protein Pept. Sci. 8:181-188. http://dx.doi.org/10.2174/138920307780363415.
    • (2007) Curr. Protein Pept. Sci. , vol.8 , pp. 181-188
    • Bryson, K.1    Cozzetto, D.2    Jones, D.T.3
  • 49
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • Jones DT. 1999. Protein secondary structure prediction based on position-specific scoring matrices. J. Mol. Biol. 292:195-202. http://dx.doi.org /10.1006/jmbi.1999.3091.
    • (1999) J. Mol. Biol. , vol.292 , pp. 195-202
    • Jones, D.T.1
  • 51
    • 0024044382 scopus 로고
    • Ancient heat shock gene is dispensable
    • Bardwell JC, Craig EA. 1988. Ancient heat shock gene is dispensable. J. Bacteriol. 170:2977-2983.
    • (1988) J. Bacteriol. , vol.170 , pp. 2977-2983
    • Bardwell, J.C.1    Craig, E.A.2
  • 52
    • 0038489504 scopus 로고    scopus 로고
    • Role for the cyanobacterial HtpG in protection from oxidative stress
    • Hossain MM, Nakamoto H. 2003. Role for the cyanobacterial HtpG in protection from oxidative stress. Curr. Microbiol. 46:70-76. http://dx.doi .org/10.1007/s00284-002-3831-5.
    • (2003) Curr. Microbiol. , vol.46 , pp. 70-76
    • Hossain, M.M.1    Nakamoto, H.2
  • 53
    • 0030034307 scopus 로고    scopus 로고
    • Heat-shock and general stress response in Bacillus subtilis
    • Hecker M, Schumann W, Völker U. 1996. Heat-shock and general stress response in Bacillus subtilis. Mol. Microbiol. 19:417-428. http://dx.doi .org/10.1046/j.1365-2958.1996.396932.x.
    • (1996) Mol. Microbiol. , vol.19 , pp. 417-428
    • Hecker, M.1    Schumann, W.2    Völker, U.3
  • 54
    • 11144298941 scopus 로고    scopus 로고
    • Osmolarity, a key environmental signal controlling expression of leptospiral proteins LigA and LigB and the extracellular release of LigA
    • Matsunaga J, Sanchez Y, Xu X, Haake DA. 2005. Osmolarity, a key environmental signal controlling expression of leptospiral proteins LigA and LigB and the extracellular release of LigA. Infect. Immun. 73:70-78. http://dx.doi.org/10.1128/IAI.73.1.70-78.2005.
    • (2005) Infect. Immun. , vol.73 , pp. 70-78
    • Matsunaga, J.1    Sanchez, Y.2    Xu, X.3    Haake, D.A.4
  • 55
    • 33749259255 scopus 로고    scopus 로고
    • Effects of temperature on gene expression patterns in Leptospira interrogans serovar Lai as assessed by whole-genome microarrays
    • Lo M, Bulach DM, Powell DR, Haake DA, Matsunaga J, Paustian ML, Zuerner RL, Adler B. 2006. Effects of temperature on gene expression patterns in Leptospira interrogans serovar Lai as assessed by whole-genome microarrays. Infect. Immun. 74:5848-5859. http://dx.doi.org/10.1128 /IAI.00755-06.
    • (2006) Infect. Immun. , vol.74 , pp. 5848-5859
    • Lo, M.1    Bulach, D.M.2    Powell, D.R.3    Haake, D.A.4    Matsunaga, J.5    Paustian, M.L.6    Zuerner, R.L.7    Adler, B.8
  • 56
    • 0033933125 scopus 로고    scopus 로고
    • ClpB and HtpG facilitate de novo protein folding in stressed Escherichia coli cells
    • Thomas JG, Baneyx F. 2000. ClpB and HtpG facilitate de novo protein folding in stressed Escherichia coli cells. Mol. Microbiol. 36:1360-1370. http://dx.doi.org/10.1046/j.1365-2958.2000.01951.x.
    • (2000) Mol. Microbiol. , vol.36 , pp. 1360-1370
    • Thomas, J.G.1    Baneyx, F.2
  • 57
    • 84880649123 scopus 로고    scopus 로고
    • Leptospiral outer membrane protein LipL41 is not essential for acute leptospirosis, but requires a small chaperone, Lep, for stable expression
    • King AM, Bartpho T, Sermswan RW, Bulach DM, Eshghi A, Picardeau M, Adler B, Murray GL. 2013. Leptospiral outer membrane protein LipL41 is not essential for acute leptospirosis, but requires a small chaperone, Lep, for stable expression. Infect. Immun. 81:2768-2776. http://dx .doi.org/10.1128/IAI.00531-13.
    • (2013) Infect. Immun. , vol.81 , pp. 2768-2776
    • King, A.M.1    Bartpho, T.2    Sermswan, R.W.3    Bulach, D.M.4    Eshghi, A.5    Picardeau, M.6    Adler, B.7    Murray, G.L.8
  • 59
    • 26244466048 scopus 로고    scopus 로고
    • Regulation of complement activation at the C3-level by serum resistant leptospires
    • Meri T, Murgia R, Stefanel P, Meri S, Cinco M. 2005. Regulation of complement activation at the C3-level by serum resistant leptospires. Microb. Pathog. 39:139-147. http://dx.doi.org/10.1016/j.micpath.2005.07 .003.
    • (2005) Microb. Pathog. , vol.39 , pp. 139-147
    • Meri, T.1    Murgia, R.2    Stefanel, P.3    Meri, S.4    Cinco, M.5
  • 61
    • 84864185721 scopus 로고    scopus 로고
    • Multiple activities of LigB potentiate virulence of Leptospira interrogans: inhibition of alternative and classical pathways of complement
    • Choy HA. 2012. Multiple activities of LigB potentiate virulence of Leptospira interrogans: inhibition of alternative and classical pathways of complement. PLoS One 7:e41566. http://dx.doi.org/10.1371/journal.pone .0041566.
    • (2012) PLoS One , vol.7
    • Choy, H.A.1
  • 62
    • 77649300543 scopus 로고    scopus 로고
    • Global transcriptomic response of Leptospira interrogans serovar Copenhageni upon exposure to serum
    • Patarakul K, Lo M, Adler B. 2010. Global transcriptomic response of Leptospira interrogans serovar Copenhageni upon exposure to serum. BMC Microbiol. 10:31. http://dx.doi.org/10.1186/1471-2180-10-31.
    • (2010) BMC Microbiol. , vol.10 , pp. 31
    • Patarakul, K.1    Lo, M.2    Adler, B.3
  • 63
    • 0037340183 scopus 로고    scopus 로고
    • Regulation of Salmonella typhimurium lipopolysaccharide O antigen chain length is required for virulence; identification of FepE as a second Wzz
    • Murray GL, Attridge SR, Morona R. 2003. Regulation of Salmonella typhimurium lipopolysaccharide O antigen chain length is required for virulence; identification of FepE as a second Wzz. Mol. Microbiol. 47: 1395-1406. http://dx.doi.org/10.1046/j.1365-2958.2003.03383.x.
    • (2003) Mol. Microbiol. , vol.47 , pp. 1395-1406
    • Murray, G.L.1    Attridge, S.R.2    Morona, R.3
  • 66
    • 84865199168 scopus 로고    scopus 로고
    • Lsa30, a novel adhesin of Leptospira interrogans binds human plasminogen and the complement regulator C4bp
    • Souza NM, Vieira ML, Alves IJ, de Morais ZM, Vasconcellos SA, Nascimento ALTO. 2012. Lsa30, a novel adhesin of Leptospira interrogans binds human plasminogen and the complement regulator C4bp. Microb. Pathog. 53:125-134. http://dx.doi.org/10.1016/j.micpath.2012.06.001.
    • (2012) Microb. Pathog. , vol.53 , pp. 125-134
    • Souza, N.M.1    Vieira, M.L.2    Alves, I.J.3    de Morais, Z.M.4    Vasconcellos, S.A.5    Nascimento, A.L.T.O.6
  • 67
    • 77953940510 scopus 로고    scopus 로고
    • Functional characterization of LcpA, a surface-exposed protein of Leptospira spp. that binds the human complement regulator C4BP
    • Barbosa AS, Monaris D, Silva LB, Morais ZM, Vasconcellos SA, Cianciarullo AM, Isaac L, Abreu PAE. 2010. Functional characterization of LcpA, a surface-exposed protein of Leptospira spp. that binds the human complement regulator C4BP. Infect. Immun. 78:3207-3216. http://dx.doi .org/10.1128/IAI.00279-10.
    • (2010) Infect. Immun. , vol.78 , pp. 3207-3216
    • Barbosa, A.S.1    Monaris, D.2    Silva, L.B.3    Morais, Z.M.4    Vasconcellos, S.A.5    Cianciarullo, A.M.6    Isaac, L.7    Abreu, P.A.E.8
  • 69
    • 77956766997 scopus 로고    scopus 로고
    • Ribosomal protein L2 associates with E. coli HtpG and activates its ATPase activity
    • Motojima-Miyazaki Y, Yoshida M, Motojima F. 2010. Ribosomal protein L2 associates with E. coli HtpG and activates its ATPase activity. Biochem. Biophys. Res. Commun. 400:241-245. http://dx.doi.org/10 .1016/j.bbrc.2010.08.047.
    • (2010) Biochem. Biophys. Res. Commun. , vol.400 , pp. 241-245
    • Motojima-Miyazaki, Y.1    Yoshida, M.2    Motojima, F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.