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Volumn 8, Issue 10, 2013, Pages

Leptospira interrogans Enolase Is Secreted Extracellularly and Interacts with Plasminogen

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ANTIGEN; BACTERIAL PROTEIN; ENOLASE; OUTER MEMBRANE PROTEIN; PLASMINOGEN;

EID: 84885817322     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0078150     Document Type: Article
Times cited : (32)

References (63)
  • 1
    • 73949084950 scopus 로고    scopus 로고
    • Leptospira and leptospirosis
    • doi:10.1016/j.vetmic.2009.03.012
    • Adler B, de la Peña Moctezuma A, (2010) Leptospira and leptospirosis. Vet Microbiol 140: 287-296. doi:10.1016/j.vetmic.2009.03.012. PubMed: 19345023.
    • (2010) Vet Microbiol , vol.140 , pp. 287-296
    • Adler, B.1    de la Peña Moctezuma, A.2
  • 2
    • 70349269503 scopus 로고    scopus 로고
    • Leptospira: the dawn of the molecular genetics era for an emerging zoonotic pathogen
    • doi:10.1038/nrmicro2208
    • Ko AI, Goarant C, Picardeau M, (2009) Leptospira: the dawn of the molecular genetics era for an emerging zoonotic pathogen. Nat Rev Microbiol 7: 736-747. doi:10.1038/nrmicro2208. PubMed: 19756012.
    • (2009) Nat Rev Microbiol , vol.7 , pp. 736-747
    • Ko, A.I.1    Goarant, C.2    Picardeau, M.3
  • 3
    • 0035072803 scopus 로고    scopus 로고
    • Leptospirosis
    • doi:10.1128/CMR.14.2.296-326.2001
    • Levett PN, (2001) Leptospirosis. Clin Microbiol Rev 14: 296-326. doi:10.1128/CMR.14.2.296-326.2001. PubMed: 11292640.
    • (2001) Clin Microbiol Rev , vol.14 , pp. 296-326
    • Levett, P.N.1
  • 4
  • 5
    • 34247608279 scopus 로고    scopus 로고
    • Leptospirosis: pathogenesis, immunity, and diagnosis
    • doi:10.1097/QCO.0b013e32814a5729
    • Palaniappan RU, Ramanujam S, Chang YF, (2007) Leptospirosis: pathogenesis, immunity, and diagnosis. Curr Opin Infect Dis 20: 284-292. doi:10.1097/QCO.0b013e32814a5729. PubMed: 17471039.
    • (2007) Curr Opin Infect Dis , vol.20 , pp. 284-292
    • Palaniappan, R.U.1    Ramanujam, S.2    Chang, Y.F.3
  • 6
    • 78650251929 scopus 로고    scopus 로고
    • New insights into the pathogenicity of leptospires: evasion of host defences
    • Cinco M, (2010) New insights into the pathogenicity of leptospires: evasion of host defences. New Microbiol 33: 283-292. PubMed: 21213586.
    • (2010) New Microbiol , vol.33 , pp. 283-292
    • Cinco, M.1
  • 7
    • 0033523415 scopus 로고    scopus 로고
    • Urban epidemic of severe leptospirosis in Brazil. Salvador Leptospirosis Study Group
    • doi:10.1016/S0140-6736(99)80012-9
    • Ko AI, Galvão Reis M, Ribeiro Dourado CM, Johnson WD Jr., Riley LW, (1999) Urban epidemic of severe leptospirosis in Brazil. Salvador Leptospirosis Study Group. Lancet 354: 820-825. doi:10.1016/S0140-6736(99)80012-9. PubMed: 10485724.
    • (1999) Lancet , vol.354 , pp. 820-825
    • Ko, A.I.1    Galvão Reis, M.2    Ribeiro Dourado, C.M.3    Johnson Jr., W.D.4    Riley, L.W.5
  • 9
    • 0344983453 scopus 로고    scopus 로고
    • Leptospirosis: a zoonotic disease of global importance
    • doi:10.1016/S1473-3099(03)00830-2
    • Bharti AR, Nally JE, Ricaldi JN, Matthias MA, Diaz MM, et al. (2003) Leptospirosis: a zoonotic disease of global importance. Lancet Infect Dis 3: 757-771. doi:10.1016/S1473-3099(03)00830-2. PubMed: 14652202.
    • (2003) Lancet Infect Dis , vol.3 , pp. 757-771
    • Bharti, A.R.1    Nally, J.E.2    Ricaldi, J.N.3    Matthias, M.A.4    Diaz, M.M.5
  • 11
    • 19944433155 scopus 로고    scopus 로고
    • Evaluation of lig-based conventional and real time PCR for the detection of pathogenic leptospires
    • doi:10.1016/j.mcp.2004.10.002
    • Palaniappan RU, Chang YF, Chang CF, Pan MJ, Yang CW, et al. (2005) Evaluation of lig-based conventional and real time PCR for the detection of pathogenic leptospires. Mol Cell Probes 19: 111-117. doi:10.1016/j.mcp.2004.10.002. PubMed: 15680212.
    • (2005) Mol Cell Probes , vol.19 , pp. 111-117
    • Palaniappan, R.U.1    Chang, Y.F.2    Chang, C.F.3    Pan, M.J.4    Yang, C.W.5
  • 12
    • 80052541260 scopus 로고    scopus 로고
    • Pathogenesis of leptospirosis: the influence of genomics
    • doi:10.1016/j.vetmic.2011.02.055
    • Adler B, Lo M, Seemann T, Murray GL, (2011) Pathogenesis of leptospirosis: the influence of genomics. Vet Microbiol 153: 73-81. doi:10.1016/j.vetmic.2011.02.055. PubMed: 21440384.
    • (2011) Vet Microbiol , vol.153 , pp. 73-81
    • Adler, B.1    Lo, M.2    Seemann, T.3    Murray, G.L.4
  • 13
    • 33750462005 scopus 로고    scopus 로고
    • A newly identified leptospiral adhesin mediates attachment to laminin
    • doi:10.1128/IAI.00460-06
    • Barbosa AS, Abreu PA, Neves FO, Atzingen MV, Watanabe MM, et al. (2006) A newly identified leptospiral adhesin mediates attachment to laminin. Infect Immun 74: 6356-6364. doi:10.1128/IAI.00460-06. PubMed: 16954400.
    • (2006) Infect Immun , vol.74 , pp. 6356-6364
    • Barbosa, A.S.1    Abreu, P.A.2    Neves, F.O.3    Atzingen, M.V.4    Watanabe, M.M.5
  • 14
    • 35748983212 scopus 로고    scopus 로고
    • Immunogenicity of the recombinant leptospiral putative outer membrane proteins as vaccine candidates
    • doi:10.1016/j.vaccine.2007.09.020
    • Chang YF, Chen CS, Palaniappan RU, He H, McDonough SP, et al. (2007) Immunogenicity of the recombinant leptospiral putative outer membrane proteins as vaccine candidates. Vaccine 25: 8190-8197. doi:10.1016/j.vaccine.2007.09.020. PubMed: 17936448.
    • (2007) Vaccine , vol.25 , pp. 8190-8197
    • Chang, Y.F.1    Chen, C.S.2    Palaniappan, R.U.3    He, H.4    McDonough, S.P.5
  • 15
    • 2642553745 scopus 로고    scopus 로고
    • Outer membrane proteins of pathogenic spirochetes
    • doi:10.1016/j.femsre.2003.10.004
    • Cullen PA, Haake DA, Adler B, (2004) Outer membrane proteins of pathogenic spirochetes. FEMS Microbiol Rev 28: 291-318. doi:10.1016/j.femsre.2003.10.004. PubMed: 15449605.
    • (2004) FEMS Microbiol Rev , vol.28 , pp. 291-318
    • Cullen, P.A.1    Haake, D.A.2    Adler, B.3
  • 16
    • 0036136449 scopus 로고    scopus 로고
    • Cytotoxic activities of Leptospira interrogans hemolysin SphH as a pore-forming protein on mammalian cells
    • doi:10.1128/IAI.70.1.315-322.2002
    • Lee SH, Kim S, Park SC, Kim MJ, (2002) Cytotoxic activities of Leptospira interrogans hemolysin SphH as a pore-forming protein on mammalian cells. Infect Immun 70: 315-322. doi:10.1128/IAI.70.1.315-322.2002. PubMed: 11748197.
    • (2002) Infect Immun , vol.70 , pp. 315-322
    • Lee, S.H.1    Kim, S.2    Park, S.C.3    Kim, M.J.4
  • 17
    • 0034175911 scopus 로고    scopus 로고
    • Identification of a 36-kDa fibronectin-binding protein expressed by a virulent variant of Leptospira interrogans serovar icterohaemorrhagiae
    • doi:10.1111/j.1574-6968.2000.tb09034.x
    • Merien F, Truccolo J, Baranton G, Perolat P, (2000) Identification of a 36-kDa fibronectin-binding protein expressed by a virulent variant of Leptospira interrogans serovar icterohaemorrhagiae. FEMS Microbiol Lett 185: 17-22. doi:10.1111/j.1574-6968.2000.tb09034.x. PubMed: 10731601.
    • (2000) FEMS Microbiol Lett , vol.185 , pp. 17-22
    • Merien, F.1    Truccolo, J.2    Baranton, G.3    Perolat, P.4
  • 18
    • 34547645283 scopus 로고    scopus 로고
    • The OmpA-like protein Loa22 is essential for leptospiral virulence
    • doi:10.1371/journal.ppat.0030097
    • Ristow P, Bourhy P, da Cruz McBride FW, Figueira CP, Huerre M, et al. (2007) The OmpA-like protein Loa22 is essential for leptospiral virulence. PLOS Pathog 3: e97. doi:10.1371/journal.ppat.0030097. PubMed: 17630832.
    • (2007) PLOS Pathog , vol.3
    • Ristow, P.1    Bourhy, P.2    da Cruz McBride, F.W.3    Figueira, C.P.4    Huerre, M.5
  • 19
    • 77955297726 scopus 로고    scopus 로고
    • In vitro identification of novel plasminogen-binding receptors of the pathogen Leptospira interrogans
    • doi:10.1371/journal.pone.0011259
    • Vieira ML, Atzingen MV, Oliveira TR, Oliveira R, Andrade DM, et al. (2010) In vitro identification of novel plasminogen-binding receptors of the pathogen Leptospira interrogans. PLOS ONE 5: e11259. doi:10.1371/journal.pone.0011259. PubMed: 20582320.
    • (2010) PLOS ONE , vol.5
    • Vieira, M.L.1    Atzingen, M.V.2    Oliveira, T.R.3    Oliveira, R.4    Andrade, D.M.5
  • 20
    • 23344432754 scopus 로고    scopus 로고
    • Surfaceome of Leptospira spp
    • doi:10.1128/IAI.73.8.4853-4863.2005
    • Cullen PA, Xu X, Matsunaga J, Sanchez Y, Ko AI, et al. (2005) Surfaceome of Leptospira spp. Infect Immun 73: 4853-4863. doi:10.1128/IAI.73.8.4853-4863.2005. PubMed: 16040999.
    • (2005) Infect Immun , vol.73 , pp. 4853-4863
    • Cullen, P.A.1    Xu, X.2    Matsunaga, J.3    Sanchez, Y.4    Ko, A.I.5
  • 21
    • 0033910411 scopus 로고    scopus 로고
    • Spirochaetal lipoproteins and pathogenesis
    • Haake DA, (2000) Spirochaetal lipoproteins and pathogenesis. Microbiology 146(7):: 1491-1504. PubMed: 10878114.
    • (2000) Microbiology , vol.146 , pp. 1491-1504
    • Haake, D.A.1
  • 22
    • 33846814927 scopus 로고    scopus 로고
    • Characterization of the outer membrane proteome of Leptospira interrogans expressed during acute lethal infection
    • doi:10.1128/IAI.00741-06
    • Nally JE, Whitelegge JP, Bassilian S, Blanco DR, Lovett MA, (2007) Characterization of the outer membrane proteome of Leptospira interrogans expressed during acute lethal infection. Infect Immun 75: 766-773. doi:10.1128/IAI.00741-06. PubMed: 17101664.
    • (2007) Infect Immun , vol.75 , pp. 766-773
    • Nally, J.E.1    Whitelegge, J.P.2    Bassilian, S.3    Blanco, D.R.4    Lovett, M.A.5
  • 24
    • 37249015372 scopus 로고    scopus 로고
    • Evaluation of protective immunity of Leptospira immunoglobulin like protein A (LigA) DNA vaccine against challenge in hamsters
    • doi:10.1016/j.vaccine.2007.10.029
    • Faisal SM, Yan W, Chen CS, Palaniappan RU, McDonough SP, et al. (2008) Evaluation of protective immunity of Leptospira immunoglobulin like protein A (LigA) DNA vaccine against challenge in hamsters. Vaccine 26: 277-287. doi:10.1016/j.vaccine.2007.10.029. PubMed: 18055070.
    • (2008) Vaccine , vol.26 , pp. 277-287
    • Faisal, S.M.1    Yan, W.2    Chen, C.S.3    Palaniappan, R.U.4    McDonough, S.P.5
  • 25
    • 0036121913 scopus 로고    scopus 로고
    • Global analysis of outer membrane proteins from Leptospira interrogans serovar Lai
    • doi:10.1128/IAI.70.5.2311-2318.2002
    • 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. doi:10.1128/IAI.70.5.2311-2318.2002. PubMed: 11953365.
    • (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
  • 26
    • 62449313550 scopus 로고    scopus 로고
    • Major surface protein LipL32 is not required for either acute or chronic infection with Leptospira interrogans
    • doi:10.1128/IAI.01370-08
    • Murray GL, Srikram A, Hoke DE, Wunder EA Jr., Henry R, et al. (2009) Major surface protein LipL32 is not required for either acute or chronic infection with Leptospira interrogans. Infect Immun 77: 952-958. doi:10.1128/IAI.01370-08. PubMed: 19103763.
    • (2009) Infect Immun , vol.77 , pp. 952-958
    • Murray, G.L.1    Srikram, A.2    Hoke, D.E.3    Wunder Jr., E.A.4    Henry, R.5
  • 27
    • 84860340859 scopus 로고    scopus 로고
    • Protection against lethal leptospirosis after vaccination with LipL32 coupled or coadministered with the B subunit of Escherichia coli heat-labile enterotoxin
    • doi:10.1128/CVI.05720-11
    • Grassmann AA, Félix SR, dos Santos CX, Amaral MG, Neto, Seixaset al. (2012) Protection against lethal leptospirosis after vaccination with LipL32 coupled or coadministered with the B subunit of Escherichia coli heat-labile enterotoxin. Clin Vaccine Immunol 19: 740-745. doi:10.1128/CVI.05720-11. PubMed: 22379066.
    • (2012) Clin Vaccine Immunol , vol.19 , pp. 740-745
    • Grassmann, A.A.1    Félix, S.R.2    dos Santos, C.X.3    Amaral, M.G.4    Neto5
  • 28
    • 57749189817 scopus 로고    scopus 로고
    • New insights into the molecular mechanisms of the fibrinolytic system
    • doi:10.1111/j.1538-7836.2008.03220.x
    • Rijken DC, Lijnen HR, (2009) New insights into the molecular mechanisms of the fibrinolytic system. J Thromb Haemost 7: 4-13. doi:10.1111/j.1538-7836.2008.03220.x. PubMed: 19017261.
    • (2009) J Thromb Haemost , vol.7 , pp. 4-13
    • Rijken, D.C.1    Lijnen, H.R.2
  • 30
    • 0026053146 scopus 로고
    • The plasminogen activator/plasmin system
    • doi:10.1172/JCI115405
    • Vassalli JD, Sappino AP, Belin D, (1991) The plasminogen activator/plasmin system. J Clin Invest 88: 1067-1072. doi:10.1172/JCI115405. PubMed: 1833420.
    • (1991) J Clin Invest , vol.88 , pp. 1067-1072
    • Vassalli, J.D.1    Sappino, A.P.2    Belin, D.3
  • 31
    • 39149123184 scopus 로고    scopus 로고
    • Immunogenic and plasminogen-binding surface-associated alpha-enolase of Trichomonas vaginalis
    • doi:10.1128/IAI.01352-07
    • Mundodi V, Kucknoor AS, Alderete JF, (2008) Immunogenic and plasminogen-binding surface-associated alpha-enolase of Trichomonas vaginalis. Infect Immun 76: 523-531. doi:10.1128/IAI.01352-07. PubMed: 18070902.
    • (2008) Infect Immun , vol.76 , pp. 523-531
    • Mundodi, V.1    Kucknoor, A.S.2    Alderete, J.F.3
  • 32
    • 0025819231 scopus 로고
    • Role of cell-surface lysines in plasminogen binding to cells: identification of alpha-enolase as a candidate plasminogen receptor
    • doi:10.1021/bi00220a034
    • Miles LA, Dahlberg CM, Plescia J, Felez J, Kato K, et al. (1991) Role of cell-surface lysines in plasminogen binding to cells: identification of alpha-enolase as a candidate plasminogen receptor. Biochemistry 30: 1682-1691. doi:10.1021/bi00220a034. PubMed: 1847072.
    • (1991) Biochemistry , vol.30 , pp. 1682-1691
    • Miles, L.A.1    Dahlberg, C.M.2    Plescia, J.3    Felez, J.4    Kato, K.5
  • 33
    • 0034931519 scopus 로고    scopus 로고
    • alpha-Enolase of Streptococcus pneumoniae is a plasmin(ogen)-binding protein displayed on the bacterial cell surface
    • doi:10.1046/j.1365-2958.2001.02448.x
    • Bergmann S, Rohde M, Chhatwal GS, Hammerschmidt S, (2001) alpha-Enolase of Streptococcus pneumoniae is a plasmin(ogen)-binding protein displayed on the bacterial cell surface. Mol Microbiol 40: 1273-1287. doi:10.1046/j.1365-2958.2001.02448.x. PubMed: 11442827.
    • (2001) Mol Microbiol , vol.40 , pp. 1273-1287
    • Bergmann, S.1    Rohde, M.2    Chhatwal, G.S.3    Hammerschmidt, S.4
  • 34
    • 0037344772 scopus 로고    scopus 로고
    • Candida albicans binds human plasminogen: identification of eight plasminogen-binding proteins
    • doi:10.1046/j.1365-2958.2003.03390.x
    • Crowe JD, Sievwright IK, Auld GC, Moore NR, Gow NA, et al. (2003) Candida albicans binds human plasminogen: identification of eight plasminogen-binding proteins. Mol Microbiol 47: 1637-1651. doi:10.1046/j.1365-2958.2003.03390.x. PubMed: 12622818.
    • (2003) Mol Microbiol , vol.47 , pp. 1637-1651
    • Crowe, J.D.1    Sievwright, I.K.2    Auld, G.C.3    Moore, N.R.4    Gow, N.A.5
  • 35
    • 69049111014 scopus 로고    scopus 로고
    • Plasminogen acquisition and activation at the surface of Leptospira species lead to fibronectin degradation
    • doi:10.1128/IAI.00353-09
    • Vieira ML, Vasconcellos SA, Gonçales AP, de Morais ZM, Nascimento AL, (2009) Plasminogen acquisition and activation at the surface of Leptospira species lead to fibronectin degradation. Infect Immun 77: 4092-4101. doi:10.1128/IAI.00353-09. PubMed: 19581392.
    • (2009) Infect Immun , vol.77 , pp. 4092-4101
    • Vieira, M.L.1    Vasconcellos, S.A.2    Gonçales, A.P.3    de Morais, Z.M.4    Nascimento, A.L.5
  • 36
    • 77951239052 scopus 로고    scopus 로고
    • Leptospiral endostatin-like protein A is a bacterial cell surface receptor for human plasminogen
    • doi:10.1128/IAI.01282-09
    • Verma A, Brissette CA, Bowman AA, Shah ST, Zipfel PF, et al. (2010) Leptospiral endostatin-like protein A is a bacterial cell surface receptor for human plasminogen. Infect Immun 78: 2053-2059. doi:10.1128/IAI.01282-09. PubMed: 20160016.
    • (2010) Infect Immun , vol.78 , pp. 2053-2059
    • Verma, A.1    Brissette, C.A.2    Bowman, A.A.3    Shah, S.T.4    Zipfel, P.F.5
  • 37
    • 0037464546 scopus 로고    scopus 로고
    • Unique physiological and pathogenic features of Leptospira interrogans revealed by whole-genome sequencing
    • doi:10.1038/nature01597
    • Ren SX, Fu G, Jiang XG, Zeng R, Miao YG, et al. (2003) Unique physiological and pathogenic features of Leptospira interrogans revealed by whole-genome sequencing. Nature 422: 888-893. doi:10.1038/nature01597. PubMed: 12712204.
    • (2003) Nature , vol.422 , pp. 888-893
    • Ren, S.X.1    Fu, G.2    Jiang, X.G.3    Zeng, R.4    Miao, Y.G.5
  • 38
    • 84863256882 scopus 로고    scopus 로고
    • A surface enolase participates in Borrelia burgdorferi-plasminogen interaction and contributes to pathogen survival within feeding ticks
    • doi:10.1128/IAI.05671-11
    • Nogueira SV, Smith AA, Qin JH, Pal U, (2012) A surface enolase participates in Borrelia burgdorferi-plasminogen interaction and contributes to pathogen survival within feeding ticks. Infect Immun 80: 82-90. doi:10.1128/IAI.05671-11. PubMed: 22025510.
    • (2012) Infect Immun , vol.80 , pp. 82-90
    • Nogueira, S.V.1    Smith, A.A.2    Qin, J.H.3    Pal, U.4
  • 39
    • 38749142579 scopus 로고    scopus 로고
    • Borrelia burgdorferi basic membrane proteins A and B participate in the genesis of Lyme arthritis
    • doi:10.1084/jem.20070962
    • Pal U, Wang P, Bao F, Yang X, Samanta S, et al. (2008) Borrelia burgdorferi basic membrane proteins A and B participate in the genesis of Lyme arthritis. J Exp Med 205: 133-141. doi:10.1084/jem.20070962. PubMed: 18166585.
    • (2008) J Exp Med , vol.205 , pp. 133-141
    • Pal, U.1    Wang, P.2    Bao, F.3    Yang, X.4    Samanta, S.5
  • 40
    • 0034104388 scopus 로고    scopus 로고
    • The leptospiral major outer membrane protein LipL32 is a lipoprotein expressed during mammalian infection
    • doi:10.1128/IAI.68.4.2276-2285.2000
    • Haake DA, Chao G, Zuerner RL, Barnett JK, Barnett D, et al. (2000) The leptospiral major outer membrane protein LipL32 is a lipoprotein expressed during mammalian infection. Infect Immun 68: 2276-2285. doi:10.1128/IAI.68.4.2276-2285.2000. PubMed: 10722630.
    • (2000) Infect Immun , vol.68 , pp. 2276-2285
    • Haake, D.A.1    Chao, G.2    Zuerner, R.L.3    Barnett, J.K.4    Barnett, D.5
  • 41
    • 70350143371 scopus 로고    scopus 로고
    • Borrelia burgdorferi small lipoprotein Lp6.6 is a member of multiple protein complexes in the outer membrane and facilitates pathogen transmission from ticks to mice
    • doi:10.1111/j.1365-2958.2009.06853.x
    • Promnares K, Kumar M, Shroder DY, Zhang X, Anderson JF, et al. (2009) Borrelia burgdorferi small lipoprotein Lp6.6 is a member of multiple protein complexes in the outer membrane and facilitates pathogen transmission from ticks to mice. Mol Microbiol 74: 112-125. doi:10.1111/j.1365-2958.2009.06853.x. PubMed: 19703109.
    • (2009) Mol Microbiol , vol.74 , pp. 112-125
    • Promnares, K.1    Kumar, M.2    Shroder, D.Y.3    Zhang, X.4    Anderson, J.F.5
  • 42
    • 80053895756 scopus 로고    scopus 로고
    • Characterization of multiprotein complexes of the Borrelia burgdorferi outer membrane vesicles
    • doi:10.1021/pr200395b
    • Yang X, Promnares K, Qin J, He M, Shroder DY, et al. (2011) Characterization of multiprotein complexes of the Borrelia burgdorferi outer membrane vesicles. J Proteome Res 10: 4556-4566. doi:10.1021/pr200395b. PubMed: 21875077.
    • (2011) J Proteome Res , vol.10 , pp. 4556-4566
    • Yang, X.1    Promnares, K.2    Qin, J.3    He, M.4    Shroder, D.Y.5
  • 43
    • 0043030106 scopus 로고    scopus 로고
    • Binding of Candida albicans enolase to plasmin(ogen) results in enhanced invasion of human brain microvascular endothelial cells
    • doi:10.1099/jmm.0.05060-0
    • Jong AY, Chen SH, Stins MF, Kim KS, Tuan TL, et al. (2003) Binding of Candida albicans enolase to plasmin(ogen) results in enhanced invasion of human brain microvascular endothelial cells. J Med Microbiol 52: 615-622. doi:10.1099/jmm.0.05060-0. PubMed: 12867553.
    • (2003) J Med Microbiol , vol.52 , pp. 615-622
    • Jong, A.Y.1    Chen, S.H.2    Stins, M.F.3    Kim, K.S.4    Tuan, T.L.5
  • 44
    • 0032486286 scopus 로고    scopus 로고
    • alpha-enolase, a novel strong plasmin(ogen) binding protein on the surface of pathogenic streptococci
    • doi:10.1074/jbc.273.23.14503
    • Pancholi V, Fischetti VA, (1998) alpha-enolase, a novel strong plasmin(ogen) binding protein on the surface of pathogenic streptococci. J Biol Chem 273: 14503-14515. doi:10.1074/jbc.273.23.14503. PubMed: 9603964.
    • (1998) J Biol Chem , vol.273 , pp. 14503-14515
    • Pancholi, V.1    Fischetti, V.A.2
  • 45
    • 52449135569 scopus 로고    scopus 로고
    • alpha-Enolase binds to human plasminogen on the surface of Bacillus anthracis
    • doi:10.1016/j.bbapap.2008.03.017
    • Agarwal S, Kulshreshtha P, Bambah Mukku D, Bhatnagar R, (2008) alpha-Enolase binds to human plasminogen on the surface of Bacillus anthracis. Biochim Biophys Acta 1784: 986-994. doi:10.1016/j.bbapap.2008.03.017. PubMed: 18456007.
    • (2008) Biochim Biophys Acta , vol.1784 , pp. 986-994
    • Agarwal, S.1    Kulshreshtha, P.2    Bambah Mukku, D.3    Bhatnagar, R.4
  • 46
    • 0036568587 scopus 로고    scopus 로고
    • Anchorless adhesins and invasins of Gram-positive bacteria: a new class of virulence factors
    • doi:10.1016/S0966-842X(02)02351-X
    • Chhatwal GS, (2002) Anchorless adhesins and invasins of Gram-positive bacteria: a new class of virulence factors. Trends Microbiol 10: 205-208. doi:10.1016/S0966-842X(02)02351-X. PubMed: 11973142.
    • (2002) Trends Microbiol , vol.10 , pp. 205-208
    • Chhatwal, G.S.1
  • 47
    • 80555140065 scopus 로고    scopus 로고
    • Borrelia burgdorferi enolase is a surface-exposed plasminogen binding protein
    • doi:10.1371/journal.pone.0027502
    • Floden AM, Watt JA, Brissette CA, (2011) Borrelia burgdorferi enolase is a surface-exposed plasminogen binding protein. PLOS ONE 6: e27502. doi:10.1371/journal.pone.0027502. PubMed: 22087329.
    • (2011) PLOS ONE , vol.6
    • Floden, A.M.1    Watt, J.A.2    Brissette, C.A.3
  • 48
    • 0031587871 scopus 로고    scopus 로고
    • Plasminogen is required for efficient dissemination of Borrelia burgdorferi in ticks and for enhancement of spirochetemia in mice
    • doi:10.1016/S0092-8674(00)80298-6
    • Coleman JL, Gebbia JA, Piesman J, Degen JL, Bugge TH, et al. (1997) Plasminogen is required for efficient dissemination of Borrelia burgdorferi in ticks and for enhancement of spirochetemia in mice. Cell 89: 1111-1119. doi:10.1016/S0092-8674(00)80298-6. PubMed: 9215633.
    • (1997) Cell , vol.89 , pp. 1111-1119
    • Coleman, J.L.1    Gebbia, J.A.2    Piesman, J.3    Degen, J.L.4    Bugge, T.H.5
  • 49
    • 0029039462 scopus 로고
    • Borrelia burgdorferi binds plasminogen, resulting in enhanced penetration of endothelial monolayers
    • Coleman JL, Sellati TJ, Testa JE, Kew RR, Furie MB, et al. (1995) Borrelia burgdorferi binds plasminogen, resulting in enhanced penetration of endothelial monolayers. Infect Immun 63: 2478-2484. PubMed: 7790059.
    • (1995) Infect Immun , vol.63 , pp. 2478-2484
    • Coleman, J.L.1    Sellati, T.J.2    Testa, J.E.3    Kew, R.R.4    Furie, M.B.5
  • 50
    • 0034064780 scopus 로고    scopus 로고
    • Identification of a Treponema denticola OppA homologue that binds host proteins present in the subgingival environment
    • doi:10.1128/IAI.68.4.1884-1892.2000
    • Fenno JC, Tamura M, Hannam PM, Wong GW, Chan RA, et al. (2000) Identification of a Treponema denticola OppA homologue that binds host proteins present in the subgingival environment. Infect Immun 68: 1884-1892. doi:10.1128/IAI.68.4.1884-1892.2000. PubMed: 10722578.
    • (2000) Infect Immun , vol.68 , pp. 1884-1892
    • Fenno, J.C.1    Tamura, M.2    Hannam, P.M.3    Wong, G.W.4    Chan, R.A.5
  • 52
    • 80053578297 scopus 로고    scopus 로고
    • Nonclassical protein secretion by Bacillus subtilis in the stationary phase is not due to cell lysis
    • doi:10.1128/JB.05897-11
    • Yang CK, Ewis HE, Zhang X, Lu CD, Hu HJ, et al. (2011) Nonclassical protein secretion by Bacillus subtilis in the stationary phase is not due to cell lysis. J Bacteriol 193: 5607-5615. doi:10.1128/JB.05897-11. PubMed: 21856851.
    • (2011) J Bacteriol , vol.193 , pp. 5607-5615
    • Yang, C.K.1    Ewis, H.E.2    Zhang, X.3    Lu, C.D.4    Hu, H.J.5
  • 53
    • 84884768623 scopus 로고    scopus 로고
    • Extracellular Proteome Analysis of Leptospira interrogans serovar Lai
    • doi:10.1089/omi.2013.0043
    • Zeng L, Zhang Y, Zhu Y, Yin H, Zhuang X, et al. (2013) Extracellular Proteome Analysis of Leptospira interrogans serovar Lai. Omics. [Epub ahead of print]. doi:10.1089/omi.2013.0043. PubMed: 23895271.
    • (2013) Omics
    • Zeng, L.1    Zhang, Y.2    Zhu, Y.3    Yin, H.4    Zhuang, X.5
  • 54
    • 83055163891 scopus 로고    scopus 로고
    • The interaction of canine plasminogen with Streptococcus pyogenes enolase: they bind to one another but what is the nature of the structures involved?
    • doi:10.1371/journal.pone.0028481
    • Kornblatt MJ, Kornblatt JA, Hancock MA, (2011) The interaction of canine plasminogen with Streptococcus pyogenes enolase: they bind to one another but what is the nature of the structures involved? PLOS ONE 6: e28481. doi:10.1371/journal.pone.0028481. PubMed: 22174817.
    • (2011) PLOS ONE , vol.6
    • Kornblatt, M.J.1    Kornblatt, J.A.2    Hancock, M.A.3
  • 55
    • 12144288984 scopus 로고    scopus 로고
    • Comparative genomics of two Leptospira interrogans serovars reveals novel insights into physiology and pathogenesis
    • doi:10.1128/JB.186.7.2164-2172.2004
    • Nascimento AL, Ko AI, Martins EA, Monteiro-Vitorello CB, Ho PL, et al. (2004) Comparative genomics of two Leptospira interrogans serovars reveals novel insights into physiology and pathogenesis. J Bacteriol 186: 2164-2172. doi:10.1128/JB.186.7.2164-2172.2004. PubMed: 15028702.
    • (2004) J Bacteriol , vol.186 , pp. 2164-2172
    • Nascimento, A.L.1    Ko, A.I.2    Martins, E.A.3    Monteiro-Vitorello, C.B.4    Ho, P.L.5
  • 56
    • 34548667697 scopus 로고    scopus 로고
    • Fibrinolysis and host response in bacterial infections
    • Bergmann S, Hammerschmidt S, (2007) Fibrinolysis and host response in bacterial infections. Thromb Haemost 98: 512-520. PubMed: 17849039.
    • (2007) Thromb Haemost , vol.98 , pp. 512-520
    • Bergmann, S.1    Hammerschmidt, S.2
  • 57
    • 0032544055 scopus 로고    scopus 로고
    • A novel mechanism for the acquisition of virulence by a human influenza A virus
    • doi:10.1073/pnas.95.17.10224
    • Goto H, Kawaoka Y, (1998) A novel mechanism for the acquisition of virulence by a human influenza A virus. Proc Natl Acad Sci U S A 95: 10224-10228. doi:10.1073/pnas.95.17.10224. PubMed: 9707628.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 10224-10228
    • Goto, H.1    Kawaoka, Y.2
  • 58
    • 77956640401 scopus 로고    scopus 로고
    • Paracoccidioides brasiliensis enolase is a surface protein that binds plasminogen and mediates interaction of yeast forms with host cells
    • doi:10.1128/IAI.00221-10
    • Nogueira SV, Fonseca FL, Rodrigues ML, Mundodi V, Abi-Chacra EA, et al. (2010) Paracoccidioides brasiliensis enolase is a surface protein that binds plasminogen and mediates interaction of yeast forms with host cells. Infect Immun 78: 4040-4050. doi:10.1128/IAI.00221-10. PubMed: 20605975.
    • (2010) Infect Immun , vol.78 , pp. 4040-4050
    • Nogueira, S.V.1    Fonseca, F.L.2    Rodrigues, M.L.3    Mundodi, V.4    Abi-Chacra, E.A.5
  • 59
    • 34247870811 scopus 로고    scopus 로고
    • Genetic and proteomic evidences support the localization of yeast enolase in the cell surface
    • doi:10.1002/pmic.200500479
    • López-Villar E, Monteoliva L, Larsen MR, Sachon E, Shabaz M, et al. (2006) Genetic and proteomic evidences support the localization of yeast enolase in the cell surface. Proteomics 6 (Suppl 1):: S107-S118. doi:10.1002/pmic.200500479. PubMed: 16544286.
    • (2006) Proteomics , vol.6 , Issue.SUPPL. 1
    • López-Villar, E.1    Monteoliva, L.2    Larsen, M.R.3    Sachon, E.4    Shabaz, M.5
  • 60
    • 0034947535 scopus 로고    scopus 로고
    • Multifunctional alpha-enolase: its role in diseases
    • doi:10.1007/PL00000910
    • Pancholi V, (2001) Multifunctional alpha-enolase: its role in diseases. Cell Mol Life Sci 58: 902-920. doi:10.1007/PL00000910. PubMed: 11497239.
    • (2001) Cell Mol Life Sci , vol.58 , pp. 902-920
    • Pancholi, V.1
  • 61
    • 84857066761 scopus 로고    scopus 로고
    • The enolase of Borrelia burgdorferi is a plasminogen receptor released in outer membrane vesicles
    • doi:10.1128/IAI.05836-11
    • Toledo A, Coleman JL, Kuhlow CJ, Crowley JT, Benach JL, (2012) The enolase of Borrelia burgdorferi is a plasminogen receptor released in outer membrane vesicles. Infect Immun 80: 359-368. doi:10.1128/IAI.05836-11. PubMed: 22083700.
    • (2012) Infect Immun , vol.80 , pp. 359-368
    • Toledo, A.1    Coleman, J.L.2    Kuhlow, C.J.3    Crowley, J.T.4    Benach, J.L.5
  • 62
    • 66749148271 scopus 로고    scopus 로고
    • Surface-associated plasminogen binding of Cryptococcus neoformans promotes extracellular matrix invasion
    • doi:10.1371/journal.pone.0005780
    • Stie J, Bruni G, Fox D, (2009) Surface-associated plasminogen binding of Cryptococcus neoformans promotes extracellular matrix invasion. PLOS ONE 4: e5780. doi:10.1371/journal.pone.0005780. PubMed: 19492051.
    • (2009) PLOS ONE , vol.4
    • Stie, J.1    Bruni, G.2    Fox, D.3
  • 63
    • 33845936904 scopus 로고    scopus 로고
    • Iron limitation and expression of immunoreactive outer membrane proteins in Leptospira interrogans serovar icterohaemorrhagiae strain Lai
    • doi:10.4103/0255-0857.29414
    • Velineni S, Asuthkar S, Sritharan M, (2006) Iron limitation and expression of immunoreactive outer membrane proteins in Leptospira interrogans serovar icterohaemorrhagiae strain Lai. Indian J Med Microbiol 24: 339-342. doi:10.4103/0255-0857.29414. PubMed: 17185872.
    • (2006) Indian J Med Microbiol , vol.24 , pp. 339-342
    • Velineni, S.1    Asuthkar, S.2    Sritharan, M.3


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