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Volumn 74, Issue 9, 2006, Pages 5152-5160

Legionella pneumophila Mip, a surface-exposed peptidylproline cis-trans-isomerase, promotes the presence of phospholipase C-like activity in culture supernatants

Author keywords

[No Author keywords available]

Indexed keywords

4 NITROPHENOL; 4 NITROPHENOL PHOSPHORYLCHOLINE HYDROLASE; BACTERIAL PROTEIN; CYCLOPHILIN; FK 506 BINDING PROTEIN; HYDROLASE; MUTANT PROTEIN; PHOSPHOLIPASE C; PHOSPHORYLCHOLINE; PROTEIN MIP; UNCLASSIFIED DRUG;

EID: 33748041655     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/IAI.00484-06     Document Type: Article
Times cited : (37)

References (90)
  • 1
    • 0026680572 scopus 로고
    • PhoA gene fusions in Legionella pneumophila generated in vivo using a new transposon, MudphoA
    • Albano, M. A., J. Arroyo, B. I. Eisenstein, and N. C. Engleberg. 1992. PhoA gene fusions in Legionella pneumophila generated in vivo using a new transposon, MudphoA. Mol. Microbiol. 6:1829-1839.
    • (1992) Mol. Microbiol. , vol.6 , pp. 1829-1839
    • Albano, M.A.1    Arroyo, J.2    Eisenstein, B.I.3    Engleberg, N.C.4
  • 2
    • 0035167098 scopus 로고    scopus 로고
    • Legionella pneumophila major acid phosphatase and its role in intracellular infection
    • Aragon, V., S. Kurtz, and N. P. Cianciotto. 2001. Legionella pneumophila major acid phosphatase and its role in intracellular infection. Infect. Immun. 69:177-185.
    • (2001) Infect. Immun. , vol.69 , pp. 177-185
    • Aragon, V.1    Kurtz, S.2    Cianciotto, N.P.3
  • 3
    • 0034021895 scopus 로고    scopus 로고
    • Secreted enzymatic activities of wild-type and pilD-deficient Legionella pneumophila
    • Aragon, V., S. Kurtz, A. Flieger, B. Neumeister, and N. P. Cianciotto. 2000. Secreted enzymatic activities of wild-type and pilD-deficient Legionella pneumophila. Infect. Immun. 68:1855-1863.
    • (2000) Infect. Immun. , vol.68 , pp. 1855-1863
    • Aragon, V.1    Kurtz, S.2    Flieger, A.3    Neumeister, B.4    Cianciotto, N.P.5
  • 4
    • 0036066615 scopus 로고    scopus 로고
    • Legionella pneumophila genes that encode lipase and phospholipase C activities
    • Aragon, V., O. Rossier, and N. P. Cianciotto. 2002. Legionella pneumophila genes that encode lipase and phospholipase C activities. Microbiology 148:2223-2231.
    • (2002) Microbiology , vol.148 , pp. 2223-2231
    • Aragon, V.1    Rossier, O.2    Cianciotto, N.P.3
  • 5
    • 0035188469 scopus 로고    scopus 로고
    • Chaperone function of FkpA, a heat shock prolyl isomerase, in the periplasm of Escherichia coli
    • Arie, J. P., N. Sassoon, and J. M. Betton. 2001. Chaperone function of FkpA, a heat shock prolyl isomerase, in the periplasm of Escherichia coli. Mol. Microbiol. 39:199-210.
    • (2001) Mol. Microbiol. , vol.39 , pp. 199-210
    • Arie, J.P.1    Sassoon, N.2    Betton, J.M.3
  • 6
    • 0021838092 scopus 로고
    • Cytolytic and phospholipase C activity in Legionella species
    • Baine, W. B. 1985. Cytolytic and phospholipase C activity in Legionella species. J. Gen. Microbiol. 131:1383-1391.
    • (1985) J. Gen. Microbiol. , vol.131 , pp. 1383-1391
    • Baine, W.B.1
  • 7
    • 0023860706 scopus 로고
    • A phospholipase C from the Dallas IE strain of Legionella pneumophila serogroup 5: Purification and characterization of conditions for optimal activity with an artificial substrate
    • Baine, W. B. 1988. A phospholipase C from the Dallas IE strain of Legionella pneumophila serogroup 5: purification and characterization of conditions for optimal activity with an artificial substrate. J. Gen. Microbiol. 134:489-498.
    • (1988) J. Gen. Microbiol. , vol.134 , pp. 489-498
    • Baine, W.B.1
  • 8
    • 17644374820 scopus 로고    scopus 로고
    • Characterization of the major secreted zinc metalloprotease-dependent glycerophospholipid:cholesterol acyltransferase, PlaC, of Legionella pneumophila
    • Banerji, S., M. Bewersdorff, B. Hermes, N. P. Cianciotto, and A. Flieger. 2005. Characterization of the major secreted zinc metalloprotease-dependent glycerophospholipid:cholesterol acyltransferase, PlaC, of Legionella pneumophila. Infect. Immun. 73:2899-2909.
    • (2005) Infect. Immun. , vol.73 , pp. 2899-2909
    • Banerji, S.1    Bewersdorff, M.2    Hermes, B.3    Cianciotto, N.P.4    Flieger, A.5
  • 9
    • 0026052692 scopus 로고
    • Nucleotide sequence analysis of the Legionella micdadei mip gene, encoding a 30-kilodalton analog of the Legionella pneumophila Mip protein
    • Bangsborg, J. M., N. P. Cianciotto, and P. Hindersson. 1991. Nucleotide sequence analysis of the Legionella micdadei mip gene, encoding a 30-kilodalton analog of the Legionella pneumophila Mip protein. Infect. Immun. 59:3836-3840.
    • (1991) Infect. Immun. , vol.59 , pp. 3836-3840
    • Bangsborg, J.M.1    Cianciotto, N.P.2    Hindersson, P.3
  • 10
    • 0025743602 scopus 로고
    • Cross-reactive Legionella antigens and the antibody response during infection
    • Bangsborg, J. M., G. Shand, E. Pearlman, and N. Höiby. 1991. Cross-reactive Legionella antigens and the antibody response during infection. APMIS 99:854-865.
    • (1991) APMIS , vol.99 , pp. 854-865
    • Bangsborg, J.M.1    Shand, G.2    Pearlman, E.3    Höiby, N.4
  • 11
    • 0036849659 scopus 로고    scopus 로고
    • Crystallographic structure of SurA, a molecular chaperone that facilitates folding of outer membrane porins
    • Bitto, E., and D. B. McKay. 2002. Crystallographic structure of SurA, a molecular chaperone that facilitates folding of outer membrane porins. Structure 10:1489-1498.
    • (2002) Structure , vol.10 , pp. 1489-1498
    • Bitto, E.1    McKay, D.B.2
  • 12
    • 84988074679 scopus 로고
    • Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels
    • Blum, H., H. Beier, and H. J. Gross. 1987. Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels. Electrophoresis 8:93-99.
    • (1987) Electrophoresis , vol.8 , pp. 93-99
    • Blum, H.1    Beier, H.2    Gross, H.J.3
  • 13
    • 8844219773 scopus 로고    scopus 로고
    • Biogenesis of the Gram-negative bacterial outer membrane
    • Bos, M. P., and J. Tommassen. 2004. Biogenesis of the Gram-negative bacterial outer membrane. Curr. Opin. Microbiol. 7:610-616.
    • (2004) Curr. Opin. Microbiol. , vol.7 , pp. 610-616
    • Bos, M.P.1    Tommassen, J.2
  • 16
    • 27844506497 scopus 로고    scopus 로고
    • Type II secretion: A protein secretion system for all seasons
    • Cianciotto, N. P. 2005. Type II secretion: a protein secretion system for all seasons. Trends Microbiol. 13:581-588.
    • (2005) Trends Microbiol. , vol.13 , pp. 581-588
    • Cianciotto, N.P.1
  • 18
    • 0025340848 scopus 로고
    • A mutation in the mip gene results in an attenuation of Legionella pneumophila virulence
    • Cianciotto, N. P., B. I. Eisenstein, C. H. Mody, and N. C. Engleberg. 1990. A mutation in the mip gene results in an attenuation of Legionella pneumophila virulence. J. Infect. Dis. 162:121-126.
    • (1990) J. Infect. Dis. , vol.162 , pp. 121-126
    • Cianciotto, N.P.1    Eisenstein, B.I.2    Mody, C.H.3    Engleberg, N.C.4
  • 19
    • 0024522755 scopus 로고
    • A Legionella pneumophila gene encoding a species-specific surface protein potentiates initiation of intracellular infection
    • Cianciotto, N. P., B. I. Eisenstein, C. H. Mody, G. B. Toews, and N. C. Engleberg. 1989. A Legionella pneumophila gene encoding a species-specific surface protein potentiates initiation of intracellular infection. Infect. Immun. 57:1255-1262.
    • (1989) Infect. Immun. , vol.57 , pp. 1255-1262
    • Cianciotto, N.P.1    Eisenstein, B.I.2    Mody, C.H.3    Toews, G.B.4    Engleberg, N.C.5
  • 20
    • 0026684173 scopus 로고
    • Legionella pneumophila mip gene potentiates intracellular infection of protozoa and human macrophages
    • Cianciotto, N. P., and B. S. Fields. 1992. Legionella pneumophila mip gene potentiates intracellular infection of protozoa and human macrophages. Proc. Natl. Acad. Sci. USA 89:5188-5191.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 5188-5191
    • Cianciotto, N.P.1    Fields, B.S.2
  • 21
    • 0028944681 scopus 로고
    • Infectivity of Legionella pneumophila mip mutant for alveolar epithelial cells
    • Cianciotto, N. P., J. Kim Stamos, and D. W. Kamp. 1995. Infectivity of Legionella pneumophila mip mutant for alveolar epithelial cells. Curr. Microbiol. 30:247-250.
    • (1995) Curr. Microbiol. , vol.30 , pp. 247-250
    • Cianciotto, N.P.1    Kim Stamos, J.2    Kamp, D.W.3
  • 22
    • 0028934899 scopus 로고
    • Detection of mip-like sequences and Mip-related proteins within the family Rickettsiaceae
    • Cianciotto, N. P., W. O'Connell, G. A. Dasch, and L. P. Mallavia. 1995. Detection of mip-like sequences and Mip-related proteins within the family Rickettsiaceae. Curr. Microbiol. 30:149-153.
    • (1995) Curr. Microbiol. , vol.30 , pp. 149-153
    • Cianciotto, N.P.1    O'Connell, W.2    Dasch, G.A.3    Mallavia, L.P.4
  • 23
    • 0032527831 scopus 로고    scopus 로고
    • A new heat-shock gene, ppiD, encodes a peptidyl-prolyl isomerase required for folding of outer membrane proteins in Escherichia coli
    • Dartigalongue, C., and S. Raina. 1998. A new heat-shock gene, ppiD, encodes a peptidyl-prolyl isomerase required for folding of outer membrane proteins in Escherichia coli. EMBO J. 17:3968-3980.
    • (1998) EMBO J. , vol.17 , pp. 3968-3980
    • Dartigalongue, C.1    Raina, S.2
  • 24
    • 0141595904 scopus 로고    scopus 로고
    • Structures of immunophilins and their ligand complexes
    • Dornan, J., P. Taylor, and M. D. Walkinshaw. 2003. Structures of immunophilins and their ligand complexes. Curr. Top. Med. Chem. 3:1392-1409.
    • (2003) Curr. Top. Med. Chem. , vol.3 , pp. 1392-1409
    • Dornan, J.1    Taylor, P.2    Walkinshaw, M.D.3
  • 26
    • 0019409995 scopus 로고
    • Improved semiselective medium for isolation of Legionella pneumophila from contaminated clinical and environmental specimens
    • Edelstein, P. H. 1981. Improved semiselective medium for isolation of Legionella pneumophila from contaminated clinical and environmental specimens. J. Clin. Microbiol. 14:298-303.
    • (1981) J. Clin. Microbiol. , vol.14 , pp. 298-303
    • Edelstein, P.H.1
  • 27
    • 16444379269 scopus 로고    scopus 로고
    • Legionella
    • G. L. Mandell, J. E. Bennett, and R. Dolin (ed.). Elsevier Churchill Livingstone, Philadelphia, Pa.
    • Edelstein, P. H., and N. P. Cianciotto. 2005. Legionella, p. 2711-2724. In G. L. Mandell, J. E. Bennett, and R. Dolin (ed.), Principles and practice of infectious diseases, 6th ed., vol. 2. Elsevier Churchill Livingstone, Philadelphia, Pa.
    • (2005) Principles and Practice of Infectious Diseases, 6th Ed. , vol.2 , pp. 2711-2724
    • Edelstein, P.H.1    Cianciotto, N.P.2
  • 28
    • 0024519112 scopus 로고
    • DNAsequence of mip, a Legionella pneumophila gene associated with macrophage infectivity
    • Engleberg, N. C., C. Carter, D. R. Weber, N. P. Cianciotto, and B. I. Eisenstein. 1989. DNAsequence of mip, a Legionella pneumophila gene associated with macrophage infectivity. Infect. Immun. 57:1263-1270.
    • (1989) Infect. Immun. , vol.57 , pp. 1263-1270
    • Engleberg, N.C.1    Carter, C.2    Weber, D.R.3    Cianciotto, N.P.4    Eisenstein, B.I.5
  • 29
    • 0021361349 scopus 로고
    • Cloning and expression of Legionella pneumophila antigens in Escherichia coli
    • Engleberg, N. C., D. J. Drutz, and B. I. Eisenstein. 1984. Cloning and expression of Legionella pneumophila antigens in Escherichia coli. Infect. Immun. 44:222-227.
    • (1984) Infect. Immun. , vol.44 , pp. 222-227
    • Engleberg, N.C.1    Drutz, D.J.2    Eisenstein, B.I.3
  • 30
    • 0025935106 scopus 로고
    • Progress in the pathogenesis of Legionella pneumophila
    • Engleberg, N. C., and B. I. Eisenstein. 1991. Progress in the pathogenesis of Legionella pneumophila. Microb. Pathog. 10:11-13.
    • (1991) Microb. Pathog. , vol.10 , pp. 11-13
    • Engleberg, N.C.1    Eisenstein, B.I.2
  • 31
    • 0021284305 scopus 로고
    • Legionella pneumophila surface antigens cloned and expressed in Escherichia coli are trans-located to the host cell surface and interact with specific anti-Legionella antibodies
    • Engleberg, N. C., E. Pearlman, and B. I. Eisenstein. 1984. Legionella pneumophila surface antigens cloned and expressed in Escherichia coli are trans-located to the host cell surface and interact with specific anti-Legionella antibodies. J. Bacteriol. 160:199-203.
    • (1984) J. Bacteriol. , vol.160 , pp. 199-203
    • Engleberg, N.C.1    Pearlman, E.2    Eisenstein, B.I.3
  • 32
    • 0036314980 scopus 로고    scopus 로고
    • Legionella and Legionnaires' disease: 25 Years of investigation
    • Fields, B. S., R. F. Benson, and R. E. Besser. 2002. Legionella and Legionnaires' disease: 25 years of investigation. Clin. Microbiol. Rev. 15:506-526.
    • (2002) Clin. Microbiol. Rev. , vol.15 , pp. 506-526
    • Fields, B.S.1    Benson, R.F.2    Besser, R.E.3
  • 33
    • 8844269404 scopus 로고    scopus 로고
    • The underlying mechanisms of type II protein secretion
    • Filloux, A. 2004. The underlying mechanisms of type II protein secretion. Biochim. Biophys. Acta Mol. Cell Res. 1694:163-179.
    • (2004) Biochim. Biophys. Acta Mol. Cell Res. , vol.1694 , pp. 163-179
    • Filloux, A.1
  • 34
    • 0026511332 scopus 로고
    • Mip protein of Legionella pneumophila exhibits peptidyl-prolyl-cis/trans isomerase (PPlase) activity
    • Fischer, G., H. Bang, B. Ludwig, K. Mann, and J. Hacker. 1992. Mip protein of Legionella pneumophila exhibits peptidyl-prolyl-cis/trans isomerase (PPlase) activity. Mol. Microbiol. 6:1375-1383.
    • (1992) Mol. Microbiol. , vol.6 , pp. 1375-1383
    • Fischer, G.1    Bang, H.2    Ludwig, B.3    Mann, K.4    Hacker, J.5
  • 35
    • 28444443093 scopus 로고    scopus 로고
    • Detection of Legionella pneumophila in water samples by species-specific real-time and nested PCR assays
    • Fiume, L., M. A. Bucci Sabattini, and G. Poda. 2005. Detection of Legionella pneumophila in water samples by species-specific real-time and nested PCR assays. Lett. Appl. Microbiol. 41:470-475.
    • (2005) Lett. Appl. Microbiol. , vol.41 , pp. 470-475
    • Fiume, L.1    Bucci Sabattini, M.A.2    Poda, G.3
  • 36
    • 0034002742 scopus 로고    scopus 로고
    • Critical evaluation of p-nitrophenylphosphorylcholine (p-NPPC) as artificial substrate for the detection of phospholipase C
    • Flieger, A., S. Gong, M. Faigle, and B. Neumeister. 2000. Critical evaluation of p-nitrophenylphosphorylcholine (p-NPPC) as artificial substrate for the detection of phospholipase C. Enzyme Microb. Technol. 26:451-458.
    • (2000) Enzyme Microb. Technol. , vol.26 , pp. 451-458
    • Flieger, A.1    Gong, S.2    Faigle, M.3    Neumeister, B.4
  • 38
    • 0036840406 scopus 로고    scopus 로고
    • Characterization of the gene encoding the major secreted lysophospholipase A of Legionella pneumophila and its role in detoxification of lysophosphatidylcholine
    • Flieger, A., B. Neumeister, and N. P. Cianciotto. 2002. Characterization of the gene encoding the major secreted lysophospholipase A of Legionella pneumophila and its role in detoxification of lysophosphatidylcholine. Infect. Immun. 70:6094-6106.
    • (2002) Infect. Immun. , vol.70 , pp. 6094-6106
    • Flieger, A.1    Neumeister, B.2    Cianciotto, N.P.3
  • 39
    • 0032967321 scopus 로고    scopus 로고
    • Legionella pneumophila contains a type II general secretion pathway required for growth in amoebae as well as for secretion of the Msp protease
    • Hales, L. M., and H. A. Shuman. 1999. Legionella pneumophila contains a type II general secretion pathway required for growth in amoebae as well as for secretion of the Msp protease. Infect. Immun. 67:3662-3666.
    • (1999) Infect. Immun. , vol.67 , pp. 3662-3666
    • Hales, L.M.1    Shuman, H.A.2
  • 40
    • 0035135102 scopus 로고    scopus 로고
    • Immunolocalization of the Mip protein of intracellularly and extracellularly grown Legionella pneumophila
    • Heibig, J. H., P. C. Luck, M. Steinert, E. Jacobs, and M. Witt. 2001. Immunolocalization of the Mip protein of intracellularly and extracellularly grown Legionella pneumophila. Lett. Appl. Microbiol. 32:83-88.
    • (2001) Lett. Appl. Microbiol. , vol.32 , pp. 83-88
    • Heibig, J.H.1    Luck, P.C.2    Steinert, M.3    Jacobs, E.4    Witt, M.5
  • 41
    • 0028933883 scopus 로고
    • Monoclonal antibodies to Legionella Mip proteins recognize genus-and species-specific epitopes
    • Helbig, J. H., B. Ludwig, P. C. Luck, A. Groh, W. Witzleb, and J. Hacker. 1995. Monoclonal antibodies to Legionella Mip proteins recognize genus-and species-specific epitopes. Clin. Diagn. Lab. Immunol. 2:160-165.
    • (1995) Clin. Diagn. Lab. Immunol. , vol.2 , pp. 160-165
    • Helbig, J.H.1    Ludwig, B.2    Luck, P.C.3    Groh, A.4    Witzleb, W.5    Hacker, J.6
  • 42
    • 21244447713 scopus 로고    scopus 로고
    • The periplasmic chaperone SurA exploits two features characteristic of integral outer membrane proteins for selective substrate recognition
    • Hennecke, G., J. Nolte, R. Volkmer-Engert, J. Schneider-Mergener, and S. Behrens. 2005. The periplasmic chaperone SurA exploits two features characteristic of integral outer membrane proteins for selective substrate recognition. J. Biol. Chem. 280:23540-23548.
    • (2005) J. Biol. Chem. , vol.280 , pp. 23540-23548
    • Hennecke, G.1    Nolte, J.2    Volkmer-Engert, R.3    Schneider-Mergener, J.4    Behrens, S.5
  • 43
    • 0031024992 scopus 로고    scopus 로고
    • Decreased intracellular survival of an fkpA mutant of Salmonella typhimurium Copenhagen
    • Home, S. M., T. J. Kottom, L. K. Nolan, and K. D. Young. 1997. Decreased intracellular survival of an fkpA mutant of Salmonella typhimurium Copenhagen. Infect. Immun. 65:806-810.
    • (1997) Infect. Immun. , vol.65 , pp. 806-810
    • Home, S.M.1    Kottom, T.J.2    Nolan, L.K.3    Young, K.D.4
  • 46
    • 0032967308 scopus 로고    scopus 로고
    • Differences in the carboxy-terminal (putative phospholipid binding) domains of Clostridium perfringens and Clostridium bifermentans phospholipases C influence the hemolytic and lethal properties of these enzymes
    • Jepson, M., A. Howells, H. L. Bullifent, B. Bolgiano, D. Crane, J. Miller, J, Holley, P. Jayasekera, and R. W. Titball. 1999. Differences in the carboxy-terminal (putative phospholipid binding) domains of Clostridium perfringens and Clostridium bifermentans phospholipases C influence the hemolytic and lethal properties of these enzymes. Infect. Immun. 67:3297-3301.
    • (1999) Infect. Immun. , vol.67 , pp. 3297-3301
    • Jepson, M.1    Howells, A.2    Bullifent, H.L.3    Bolgiano, B.4    Crane, D.5    Miller, J.6    Holley, J.7    Jayasekera, P.8    Titball, R.W.9
  • 47
    • 27744565064 scopus 로고    scopus 로고
    • Periplasmic peptidyl prolyl cis-trans isomerases are not essential for viability, but SurA is required for pilus biogenesis in Escherichia coli
    • Justice, S. S., D. A. Hunstad, J. R. Harper, A. R. Duguay, J. S. Pinkner, J. Bann, C. Frieden, T. J. Silhavy, and S. J. Hultgren. 2005. Periplasmic peptidyl prolyl cis-trans isomerases are not essential for viability, but SurA is required for pilus biogenesis in Escherichia coli. J. Bacteriol. 187:7680-7686.
    • (2005) J. Bacteriol. , vol.187 , pp. 7680-7686
    • Justice, S.S.1    Hunstad, D.A.2    Harper, J.R.3    Duguay, A.R.4    Pinkner, J.S.5    Bann, J.6    Frieden, C.7    Silhavy, T.J.8    Hultgren, S.J.9
  • 48
    • 0033979096 scopus 로고    scopus 로고
    • Expression and use of the green fluorescent protein as a reporter system in Legionella pneumophila
    • Kohler, R., A. Bubert, W. Goebel, M. Steinert, J. Hacker, and B. Bubert. 2000. Expression and use of the green fluorescent protein as a reporter system in Legionella pneumophila. Mol. Gen. Genet. 262:1060-1069.
    • (2000) Mol. Gen. Genet. , vol.262 , pp. 1060-1069
    • Kohler, R.1    Bubert, A.2    Goebel, W.3    Steinert, M.4    Hacker, J.5    Bubert, B.6
  • 49
    • 0042265192 scopus 로고    scopus 로고
    • Biochemical and functional analyses of the Mip protein: Influence of the N-terminal half and of peptidylprolyl isomerase activity on the virulence of Legionella pneumophila
    • Kohler, R., J. Fanghanel, B. Konig, E. Luneberg, M. Frosch, J. U. Rahfeld, R. Hilgenfeld, G. Fischer, J. Hacker, and M. Steinert. 2003. Biochemical and functional analyses of the Mip protein: influence of the N-terminal half and of peptidylprolyl isomerase activity on the virulence of Legionella pneumophila. Infect. Immun. 71:4389-4397.
    • (2003) Infect. Immun. , vol.71 , pp. 4389-4397
    • Kohler, R.1    Fanghanel, J.2    Konig, B.3    Luneberg, E.4    Frosch, M.5    Rahfeld, J.U.6    Hilgenfeld, R.7    Fischer, G.8    Hacker, J.9    Steinert, M.10
  • 50
    • 27444447753 scopus 로고    scopus 로고
    • Ng-MIP, a surface-exposed lipoprotein of Neisseria gonorrhoeae, has a peptidyl-prolyl cis/trans isomerase (PPIase) activity and is involved in persistence in macrophages
    • Leuzzi, R., L. Serino, M. Scarselli, S. Savino, M. R. Fontana, E. Monaci, A. Taddei, G. Fischer, R. Rappuoli, and M. Pizza. 2005. Ng-MIP, a surface-exposed lipoprotein of Neisseria gonorrhoeae, has a peptidyl-prolyl cis/trans isomerase (PPIase) activity and is involved in persistence in macrophages. Mol. Microbiol. 58:669-681.
    • (2005) Mol. Microbiol. , vol.58 , pp. 669-681
    • Leuzzi, R.1    Serino, L.2    Scarselli, M.3    Savino, S.4    Fontana, M.R.5    Monaci, E.6    Taddei, A.7    Fischer, G.8    Rappuoli, R.9    Pizza, M.10
  • 51
    • 0032907336 scopus 로고    scopus 로고
    • The prepilin peptidase is required for protein secretion by and the virulence of the intracellular pathogen Legionella pneumophila
    • Lues, M. R., P. H. Edelstein, and N. P. Cianciotto. 1999. The prepilin peptidase is required for protein secretion by and the virulence of the intracellular pathogen Legionella pneumophila. Mol. Microbiol. 31:959-970.
    • (1999) Mol. Microbiol. , vol.31 , pp. 959-970
    • Lues, M.R.1    Edelstein, P.H.2    Cianciotto, N.P.3
  • 52
    • 0032038704 scopus 로고    scopus 로고
    • Identification and temperature regulation of Legionella pneumophila genes involved in type IV pilus biogenesis and type II protein secretion
    • Liles, M. R., V. K. Viswanathan, and N. P. Cianciotto. 1998. Identification and temperature regulation of Legionella pneumophila genes involved in type IV pilus biogenesis and type II protein secretion. Infect. Immun. 66:1776-1782.
    • (1998) Infect. Immun. , vol.66 , pp. 1776-1782
    • Liles, M.R.1    Viswanathan, V.K.2    Cianciotto, N.P.3
  • 54
    • 0032768537 scopus 로고    scopus 로고
    • Cloning, sequencing, and role in virulence of two phospholipases (A1 and C) from mesophilic Aeromonas sp. serogroup O:34
    • Merino, S., A. Aguilar, M. M. Nogueras, M. Regue, S. Swift, and J. M. Tomas. 1999. Cloning, sequencing, and role in virulence of two phospholipases (A1 and C) from mesophilic Aeromonas sp. serogroup O:34. Infect. Immun. 67:4008-4013.
    • (1999) Infect. Immun. , vol.67 , pp. 4008-4013
    • Merino, S.1    Aguilar, A.2    Nogueras, M.M.3    Regue, M.4    Swift, S.5    Tomas, J.M.6
  • 55
    • 0028832453 scopus 로고
    • Molecular cloning of a Coxiella burnetii gene encoding a macrophage infectivity potentiator (Mip) analogue
    • Mo, Y. Y., N. P. Cianciotto, and L. P. Mallavia. 1995. Molecular cloning of a Coxiella burnetii gene encoding a macrophage infectivity potentiator (Mip) analogue. Microbiology 141:2861-2871.
    • (1995) Microbiology , vol.141 , pp. 2861-2871
    • Mo, Y.Y.1    Cianciotto, N.P.2    Mallavia, L.P.3
  • 56
    • 0019465110 scopus 로고
    • Enzymatic profile of Legionella pneumophilia
    • Muller, H. E. 1981. Enzymatic profile of Legionella pneumophilia. J. Clin. Microbiol. 13:423-426.
    • (1981) J. Clin. Microbiol. , vol.13 , pp. 423-426
    • Muller, H.E.1
  • 57
    • 0020056969 scopus 로고
    • Enzymatic activities of Legionella pneumophila and Legionella-like organisms
    • Nolte, F. S., G. E. Hollick, and R. G. Robertson. 1982. Enzymatic activities of Legionella pneumophila and Legionella-like organisms. J. Clin. Microbiol. 15:175-177.
    • (1982) J. Clin. Microbiol. , vol.15 , pp. 175-177
    • Nolte, F.S.1    Hollick, G.E.2    Robertson, R.G.3
  • 58
    • 0029098198 scopus 로고
    • Characterization of a Legionella micdadei mip mutant
    • O'Connell, W. A., J. M. Bangsborg, and N. P. Cianciotto. 1995. Characterization of a Legionella micdadei mip mutant. Infect. Immun. 63:2840-2845.
    • (1995) Infect. Immun. , vol.63 , pp. 2840-2845
    • O'Connell, W.A.1    Bangsborg, J.M.2    Cianciotto, N.P.3
  • 61
    • 0035139918 scopus 로고    scopus 로고
    • Identification of Legionella pneumophila genes important for infection of amoebas by signature-tagged mutagenesis
    • Polesky, A. H., J. T. Ross, S. Falkow, and L. S. Tompkins. 2001. Identification of Legionella pneumophila genes important for infection of amoebas by signature-tagged mutagenesis. Infect. Immun. 69:977-987.
    • (2001) Infect. Immun. , vol.69 , pp. 977-987
    • Polesky, A.H.1    Ross, J.T.2    Falkow, S.3    Tompkins, L.S.4
  • 62
    • 0034792492 scopus 로고    scopus 로고
    • Molecular characterization of a phosphatidylcholine-hydrolyzing phospholipase C
    • Preuss, I., I. Kaiser, and U. Gehring. 2001. Molecular characterization of a phosphatidylcholine-hydrolyzing phospholipase C. Eur. J. Biochem. 268:5081-5091.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 5081-5091
    • Preuss, I.1    Kaiser, I.2    Gehring, U.3
  • 63
    • 0030924593 scopus 로고    scopus 로고
    • Interspecies sequence differences in the Mip protein from the genus Legionella: Implications for function and evolutionary relatedness
    • Ratclitf, R. M., S. C. Donnellan, J. A. Lanser, P. A. Manning, and M. W. Heuzenroeder. 1997. Interspecies sequence differences in the Mip protein from the genus Legionella: implications for function and evolutionary relatedness. Mol. Microbiol. 25:1149-1158.
    • (1997) Mol. Microbiol. , vol.25 , pp. 1149-1158
    • Ratclitf, R.M.1    Donnellan, S.C.2    Lanser, J.A.3    Manning, P.A.4    Heuzenroeder, M.W.5
  • 64
    • 0031977470 scopus 로고    scopus 로고
    • Sequence-based classification scheme for the genus Legionella targeting the mip gene
    • Ratcliff, R. M., J. A. Lanser, P. A. Manning, and M. W. Heuzenroeder. 1998. Sequence-based classification scheme for the genus Legionella targeting the mip gene. J. Clin. Microbiol. 36:1560-1567.
    • (1998) J. Clin. Microbiol. , vol.36 , pp. 1560-1567
    • Ratcliff, R.M.1    Lanser, J.A.2    Manning, P.A.3    Heuzenroeder, M.W.4
  • 66
    • 0029729863 scopus 로고    scopus 로고
    • Distribution of mip-related sequences in 39 species (48 serogroups) of Legionellaceae
    • Ritfard, S., F. Vandenesch, M. Reyrolle, and J. Etienne. 1996. Distribution of mip-related sequences in 39 species (48 serogroups) of Legionellaceae. Epidemiol. Infect. 117:501-506.
    • (1996) Epidemiol. Infect. , vol.117 , pp. 501-506
    • Ritfard, S.1    Vandenesch, F.2    Reyrolle, M.3    Etienne, J.4
  • 67
    • 0030005736 scopus 로고    scopus 로고
    • A 28 kDa major immunogen of Chlamydia psittaci shares identity with Mip proteins of Legionella spp. and Chlamydia trachomatis-cloning and characterization of the C. psittaci mip-like gene
    • Rockey, D. D., B. B. Chesebro, R. A. Heinzen, and T. Hackstadt. 1996. A 28 kDa major immunogen of Chlamydia psittaci shares identity with Mip proteins of Legionella spp. and Chlamydia trachomatis-cloning and characterization of the C. psittaci mip-like gene. Microbiology 142:945-953.
    • (1996) Microbiology , vol.142 , pp. 945-953
    • Rockey, D.D.1    Chesebro, B.B.2    Heinzen, R.A.3    Hackstadt, T.4
  • 68
    • 16244414601 scopus 로고    scopus 로고
    • The Legionella pneumophila tatB gene facilitates secretion of phospholipase C, growth under iron-limiting conditions, and intracellular infection
    • Rossier, O., and N. P. Cianciotto. 2005. The Legionella pneumophila tatB gene facilitates secretion of phospholipase C, growth under iron-limiting conditions, and intracellular infection. Infect. Immun. 73:2020-2032.
    • (2005) Infect. Immun. , vol.73 , pp. 2020-2032
    • Rossier, O.1    Cianciotto, N.P.2
  • 69
    • 0035077415 scopus 로고    scopus 로고
    • Type II protein secretion is a subset of the PilD-dependent processes that facilitate intracellular infection by Legionella pneumophila
    • Rossier, O., and N. P. Cianciotto. 2001. Type II protein secretion is a subset of the PilD-dependent processes that facilitate intracellular infection by Legionella pneumophila. Infect. Immun. 69:2092-2098.
    • (2001) Infect. Immun. , vol.69 , pp. 2092-2098
    • Rossier, O.1    Cianciotto, N.P.2
  • 70
    • 0346251028 scopus 로고    scopus 로고
    • Legionella pneumophila type II protein secretion promotes virulence in the A/J mouse model of Legionnaires' disease pneumonia
    • Rossier, O., S. Starkenburg, and N. P. Cianciotto. 2004. Legionella pneumophila type II protein secretion promotes virulence in the A/J mouse model of Legionnaires' disease pneumonia. Infect. Immun. 72:310-321.
    • (2004) Infect. Immun. , vol.72 , pp. 310-321
    • Rossier, O.1    Starkenburg, S.2    Cianciotto, N.P.3
  • 71
    • 0031025290 scopus 로고    scopus 로고
    • Topology of Legionella pneumophila DotA: An inner membrane protein required for replication in macrophages
    • Roy, C. R., and R. R. Isberg. 1997. Topology of Legionella pneumophila DotA: an inner membrane protein required for replication in macrophages. Infect. Immun. 65:571-578.
    • (1997) Infect. Immun. , vol.65 , pp. 571-578
    • Roy, C.R.1    Isberg, R.R.2
  • 72
    • 31344479308 scopus 로고    scopus 로고
    • Advances in understanding bacterial outer-membrane biogenesis
    • Ruiz, N., D. Kahne, and T. J. Silhavy. 2006. Advances in understanding bacterial outer-membrane biogenesis. Nat. Rev. Microbiol. 4:57-66.
    • (2006) Nat. Rev. Microbiol. , vol.4 , pp. 57-66
    • Ruiz, N.1    Kahne, D.2    Silhavy, T.J.3
  • 74
    • 0035029580 scopus 로고    scopus 로고
    • Biology of type II secretion
    • Sandkvist, M. 2001. Biology of type II secretion. Mol. Microbiol. 40:271-283.
    • (2001) Mol. Microbiol. , vol.40 , pp. 271-283
    • Sandkvist, M.1
  • 75
    • 0035019730 scopus 로고    scopus 로고
    • Type II secretion and pathogenesis
    • Sandkvist, M. 2001. Type II secretion and pathogenesis. Infect. Immun. 69:3523-3535.
    • (2001) Infect. Immun. , vol.69 , pp. 3523-3535
    • Sandkvist, M.1
  • 76
    • 0346366809 scopus 로고    scopus 로고
    • Structural and functional studies of FkpA from Escherichia coli, a cis/trans peptidyl-prolyl isomerase with chaperone activity
    • Saul, F. A., J. P. Arie, B. Vulliez-le Normand, R. Kahn, J. M. Betton, and G. A. Bentley. 2004. Structural and functional studies of FkpA from Escherichia coli, a cis/trans peptidyl-prolyl isomerase with chaperone activity. J. Mol. Biol. 335:595-608.
    • (2004) J. Mol. Biol. , vol.335 , pp. 595-608
    • Saul, F.A.1    Arie, J.P.2    Vulliez-Le Normand, B.3    Kahn, R.4    Betton, J.M.5    Bentley, G.A.6
  • 77
    • 0029133292 scopus 로고
    • Small-angle X-ray solution scattering study on the dimerization of the FKBP25mem from Legionella pneumophila
    • Schmidt, B., S. Konig, D. Svergun, V. Volkov, G. Fischer, and M. H. Koch. 1995. Small-angle X-ray solution scattering study on the dimerization of the FKBP25mem from Legionella pneumophila. FEBS Lett. 372:169-172.
    • (1995) FEBS Lett. , vol.372 , pp. 169-172
    • Schmidt, B.1    Konig, S.2    Svergun, D.3    Volkov, V.4    Fischer, G.5    Koch, M.H.6
  • 78
    • 0028074989 scopus 로고
    • A homodimer represents an active species of the peptidyl-prolyl cis/trans isomerase FKBP25mem from Legionella pneumophila
    • Schmidt, B., J. Rahfeld, A. Schierhorn, B. Ludwig, J. Hacker, and G. Fischer. 1994. A homodimer represents an active species of the peptidyl-prolyl cis/trans isomerase FKBP25mem from Legionella pneumophila. FEBS Lett. 352:185-190.
    • (1994) FEBS Lett. , vol.352 , pp. 185-190
    • Schmidt, B.1    Rahfeld, J.2    Schierhorn, A.3    Ludwig, B.4    Hacker, J.5    Fischer, G.6
  • 79
    • 30144446085 scopus 로고    scopus 로고
    • SlyD proteins from different species exhibit high prolyl isomerase and chaperone activities
    • Scholz, C., B. Eckert, F. Hagn, P. Schaarschmidt, J. Balbach, and F. X. Schmid. 2006. SlyD proteins from different species exhibit high prolyl isomerase and chaperone activities. Biochemistry 45:20-33.
    • (2006) Biochemistry , vol.45 , pp. 20-33
    • Scholz, C.1    Eckert, B.2    Hagn, F.3    Schaarschmidt, P.4    Balbach, J.5    Schmid, F.X.6
  • 80
    • 2942544266 scopus 로고    scopus 로고
    • The type II protein secretion system of Legionella pneumophila promotes growth at low temperatures
    • Söderberg, M. A, O. Rossier, and N. P. Cianciotto. 2004. The type II protein secretion system of Legionella pneumophila promotes growth at low temperatures. J. Bacteriol. 186:3712-3720.
    • (2004) J. Bacteriol. , vol.186 , pp. 3712-3720
    • Söderberg, M.A.1    Rossier, O.2    Cianciotto, N.P.3
  • 81
    • 0029944643 scopus 로고    scopus 로고
    • De novo synthesis of Legionella pneumophila antigens during intracellular growth in phagocytic cells
    • Susa, M., J. Hacker, and R. Marre. 1996. De novo synthesis of Legionella pneumophila antigens during intracellular growth in phagocytic cells. Infect. Immun. 64:1679-1684.
    • (1996) Infect. Immun. , vol.64 , pp. 1679-1684
    • Susa, M.1    Hacker, J.2    Marre, R.3
  • 82
    • 0034566380 scopus 로고    scopus 로고
    • Legionella pneumophila pathogenesis: A fateful journey from amoebae to macrophages
    • Swanson, M. S., and B. K. Hammer. 2000. Legionella pneumophila pathogenesis: a fateful journey from amoebae to macrophages. Annu. Rev. Microbiol. 54:567-613.
    • (2000) Annu. Rev. Microbiol. , vol.54 , pp. 567-613
    • Swanson, M.S.1    Hammer, B.K.2
  • 83
    • 0032947599 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa hemolytic phospholipase C suppresses neutrophil respiratory burst activity
    • Terada, L. S., K. A. Johansen, S. Nowbar, A. I. Vasil, and M. L. Vasil. 1999. Pseudomonas aeruginosa hemolytic phospholipase C suppresses neutrophil respiratory burst activity. Infect. Immun. 67:2371-2376.
    • (1999) Infect. Immun. , vol.67 , pp. 2371-2376
    • Terada, L.S.1    Johansen, K.A.2    Nowbar, S.3    Vasil, A.I.4    Vasil, M.L.5
  • 84
    • 0019500110 scopus 로고
    • Extracellular enzymes of Legionella pneumophila
    • Thorpe, T. C., and R. D. Miller. 1981. Extracellular enzymes of Legionella pneumophila. Infect. Immun. 33:632-635.
    • (1981) Infect. Immun. , vol.33 , pp. 632-635
    • Thorpe, T.C.1    Miller, R.D.2
  • 85
    • 0037348510 scopus 로고    scopus 로고
    • The extracytoplasmic folding factor PrsA is required for protein secretion only in the presence of the cell wall in Bacillus subtilis
    • Wahlstrom, E., M. Vitikainen, V. P. Kontinen, and M. Sarvas. 2003. The extracytoplasmic folding factor PrsA is required for protein secretion only in the presence of the cell wall in Bacillus subtilis. Microbiology 149:569-577.
    • (2003) Microbiology , vol.149 , pp. 569-577
    • Wahlstrom, E.1    Vitikainen, M.2    Kontinen, V.P.3    Sarvas, M.4
  • 86
    • 0345034820 scopus 로고    scopus 로고
    • Regulation of expression of the nonhemolytic phospholipase C of Burkholderia cepacia
    • Weingart, C. L., and A. M. Hooke. 1999. Regulation of expression of the nonhemolytic phospholipase C of Burkholderia cepacia. Curr. Microbiol. 39:336-341.
    • (1999) Curr. Microbiol. , vol.39 , pp. 336-341
    • Weingart, C.L.1    Hooke, A.M.2
  • 87
    • 0037129846 scopus 로고    scopus 로고
    • Regulation of the Legionella mip-promotor during infection of human monocytes
    • Wieland, H, M. Faigle, F. Lang, H. Northoff, and B. Neumeister. 2002. Regulation of the Legionella mip-promotor during infection of human monocytes. FEMS Microbiol. Lett. 212:127-132.
    • (2002) FEMS Microbiol. Lett. , vol.212 , pp. 127-132
    • Wieland, H.1    Faigle, M.2    Lang, F.3    Northoff, H.4    Neumeister, B.5
  • 90
    • 0028846924 scopus 로고
    • Influence of site specifically altered Mip proteins on intracellular survival of Legionella pneumophila in eukaryotic cells
    • Wintermeyer, E., B. Ludwig, M. Steinert, B. Schmidt, G. Fischer, and J. Hacker. 1995. Influence of site specifically altered Mip proteins on intracellular survival of Legionella pneumophila in eukaryotic cells. Infect. Immun. 63:4576-4583.
    • (1995) Infect. Immun. , vol.63 , pp. 4576-4583
    • Wintermeyer, E.1    Ludwig, B.2    Steinert, M.3    Schmidt, B.4    Fischer, G.5    Hacker, J.6


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