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Volumn 79, Issue 11, 2011, Pages 4299-4307

A burkholderia pseudomallei macrophage infectivity potentiator-like protein has rapamycin-inhibitable peptidylprolyl isomerase activity and pleiotropic effects on virulence

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; BPSS1823 PROTEIN; FK 506 BINDING PROTEIN; MACROPHAGE INFECTIVITY POTENTIATOR; PEPTIDYLPROLYL ISOMERASE; RAPAMYCIN; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG; VIRULENCE FACTOR;

EID: 80855129356     PISSN: 00199567     EISSN: 10985522     Source Type: Journal    
DOI: 10.1128/IAI.00134-11     Document Type: Article
Times cited : (38)

References (45)
  • 1
    • 70349668852 scopus 로고    scopus 로고
    • The molecular and cellular basis of pathogenesis in melioidosis: how does Burkholderia pseudomallei cause disease?
    • Adler, N. R. L., et al. 2009. The molecular and cellular basis of pathogenesis in melioidosis: how does Burkholderia pseudomallei cause disease? FEMS Microbiol. Rev. 33:1079-1099.
    • (2009) FEMS Microbiol Rev. , vol.33 , pp. 1079-1099
    • Adler, N.R.L.1
  • 2
    • 0019967719 scopus 로고
    • Proteolytic activity of rumen microorganisms and effects of proteinase-inhibitors
    • Brock, F. M., C. W. Forsberg, and J. G. Buchanansmith. 1982. Proteolytic activity of rumen microorganisms and effects of proteinase-inhibitors. Appl. Environ. Microbiol. 44:561-569.
    • (1982) Appl. Environ. Microbiol. , vol.44 , pp. 561-569
    • Brock, F.M.1    Forsberg, C.W.2    Buchanansmith, J.G.3
  • 3
    • 42149162252 scopus 로고    scopus 로고
    • Solution structure of the Legionella pneumophila Mip-rapamycin complex
    • Ceymann, A., et al. 2008. Solution structure of the Legionella pneumophila Mip-rapamycin complex. BMC Struct. Biol. 8:17.
    • (2008) BMC Struct. Biol. , vol.8 , pp. 17
    • Ceymann, A.1
  • 4
    • 17444369030 scopus 로고    scopus 로고
    • Melioidosis: epidemiology, pathophysiology, and management
    • Cheng, A. C., and B. J. Currie. 2005. Melioidosis: epidemiology, pathophysiology, and management. Clin. Microbiol. Rev. 18:383-416.
    • (2005) Clin. Microbiol. Rev. , vol.18 , pp. 383-416
    • Cheng, A.C.1    Currie, B.J.2
  • 5
    • 0037379533 scopus 로고    scopus 로고
    • Flagella are virulence determinants of Burkholderia pseudomallei
    • Chua, K. L., Y. Y. Chan, and Y. H. Gan. 2003. Flagella are virulence determinants of Burkholderia pseudomallei. Infect. Immun. 71:1622-1629.
    • (2003) Infect. Immun. , vol.71 , pp. 1622-1629
    • Chua, K.L.1    Chan, Y.Y.2    Gan, Y.H.3
  • 7
    • 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
  • 8
    • 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
  • 9
    • 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. U. S. A. 89:5188-5191.
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 5188-5191
    • Cianciotto, N.P.1    Fields, B.S.2
  • 10
    • 0345601067 scopus 로고    scopus 로고
    • Intensity of rainfall and severity of melioidosis, Australia
    • Currie, B. J., and S. P. Jacups. 2003. Intensity of rainfall and severity of melioidosis, Australia. Emerg. Infect. Dis. 9:1538-1542.
    • (2003) Emerg. Infect. Dis. , vol.9 , pp. 1538-1542
    • Currie, B.J.1    Jacups, S.P.2
  • 11
    • 0033213982 scopus 로고    scopus 로고
    • Phagosomal maturation, acidification, and inhibition of bacterial growth in nonphagocytic cells transfected with Fc gamma RIIA receptors
    • Downey, G. P., et al. 1999. Phagosomal maturation, acidification, and inhibition of bacterial growth in nonphagocytic cells transfected with Fc gamma RIIA receptors. J. Biol. Chem. 274:28436-28444.
    • (1999) J. Biol. Chem. , vol.274 , pp. 28436-28444
    • Downey, G.P.1
  • 12
    • 43749107283 scopus 로고    scopus 로고
    • Comparative protein structure modeling using Modeller
    • Eswar, N., et al. 2006. Comparative protein structure modeling using Modeller. Curr. Protoc. Bioinformatics 5:5.6.
    • (2006) Curr. Protoc. Bioinformatics 5:5. , pp. 6
    • Eswar, N.1
  • 13
    • 0000527903 scopus 로고
    • Replication of an origin-containing derivative of plasmid RK2 dependent on a plasmid function provided in trans
    • Figurski, D. H., and D. R. Helinski. 1979. Replication of an origin-containing derivative of plasmid RK2 dependent on a plasmid function provided in trans. Proc. Natl. Acad. Sci. U. S. A. 76:1648-1652.
    • (1979) Proc. Natl. Acad. Sci. U. S. A. , vol.76 , pp. 1648-1652
    • Figurski, D.H.1    Helinski, D.R.2
  • 14
    • 0021668676 scopus 로고
    • Detection of enzyme catalysis for cis-trans isomerization of peptide-bonds using proline-containing peptides as substrates
    • Fischer, G., H. Bang, and C. Mech. 1984. Detection of enzyme catalysis for cis-trans isomerization of peptide-bonds using proline-containing peptides as substrates. Biomed. Biochim. Acta 43:1101-1111.
    • (1984) Biomed. Biochim. Acta , vol.43 , pp. 1101-1111
    • Fischer, G.1    Bang, H.2    Mech, C.3
  • 15
    • 0033980498 scopus 로고    scopus 로고
    • Protease production by Burkholderia pseudomallei and virulence in mice
    • Gauthier, Y. P., F. M. Thibault, J. C. Paucod, and D. R. Vidal. 2000. Protease production by Burkholderia pseudomallei and virulence in mice. Acta Trop. 74:215-220.
    • (2000) Acta Trop. , vol.74 , pp. 215-220
    • Gauthier, Y.P.1    Thibault, F.M.2    Paucod, J.C.3    Vidal, D.R.4
  • 16
    • 17644413069 scopus 로고    scopus 로고
    • Vanishingly low levels of Ess1 prolyl-isomerase activity are sufficient for growth in Saccharomyces cerevisiae
    • Gemmill, T. R., X. Y. Wu, and S. D. Hanes. 2005. Vanishingly low levels of Ess1 prolyl-isomerase activity are sufficient for growth in Saccharomyces cerevisiae. J. Biol. Chem. 280:15510-15517.
    • (2005) J. Biol. Chem. , vol.280 , pp. 15510-15517
    • Gemmill, T.R.1    Wu, X.Y.2    Hanes, S.D.3
  • 17
    • 0031610305 scopus 로고    scopus 로고
    • An ultrastructural study of the phagocytosis of Burkholderia pseudomallei
    • Harley, V. S., D. A. B. Dance, G. Tovey, M. V. McCrossan, and B. S. Drasar. 1998. An ultrastructural study of the phagocytosis of Burkholderia pseudomallei. Microbios 94:35-45.
    • (1998) Microbios , vol.94 , pp. 35-45
    • Harley, V.S.1    Dance, D.A.B.2    Tovey, G.3    McCrossan, M.V.4    Drasar, B.S.5
  • 18
    • 0025373627 scopus 로고
    • Substrate specificities of the peptidyl prolyl cis-trans isomerase activities of cyclophilin and FK-506 binding-protein- evidence for the existence of a family of distinct enzymes
    • Harrison, R. K., and R. L. Stein. 1990. Substrate specificities of the peptidyl prolyl cis-trans isomerase activities of cyclophilin and FK-506 binding-protein- evidence for the existence of a family of distinct enzymes. Biochemistry 29:3813-3816.
    • (1990) Biochemistry , vol.29 , pp. 3813-3816
    • Harrison, R.K.1    Stein, R.L.2
  • 19
    • 0037229012 scopus 로고    scopus 로고
    • The PPIase active site of Legionella pneumophila Mip protein is involved in the infection of eukaryotic host cells
    • Helbig, J. H., et al. 2003. The PPIase active site of Legionella pneumophila Mip protein is involved in the infection of eukaryotic host cells. Biol. Chem. 384:125-137.
    • (2003) Biol. Chem. , vol.384 , pp. 125-137
    • Helbig, J.H.1
  • 20
    • 0031024992 scopus 로고    scopus 로고
    • Decreased intracellular survival of an fkpA mutant of Salmonella typhimurium Copenhagen
    • Horne, 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
    • Horne, S.M.1    Kottom, T.J.2    Nolan, L.K.3    Young, K.D.4
  • 21
    • 36448957938 scopus 로고    scopus 로고
    • Requirements for peptidyl-prolyl isomerization activity: a comprehensive mutational analysis of the substrate-binding cavity of FK506-binding protein 12
    • Ikura, T., and N. Ito. 2007. Requirements for peptidyl-prolyl isomerization activity: a comprehensive mutational analysis of the substrate-binding cavity of FK506-binding protein 12. Protein Sci. 16:2618-2625.
    • (2007) Protein Sci. , vol.16 , pp. 2618-2625
    • Ikura, T.1    Ito, N.2
  • 22
    • 0344837299 scopus 로고    scopus 로고
    • Flagellum-mediated adhesion by Burkholderia pseudomallei precedes invasion of Acanthamoeba astronyxis
    • Inglis, T. J. J., T. Robertson, D. E. Woods, N. Dutton, and B. J. Chang. 2003. Flagellum-mediated adhesion by Burkholderia pseudomallei precedes invasion of Acanthamoeba astronyxis. Infect. Immun. 71:2280-2282.
    • (2003) Infect. Immun. , vol.71 , pp. 2280-2282
    • Inglis, T.J.J.1    Robertson, T.2    Woods, D.E.3    Dutton, N.4    Chang, B.J.5
  • 23
    • 0030023035 scopus 로고    scopus 로고
    • Intracellular survival of Burkholderia pseudomallei
    • Jones, A. L., T. J. Beveridge, and D. E. Woods. 1996. Intracellular survival of Burkholderia pseudomallei. Infect. Immun. 64:782-790.
    • (1996) Infect. Immun. , vol.64 , pp. 782-790
    • Jones, A.L.1    Beveridge, T.J.2    Woods, D.E.3
  • 24
    • 0033857225 scopus 로고    scopus 로고
    • Burkholderia pseudomallei induces cell fusion and actin-associated membrane protrusion: a possible mechanism for cell-to-cell spreading
    • Kespichayawattana, W., S. Rattanachetkul, T. Wanun, P. Utaisincharoen, and S. Sirisinha. 2000. Burkholderia pseudomallei induces cell fusion and actin-associated membrane protrusion: a possible mechanism for cell-to-cell spreading. Infect. Immun. 68:5377-5384.
    • (2000) Infect. Immun. , vol.68 , pp. 5377-5384
    • Kespichayawattana, W.1    Rattanachetkul, S.2    Wanun, T.3    Utaisincharoen, P.4    Sirisinha, S.5
  • 25
    • 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., et al. 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
  • 26
    • 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., et al. 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
  • 27
    • 59849109196 scopus 로고    scopus 로고
    • Facile construction of unmarked deletion mutants in Burkholderia pseudomallei using sacB counter-selection in sucrose-resistant and sucrose-sensitive isolates
    • Logue, C. A., I. R. A. Peak, and I. R. Beacham. 2009. Facile construction of unmarked deletion mutants in Burkholderia pseudomallei using sacB counter-selection in sucrose-resistant and sucrose-sensitive isolates. J. Microbiol. Methods 76:320-323.
    • (2009) J. Microbiol. Methods , vol.76 , pp. 320-323
    • Logue, C.A.1    Peak, I.R.A.2    Beacham, I.R.3
  • 28
    • 0037441653 scopus 로고    scopus 로고
    • Structure validation by C alpha geometry: phi, psi and C beta deviation
    • Lovell, S. C., et al. 2003. Structure validation by C alpha geometry: phi, psi and C beta deviation. Proteins 50:437-450.
    • (2003) Proteins , vol.50 , pp. 437-450
    • Lovell, S.C.1
  • 29
    • 77951631052 scopus 로고    scopus 로고
    • Crystal structure determination and functional characterization of the metallochaperone SlyD from Thermus thermophilus
    • Löw, C., et al. 2010. Crystal structure determination and functional characterization of the metallochaperone SlyD from Thermus thermophilus. J. Mol. Biol. 398:375-390.
    • (2010) J. Mol. Biol. , vol.398 , pp. 375-390
    • Löw, C.1
  • 30
    • 0027483193 scopus 로고
    • Chlamydia trachomatis Mip-like protein has peptidyl-prolyl cis-trans isomerase activity that is inhibited by FK506 and rapamycin and is implicated in initiation of chlamydial infection
    • Lundemose, A. G., J. E. Kay, and J. H. Pearce. 1993. Chlamydia trachomatis Mip-like protein has peptidyl-prolyl cis-trans isomerase activity that is inhibited by FK506 and rapamycin and is implicated in initiation of chlamydial infection. Mol. Microbiol. 7:777-783.
    • (1993) Mol. Microbiol. , vol.7 , pp. 777-783
    • Lundemose, A.G.1    Kay, J.E.2    Pearce, J.H.3
  • 31
    • 25144458667 scopus 로고    scopus 로고
    • A new progressiveiterative algorithm for multiple structure alignment
    • Lupyan, D., A. Leo-Macias, and A. R. Ortiz. 2005. A new progressiveiterative algorithm for multiple structure alignment. Bioinformatics 21:3255-3263.
    • (2005) Bioinformatics , vol.21 , pp. 3255-3263
    • Lupyan, D.1    Leo-Macias, A.2    Ortiz, A.R.3
  • 33
    • 0028999723 scopus 로고
    • Secretion by Trypanosoma cruzi of a peptidyl-prolyl cis-trans isomerase involved in cell infection
    • Moro, A., F. Ruizcabello, A. Fernandezcano, R. P. Stock, and A. Gonzalez. 1995. Secretion by Trypanosoma cruzi of a peptidyl-prolyl cis-trans isomerase involved in cell infection. EMBO J. 14:2483-2490.
    • (1995) EMBO J , vol.14 , pp. 2483-2490
    • Moro, A.1    Ruizcabello, F.2    Fernandezcano, A.3    Stock, R.P.4    Gonzalez, A.5
  • 34
    • 1942441548 scopus 로고    scopus 로고
    • Bacteraemic melioidosis pneumonia: impact on outcome, clinical and radiological features
    • Mukhopadhyay, A., K. H. Lee, and P. A. Tambyah. 2004. Bacteraemic melioidosis pneumonia: impact on outcome, clinical and radiological features. J. Infect. 48:334-338.
    • (2004) J. Infect. , vol.48 , pp. 334-338
    • Mukhopadhyay, A.1    Lee, K.H.2    Tambyah, P.A.3
  • 35
    • 79960254326 scopus 로고    scopus 로고
    • The structure of a Burkholderia pseudomallei immunophilin-inhibitor complex reveals new approaches to antimicrobial development
    • Norville, I. H., et al. 2011. The structure of a Burkholderia pseudomallei immunophilin-inhibitor complex reveals new approaches to antimicrobial development. Biochem. J. 437:413-422.
    • (2011) Biochem. J. , vol.437 , pp. 413-422
    • Norville, I.H.1
  • 36
    • 0026662710 scopus 로고
    • An improved suicide vector for construction of chromosomal insertion mutations in bacteria
    • Penfold, R. J., and J. M. Pemberton. 1992. An improved suicide vector for construction of chromosomal insertion mutations in bacteria. Gene 118:145-146.
    • (1992) Gene , vol.118 , pp. 145-146
    • Penfold, R.J.1    Pemberton, J.M.2
  • 37
    • 0034862888 scopus 로고    scopus 로고
    • Crystal structure of Mip, a prolylisomerase from Legionella pneumophila
    • Riboldi-Tunnicliffe, A., et al. 2001. Crystal structure of Mip, a prolylisomerase from Legionella pneumophila. Nat. Struct. Biol. 8:779-783.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 779-783
    • Riboldi-Tunnicliffe, A.1
  • 39
    • 0026030568 scopus 로고
    • Chemistry and biology of the immunophilins and their immunosuppressive ligands
    • Schreiber, S. L. 1991. Chemistry and biology of the immunophilins and their immunosuppressive ligands. Science 251:283-287.
    • (1991) Science , vol.251 , pp. 283-287
    • Schreiber, S.L.1
  • 40
    • 0028028157 scopus 로고
    • Purification and characterization of a protease from Pseudomonas pseudomallei
    • Sexton, M. M., A. L. Jones, W. Chaowagul, and D. E. Woods. 1994. Purification and characterization of a protease from Pseudomonas pseudomallei. Can. J. Microbiol. 40:903-910.
    • (1994) Can. J. Microbiol. , vol.40 , pp. 903-910
    • Sexton, M.M.1    Jones, A.L.2    Chaowagul, W.3    Woods, D.E.4
  • 41
    • 0035967880 scopus 로고    scopus 로고
    • FUGUE: sequencestructure homology recognition using environment-specific substitution tables and structure-dependent gap penalties
    • Shi, J. Y., T. L. Blundell, and K. Mizuguchi. 2001. FUGUE: sequencestructure homology recognition using environment-specific substitution tables and structure-dependent gap penalties. J. Mol. Biol. 310:243-257.
    • (2001) J. Mol. Biol. , vol.310 , pp. 243-257
    • Shi, J.Y.1    Blundell, T.L.2    Mizuguchi, K.3
  • 42
    • 66249114348 scopus 로고    scopus 로고
    • Characterization of the role of the Escherichia coli periplasmic chaperone SurA using differential proteomics
    • Vertommen, D., N. Ruiz, P. Leverrier, T. J. Silhavy, and J. F. Collet. 2009. Characterization of the role of the Escherichia coli periplasmic chaperone SurA using differential proteomics. Proteomics 9:2432-2443.
    • (2009) Proteomics , vol.9 , pp. 2432-2443
    • Vertommen, D.1    Ruiz, N.2    Leverrier, P.3    Silhavy, T.J.4    Collet, J.F.5
  • 43
    • 33846230030 scopus 로고    scopus 로고
    • Collagen binding protein Mip enables Legionella pneumophila to transmigrate through a barrier of NCI-H292 lung epithelial cells and extracellular matrix
    • Wagner, C., et al. 2007. Collagen binding protein Mip enables Legionella pneumophila to transmigrate through a barrier of NCI-H292 lung epithelial cells and extracellular matrix. Cell. Microbiol. 9:450-462.
    • (2007) Cell. Microbiol. , vol.9 , pp. 450-462
    • Wagner, C.1
  • 44
    • 0018699952 scopus 로고
    • The kinetics of reversible tightbinding inhibition
    • Williams, J. W., and J. F. Morrison. 1979. The kinetics of reversible tightbinding inhibition. Methods Enzymol. 63:437-467.
    • (1979) Methods Enzymol. , vol.63 , pp. 437-467
    • Williams, J.W.1    Morrison, J.F.2
  • 45
    • 0028846924 scopus 로고
    • Influence of site-specifically altered Mip proteins on intracellular survival of Legionella pneumophila in eukaryotic cells
    • Wintermeyer, E., et al. 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


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