메뉴 건너뛰기




Volumn 12, Issue 8, 2013, Pages 2081-2095

Analysis of the secretome and identification of novel constituents from culture filtrate of bacillus calmette-guérin using high-resolution mass spectrometry

Author keywords

[No Author keywords available]

Indexed keywords

BCG VACCINE; PROTEOME; SECRETOME; UNCLASSIFIED DRUG; BACTERIAL PROTEIN;

EID: 84881106205     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M113.027318     Document Type: Article
Times cited : (29)

References (73)
  • 2
    • 33644991496 scopus 로고    scopus 로고
    • Global epidemiology of tuberculosis
    • Dye, C. (2006) Global epidemiology of tuberculosis. Lancet 367, 938-940
    • (2006) Lancet , vol.367 , pp. 938-940
    • Dye, C.1
  • 3
    • 0029920827 scopus 로고    scopus 로고
    • Molecular analysis of genetic differences between Mycobacterium bovis BCG and virulent M
    • Mahairas, G. G., Sabo, P. J., Hickey, M. J., Singh, D. C., and Stover, C. K. (1996) Molecular analysis of genetic differences between Mycobacterium bovis BCG and virulent M. bovis. J. Bacteriol. 178, 1274-1282
    • (1996) Bovis. J. Bacteriol. , vol.178 , pp. 1274-1282
    • Mahairas, G.G.1    Sabo, P.J.2    Hickey, M.J.3    Singh, D.C.4    Stover, C.K.5
  • 4
    • 27944472724 scopus 로고    scopus 로고
    • A review of vaccine research and development: Tuberculosis
    • Girard, M. P., Fruth, U., and Kieny, M. P. (2005) A review of vaccine research and development: tuberculosis. Vaccine 23, 5725-5731
    • (2005) Vaccine , vol.23 , pp. 5725-5731
    • Girard, M.P.1    Fruth, U.2    Kieny, M.P.3
  • 5
    • 22944433876 scopus 로고    scopus 로고
    • The success and failure of BCG- implications for a novel tuberculosis vaccine
    • Andersen, P., and Doherty, T. M. (2005) The success and failure of BCG- implications for a novel tuberculosis vaccine. Nat. Rev. Microbiol. 3, 656-662
    • (2005) Nat. Rev. Microbiol. , vol.3 , pp. 656-662
    • Andersen, P.1    Doherty, T.M.2
  • 6
    • 84867362036 scopus 로고    scopus 로고
    • Selective enrichment of newly synthesized proteins for quantitative secretome analysis
    • Eichelbaum, K., Winter, M., Diaz, M. B., Herzig, S., and Krijgsveld, J. (2012) Selective enrichment of newly synthesized proteins for quantitative secretome analysis. Nat. Biotechnol. 30, 984-990
    • (2012) Nat. Biotechnol. , vol.30 , pp. 984-990
    • Eichelbaum, K.1    Winter, M.2    Diaz, M.B.3    Herzig, S.4    Krijgsveld, J.5
  • 7
    • 77957352841 scopus 로고    scopus 로고
    • Comprehensive appraisal of the extracellular proteins from a monoderm bacterium: Theoretical and empirical exoproteomes of Listeria monocytogenes EGD-e by secretomics
    • Desvaux, M., Dumas, E., Chafsey, I., Chambon, C., and Hebraud, M. (2010) Comprehensive appraisal of the extracellular proteins from a monoderm bacterium: theoretical and empirical exoproteomes of Listeria monocytogenes EGD-e by secretomics. J. Proteome Res. 9, 5076-5092
    • (2010) J. Proteome Res. , vol.9 , pp. 5076-5092
    • Desvaux, M.1    Dumas, E.2    Chafsey, I.3    Chambon, C.4    Hebraud, M.5
  • 9
    • 77957755656 scopus 로고    scopus 로고
    • Secretome proteomics for discovery of cancer biomarkers
    • Makridakis, M., and Vlahou, A. (2010) Secretome proteomics for discovery of cancer biomarkers. J. Proteomics 73, 2291-2305
    • (2010) J. Proteomics , vol.73 , pp. 2291-2305
    • Makridakis, M.1    Vlahou, A.2
  • 10
    • 5644237689 scopus 로고    scopus 로고
    • CFP10 discriminates between nonacetylated and acetylated ESAT-6 of Mycobacterium tuberculosis by differential interaction
    • Okkels, L. M., Muller, E. C., Schmid, M., Rosenkrands, I., Kaufmann, S. H., Andersen, P., and Jungblut, P. R. (2004) CFP10 discriminates between nonacetylated and acetylated ESAT-6 of Mycobacterium tuberculosis by differential interaction. Proteomics 4, 2954-2960
    • (2004) Proteomics , vol.4 , pp. 2954-2960
    • Okkels, L.M.1    Muller, E.C.2    Schmid, M.3    Rosenkrands, I.4    Kaufmann, S.H.5    Andersen, P.6    Jungblut, P.R.7
  • 11
    • 34249701192 scopus 로고    scopus 로고
    • Comprehensive analysis of exported proteins from Mycobacterium tuberculosis H37Rv
    • Malen, H., Berven, F. S., Fladmark, K. E., and Wiker, H. G. (2007) Comprehensive analysis of exported proteins from Mycobacterium tuberculosis H37Rv. Proteomics 7, 1702-1718
    • (2007) Proteomics , vol.7 , pp. 1702-1718
    • Malen, H.1    Berven, F.S.2    Fladmark, K.E.3    Wiker, H.G.4
  • 12
    • 0037541109 scopus 로고    scopus 로고
    • Identification of novel proteins in culture filtrates of Mycobacterium bovis bacillus Calmette-Guerin in the isoelectric point range 6
    • Florio, W., Batoni, G., Esin, S., Bottai, D., Maisetta, G., Pardini, M., and Campa, M. (2003) Identification of novel proteins in culture filtrates of Mycobacterium bovis bacillus Calmette-Guerin in the isoelectric point range 6- Proteomics 3, 798-802
    • (2003) Proteomics , vol.3 , pp. 798-802
    • Florio, W.1    Batoni, G.2    Esin, S.3    Bottai, D.4    Maisetta, G.5    Pardini, M.6    Campa, M.7
  • 13
    • 77952534524 scopus 로고    scopus 로고
    • The secretome of a recombinant BCG substrain reveals differences in hypothetical proteins
    • Rodriguez-Alvarez, M., Palomec-Nava, I. D., Mendoza-Hernandez, G., and Lopez-Vidal, Y. (2010) The secretome of a recombinant BCG substrain reveals differences in hypothetical proteins. Vaccine 28, 3997-4001
    • (2010) Vaccine , vol.28 , pp. 3997-4001
    • Rodriguez-Alvarez, M.1    Palomec-Nava, I.D.2    Mendoza-Hernandez, G.3    Lopez-Vidal, Y.4
  • 15
    • 84355166446 scopus 로고    scopus 로고
    • Analytical constraints for the analysis of human cell line secretomes by shotgun proteomics
    • Malard, V., Chardan, L., Roussi, S., Darolles, C., Sage, N., Gaillard, J. C., and Armengaud, J. (2012) Analytical constraints for the analysis of human cell line secretomes by shotgun proteomics. J. Proteomics 75, 1043-1054
    • (2012) J. Proteomics , vol.75 , pp. 1043-1054
    • Malard, V.1    Chardan, L.2    Roussi, S.3    Darolles, C.4    Sage, N.5    Gaillard, J.C.6    Armengaud, J.7
  • 16
    • 78651431723 scopus 로고    scopus 로고
    • Combining blue native polyacrylamide gel electrophoresis with liquid chromatography tandem mass spectrometry as an effective strategy for analyzing potential membrane protein complexes of Mycobacterium bovis bacillus Calmette-Guerin
    • Zheng, J., Wei, C., Zhao, L., Liu, L., Leng, W., Li, W., and Jin, Q. (2011) Combining blue native polyacrylamide gel electrophoresis with liquid chromatography tandem mass spectrometry as an effective strategy for analyzing potential membrane protein complexes of Mycobacterium bovis bacillus Calmette-Guerin. BMC Genomics 12, 40
    • (2011) BMC Genomics , vol.12 , pp. 40
    • Zheng, J.1    Wei, C.2    Zhao, L.3    Liu, L.4    Leng, W.5    Li, W.6    Jin, Q.7
  • 17
    • 67650750887 scopus 로고    scopus 로고
    • Validating divergent ORF annotation of the Mycobacterium leprae genome through a full translation data set and peptide identification by tandem mass spectrometry
    • de Souza, G. A., Softeland, T., Koehler, C. J., Thiede, B., and Wiker, H. G. (2009) Validating divergent ORF annotation of the Mycobacterium leprae genome through a full translation data set and peptide identification by tandem mass spectrometry. Proteomics 9, 3233-3243
    • (2009) Proteomics , vol.9 , pp. 3233-3243
    • De Souza, G.A.1    Softeland, T.2    Koehler, C.J.3    Thiede, B.4    Wiker, H.G.5
  • 18
    • 84870393056 scopus 로고    scopus 로고
    • A comprehensive proteomic analysis of Mycobacterium bovis bacillus Calmette-Guerin using high resolution Fourier transform mass spectrometry
    • Zheng, J., Liu, L., Wei, C., Leng, W., Yang, J., Li, W., Wang, J., and Jin, Q. (2012) A comprehensive proteomic analysis of Mycobacterium bovis bacillus Calmette-Guerin using high resolution Fourier transform mass spectrometry. J. Proteomics 77, 357-371
    • (2012) J. Proteomics , vol.77 , pp. 357-371
    • Zheng, J.1    Liu, L.2    Wei, C.3    Leng, W.4    Yang, J.5    Li, W.6    Wang, J.7    Jin, Q.8
  • 19
    • 33947413501 scopus 로고    scopus 로고
    • Lipoprotein synthesis in mycobacteria
    • Rezwan, M., Grau, T., Tschumi, A., and Sander, P. (2007) Lipoprotein synthesis in mycobacteria. Microbiology 153, 652-658
    • (2007) Microbiology , vol.153 , pp. 652-658
    • Rezwan, M.1    Grau, T.2    Tschumi, A.3    Sander, P.4
  • 20
    • 7944226058 scopus 로고    scopus 로고
    • Lipoproteins of Mycobacterium tuberculosis: An abundant and functionally diverse class of cell envelope components
    • Sutcliffe, I. C., and Harrington, D. J. (2004) Lipoproteins of Mycobacterium tuberculosis: an abundant and functionally diverse class of cell envelope components. FEMS Microbiol. Rev. 28, 645-659
    • (2004) FEMS Microbiol. Rev. , vol.28 , pp. 645-659
    • Sutcliffe, I.C.1    Harrington, D.J.2
  • 21
    • 61549096272 scopus 로고    scopus 로고
    • Prediction of lipoprotein signal peptides in Gram-positive bacteria with a Hidden Markov Model
    • Bagos, P. G., Tsirigos, K. D., Liakopoulos, T. D., and Hamodrakas, S. J. (2008) Prediction of lipoprotein signal peptides in Gram-positive bacteria with a Hidden Markov Model. J. Proteome Res. 7, 5082-5093
    • (2008) J. Proteome Res. , vol.7 , pp. 5082-5093
    • Bagos, P.G.1    Tsirigos, K.D.2    Liakopoulos, T.D.3    Hamodrakas, S.J.4
  • 25
    • 0030862226 scopus 로고    scopus 로고
    • Definition of Mycobacterium tuberculosis culture filtrate proteins by two-dimensional polyacrylamide gel electrophoresis, N-terminal amino acid sequencing, and electrospray mass spectrometry
    • Sonnenberg, M. G., and Belisle, J. T. (1997) Definition of Mycobacterium tuberculosis culture filtrate proteins by two-dimensional polyacrylamide gel electrophoresis, N-terminal amino acid sequencing, and electrospray mass spectrometry. Infect. Immun. 65, 4515-4524
    • (1997) Infect. Immun. , vol.65 , pp. 4515-4524
    • Sonnenberg, M.G.1    Belisle, J.T.2
  • 28
    • 0034031272 scopus 로고    scopus 로고
    • Mapping and identification of Mycobacterium tuberculosis proteins by two-dimensional gel electrophoresis, microsequencing and immunodetection
    • Rosenkrands, I., Weldingh, K., Jacobsen, S., Hansen, C. V., Florio, W., Gianetri, I., and Andersen, P. (2000) Mapping and identification of Mycobacterium tuberculosis proteins by two-dimensional gel electrophoresis, microsequencing and immunodetection. Electrophoresis 21, 935-948
    • (2000) Electrophoresis , vol.21 , pp. 935-948
    • Rosenkrands, I.1    Weldingh, K.2    Jacobsen, S.3    Hansen, C.V.4    Florio, W.5    Gianetri, I.6    Andersen, P.7
  • 29
    • 0035319968 scopus 로고    scopus 로고
    • The application of proteomics in defining the T cell antigens of Mycobacterium tuberculosis
    • Covert, B. A., Spencer, J. S., Orme, I. M., and Belisle, J. T. (2001) The application of proteomics in defining the T cell antigens of Mycobacterium tuberculosis. Proteomics 1, 574-586
    • (2001) Proteomics , vol.1 , pp. 574-586
    • Covert, B.A.1    Spencer, J.S.2    Orme, I.M.3    Belisle, J.T.4
  • 30
    • 0036285253 scopus 로고    scopus 로고
    • Hypoxic response of Mycobacterium tuberculosis studied by metabolic labeling and proteome analysis of cellular and extracellular proteins
    • Rosenkrands, I., Slayden, R. A., Crawford, J., Aagaard, C., Barry, C. E., 3rd, and Andersen, P. (2002) Hypoxic response of Mycobacterium tuberculosis studied by metabolic labeling and proteome analysis of cellular and extracellular proteins. J. Bacteriol. 184, 3485-3491
    • (2002) J. Bacteriol. , vol.184 , pp. 3485-3491
    • Rosenkrands, I.1    Slayden, R.A.2    Crawford, J.3    Aagaard, C.4    Barry III, C.E.5    Andersen, P.6
  • 31
    • 0042564532 scopus 로고    scopus 로고
    • Comparative proteome analysis of culture supernatant proteins of Mycobacterium tuberculosis H37Rv and H37Ra
    • He, X. Y., Zhuang, Y. H., Zhang, X. G., and Li, G. L. (2003) Comparative proteome analysis of culture supernatant proteins of Mycobacterium tuberculosis H37Rv and H37Ra. Microbes Infect. 5, 851-856
    • (2003) Microbes Infect. , vol.5 , pp. 851-856
    • He, X.Y.1    Zhuang, Y.H.2    Zhang, X.G.3    Li, G.L.4
  • 33
    • 66749167039 scopus 로고    scopus 로고
    • Immunoproteomic identification of secretory and subcellular protein antigens and functional evaluation of the secretome fraction of Mycobacterium immunogenum, a newly recognized species of the Mycobacterium chelonae-Mycobacterium abscessus group
    • Gupta, M. K., Subramanian, V., and Yadav, J. S. (2009) Immunoproteomic identification of secretory and subcellular protein antigens and functional evaluation of the secretome fraction of Mycobacterium immunogenum, a newly recognized species of the Mycobacterium chelonae-Mycobacterium abscessus group. J. Proteome Res. 8, 2319-2330
    • (2009) J. Proteome Res. , vol.8 , pp. 2319-2330
    • Gupta, M.K.1    Subramanian, V.2    Yadav, J.S.3
  • 34
    • 77952344404 scopus 로고    scopus 로고
    • Descriptive proteomic analysis shows protein variability between closely related clinical isolates of Mycobacterium tuberculosis
    • Mehaffy, C., Hess, A., Prenni, J. E., Mathema, B., Kreiswirth, B., and Dobos, a. K. M. (2010) Descriptive proteomic analysis shows protein variability between closely related clinical isolates of Mycobacterium tuberculosis. Proteomics 10, 1966-1984
    • (2010) Proteomics , vol.10 , pp. 1966-1984
    • Mehaffy, C.1    Hess, A.2    Prenni, J.E.3    Mathema, B.4    Kreiswirth, B.5    Dobos, A.K.M.6
  • 35
    • 33847208190 scopus 로고    scopus 로고
    • Experimental determination of translational starts using peptide mass mapping and tandem mass spectrometry within the proteome of Mycobacterium tuberculosis
    • Rison, S. C., Mattow, J., Jungblut, P. R., and Stoker, N. G. (2007) Experimental determination of translational starts using peptide mass mapping and tandem mass spectrometry within the proteome of Mycobacterium tuberculosis. Microbiology 153, 521-528
    • (2007) Microbiology , vol.153 , pp. 521-528
    • Rison, S.C.1    Mattow, J.2    Jungblut, P.R.3    Stoker, N.G.4
  • 36
    • 12344296536 scopus 로고    scopus 로고
    • Accuracy improvement for identifying translation initiation sites in microbial genomes
    • Zhu, H. Q., Hu, G. Q., Ouyang, Z. Q., Wang, J., and She, Z. S. (2004) Accuracy improvement for identifying translation initiation sites in microbial genomes. Bioinformatics 20, 3308-3317
    • (2004) Bioinformatics , vol.20 , pp. 3308-3317
    • Zhu, H.Q.1    Hu, G.Q.2    Ouyang, Z.Q.3    Wang, J.4    She, Z.S.5
  • 37
    • 48249147316 scopus 로고    scopus 로고
    • High accuracy mass spectrometry analysis as a tool to verify and improve gene annotation using Mycobacterium tuberculosis as an example
    • de Souza, G. A., Malen, H., Softeland, T., Saelensminde, G., Prasad, S., Jonassen, I., and Wiker, H. G. (2008) High accuracy mass spectrometry analysis as a tool to verify and improve gene annotation using Mycobacterium tuberculosis as an example. BMC Genomics 9, 316
    • (2008) BMC Genomics , vol.9 , pp. 316
    • De Souza, G.A.1    Malen, H.2    Softeland, T.3    Saelensminde, G.4    Prasad, S.5    Jonassen, I.6    Wiker, H.G.7
  • 38
    • 0030805979 scopus 로고    scopus 로고
    • Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K
    • Link, A. J., Robison, K., and Church, G. M. (1997) Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K. Electrophoresis 18, 1259-1313
    • (1997) Electrophoresis , vol.18 , pp. 1259-1313
    • Link, A.J.1    Robison, K.2    Church, G.M.3
  • 40
    • 0034868629 scopus 로고    scopus 로고
    • Proteomics reveals open reading frames in Mycobacterium tuberculosis H37Rv not predicted by genomics
    • Jungblut, P. R., Muller, E. C., Mattow, J., and Kaufmann, S. H. (2001) Proteomics reveals open reading frames in Mycobacterium tuberculosis H37Rv not predicted by genomics. Infect. Immun. 69, 5905-5907
    • (2001) Infect. Immun. , vol.69 , pp. 5905-5907
    • Jungblut, P.R.1    Muller, E.C.2    Mattow, J.3    Kaufmann, S.H.4
  • 44
    • 0031825604 scopus 로고    scopus 로고
    • Two-dimensional electrophoresis for analysis of Mycobacterium tuberculosis culture filtrate and purification and characterization of six novel proteins
    • Weldingh, K., Rosenkrands, I., Jacobsen, S., Rasmussen, P. B., Elhay, M. J., and Andersen, P. (1998) Two-dimensional electrophoresis for analysis of Mycobacterium tuberculosis culture filtrate and purification and characterization of six novel proteins. Infect. Immun. 66, 3492-3500
    • (1998) Infect. Immun. , vol.66 , pp. 3492-3500
    • Weldingh, K.1    Rosenkrands, I.2    Jacobsen, S.3    Rasmussen, P.B.4    Elhay, M.J.5    Andersen, P.6
  • 45
    • 0031688910 scopus 로고    scopus 로고
    • Molecular cloning, expression, and immunogenicity of MTB12, a novel low-molecular-weight antigen secreted by Mycobacterium tuberculosis
    • Webb, J. R., Vedvick, T. S., Alderson, M. R., Guderian, J. A., Jen, S. S., Ovendale, P. J., Johnson, S. M., Reed, S. G., and Skeiky, Y. A. (1998) Molecular cloning, expression, and immunogenicity of MTB12, a novel low-molecular-weight antigen secreted by Mycobacterium tuberculosis. Infect. Immun. 66, 4208-4214
    • (1998) Infect. Immun. , vol.66 , pp. 4208-4214
    • Webb, J.R.1    Vedvick, T.S.2    Alderson, M.R.3    Guderian, J.A.4    Jen, S.S.5    Ovendale, P.J.6    Johnson, S.M.7    Reed, S.G.8    Skeiky, Y.A.9
  • 46
    • 0034659980 scopus 로고    scopus 로고
    • Isolation, purification and immunological characterization of novel low molecular weight protein antigen CFP 6 from culture filtrate of M
    • Bhaskar, S., Khanna, S. P., and Mukherjee, R. (2000) Isolation, purification and immunological characterization of novel low molecular weight protein antigen CFP 6 from culture filtrate of M. tuberculosis. Vaccine 18, 2856-2866
    • (2000) Tuberculosis. Vaccine , vol.18 , pp. 2856-2866
    • Bhaskar, S.1    Khanna, S.P.2    Mukherjee, R.3
  • 49
    • 50849085761 scopus 로고    scopus 로고
    • Intratracheal administration of third-generation lentivirus vector encoding MPT51 from Mycobacterium tuberculosis induces specific CD8+ T-cell responses in the lung
    • Hashimoto, D., Nagata, T., Uchijima, M., Seto, S., Suda, T., Chida, K., Miyoshi, H., Nakamura, H., and Koide, Y. (2008) Intratracheal administration of third-generation lentivirus vector encoding MPT51 from Mycobacterium tuberculosis induces specific CD8+ T-cell responses in the lung. Vaccine 26, 5095-5100
    • (2008) Vaccine , vol.26 , pp. 5095-5100
    • Hashimoto, D.1    Nagata, T.2    Uchijima, M.3    Seto, S.4    Suda, T.5    Chida, K.6    Miyoshi, H.7    Nakamura, H.8    Koide, Y.9
  • 51
    • 0033118862 scopus 로고    scopus 로고
    • Cloning, expression and significance of MPT53 for identification of secreted proteins of Mycobacterium tuberculosis
    • Wiker, H. G., Michell, S. L., Hewinson, R. G., Spierings, E., Nagai, S., and Harboe, M. (1999) Cloning, expression and significance of MPT53 for identification of secreted proteins of Mycobacterium tuberculosis. Microb. Pathog. 26, 207-219
    • (1999) Microb. Pathog. , vol.26 , pp. 207-219
    • Wiker, H.G.1    Michell, S.L.2    Hewinson, R.G.3    Spierings, E.4    Nagai, S.5    Harboe, M.6
  • 52
    • 1842431883 scopus 로고    scopus 로고
    • Induction of protective cellular immunity against Mycobacterium tuberculosis by recombinant attenuated self-destructing Listeria monocytogenes strains harboring eukaryotic expression plasmids for antigen 85 complex and MPB/ MPT
    • Miki, K., Nagata, T., Tanaka, T., Kim, Y. H., Uchijima, M., Ohara, N., Nakamura, S., Okada, M., and Koide, Y. (2004) Induction of protective cellular immunity against Mycobacterium tuberculosis by recombinant attenuated self-destructing Listeria monocytogenes strains harboring eukaryotic expression plasmids for antigen 85 complex and MPB/ MPT. Infect. Immun. 72, 2014-2021
    • (2004) Infect. Immun. , vol.72 , pp. 2014-2021
    • Miki, K.1    Nagata, T.2    Tanaka, T.3    Kim, Y.H.4    Uchijima, M.5    Ohara, N.6    Nakamura, S.7    Okada, M.8    Koide, Y.9
  • 53
    • 65349118783 scopus 로고    scopus 로고
    • MPB70 and MPB83-major antigens of Mycobacterium bovis
    • Wiker, H. G. (2009) MPB70 and MPB83-major antigens of Mycobacterium bovis. Scand. J. Immunol. 69, 492-499
    • (2009) Scand. J. Immunol. , vol.69 , pp. 492-499
    • Wiker, H.G.1
  • 54
    • 0031024720 scopus 로고    scopus 로고
    • Molecular cloning, purification, and serological characterization of MPT63, a novel antigen secreted by Mycobacterium tuberculosis
    • Manca, C., Lyashchenko, K., Wiker, H. G., Usai, D., Colangeli, R., and Gennaro, M. L. (1997) Molecular cloning, purification, and serological characterization of MPT63, a novel antigen secreted by Mycobacterium tuberculosis. Infect. Immun. 65, 16-23
    • (1997) Infect. Immun. , vol.65 , pp. 16-23
    • Manca, C.1    Lyashchenko, K.2    Wiker, H.G.3    Usai, D.4    Colangeli, R.5    Gennaro, M.L.6
  • 55
    • 77953122218 scopus 로고    scopus 로고
    • Identification of murine T-cell epitopes on low-molecular-mass secretory proteins (CFP11, CFP17, and TB5) of Mycobacterium tuberculosis
    • Eweda, G., Suzuki, D., Nagata, T., Tsujimura, K., and Koide, Y. (2010) Identification of murine T-cell epitopes on low-molecular-mass secretory proteins (CFP11, CFP17, and TB5) of Mycobacterium tuberculosis. Vaccine 28, 4616-4625
    • (2010) Vaccine , vol.28 , pp. 4616-4625
    • Eweda, G.1    Suzuki, D.2    Nagata, T.3    Tsujimura, K.4    Koide, Y.5
  • 56
    • 67349217383 scopus 로고    scopus 로고
    • TLR2 and its co-receptors determine responses of macrophages and dendritic cells to lipoproteins of Mycobacterium tuberculosis
    • Drage, M. G., Pecora, N. D., Hise, A. G., Febbraio, M., Silverstein, R. L., Golenbock, D. T., Boom, W. H., and Harding, C. V. (2009) TLR2 and its co-receptors determine responses of macrophages and dendritic cells to lipoproteins of Mycobacterium tuberculosis. Cell. Immunol. 258, 29-37
    • (2009) Cell. Immunol. , vol.258 , pp. 29-37
    • Drage, M.G.1    Pecora, N.D.2    Hise, A.G.3    Febbraio, M.4    Silverstein, R.L.5    Golenbock, D.T.6    Boom, W.H.7    Harding, C.V.8
  • 58
    • 33745298718 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis LprA is a lipoprotein agonist of TLR2 that regulates innate immunity and APC function
    • Pecora, N. D., Gehring, A. J., Canaday, D. H., Boom, W. H., and Harding, C. V. (2006) Mycobacterium tuberculosis LprA is a lipoprotein agonist of TLR2 that regulates innate immunity and APC function. J. Immunol. 177, 422-429
    • (2006) J. Immunol. , vol.177 , pp. 422-429
    • Pecora, N.D.1    Gehring, A.J.2    Canaday, D.H.3    Boom, W.H.4    Harding, C.V.5
  • 59
    • 8244238391 scopus 로고    scopus 로고
    • Three different putative phosphate transport receptors are encoded by the Mycobacterium tuberculosis genome and are present at the surface of Mycobacterium bovis BCG
    • Lefevre, P., Braibant, M., de Wit, L., Kalai, M., Roeper, D., Grotzinger, J., Delville, J. P., Peirs, P., Ooms, J., Huygen, K., and Content, J. (1997) Three different putative phosphate transport receptors are encoded by the Mycobacterium tuberculosis genome and are present at the surface of Mycobacterium bovis BCG. J. Bacteriol. 179, 2900-2906
    • (1997) J. Bacteriol. , vol.179 , pp. 2900-2906
    • Lefevre, P.1    Braibant, M.2    De Wit, L.3    Kalai, M.4    Roeper, D.5    Grotzinger, J.6    Delville, J.P.7    Peirs, P.8    Ooms, J.9    Huygen, K.10    Content, J.11
  • 61
    • 77649272164 scopus 로고    scopus 로고
    • An extracellular disulfide bond forming protein (DsbF) from Mycobacterium tuberculosis: Structural, biochemical, and gene expression analysis
    • Chim, N., Riley, R., The, J., Im, S., Segelke, B., Lekin, T., Yu, M., Hung, L. W., Terwilliger, T., Whitelegge, J. P., and Goulding, C. W. (2010) An extracellular disulfide bond forming protein (DsbF) from Mycobacterium tuberculosis: structural, biochemical, and gene expression analysis. J. Mol. Biol. 396, 1211-1226
    • (2010) J. Mol. Biol. , vol.396 , pp. 1211-1226
    • Chim, N.1    Riley, R.2    The, J.3    Im, S.4    Segelke, B.5    Lekin, T.6    Yu, M.7    Hung, L.W.8    Terwilliger, T.9    Whitelegge, J.P.10    Goulding, C.W.11
  • 62
    • 1242339645 scopus 로고    scopus 로고
    • Cation-pi interactions as determinants for binding of the compatible solutes glycine betaine and proline betaine by the periplasmic ligand-binding protein ProX from Escherichia coli
    • Schiefner, A., Breed, J., Bosser, L., Kneip, S., Gade, J., Holtmann, G., Diederichs, K., Welte, W., and Bremer, E. (2004) Cation-pi interactions as determinants for binding of the compatible solutes glycine betaine and proline betaine by the periplasmic ligand-binding protein ProX from Escherichia coli. J. Biol. Chem. 279, 5588-5596
    • (2004) J. Biol. Chem. , vol.279 , pp. 5588-5596
    • Schiefner, A.1    Breed, J.2    Bosser, L.3    Kneip, S.4    Gade, J.5    Holtmann, G.6    Diederichs, K.7    Welte, W.8    Bremer, E.9
  • 63
    • 0036271841 scopus 로고    scopus 로고
    • Functional genomics reveals the sole sulphate transporter of the Mycobacterium tuberculosis complex and its relevance to the acquisition of sulphur in vivo
    • Wooff, E., Michell, S. L., Gordon, S. V., Chambers, M. A., Bardarov, S., Jacobs, W. R., Jr., Hewinson, R. G., and Wheeler, P. R. (2002) Functional genomics reveals the sole sulphate transporter of the Mycobacterium tuberculosis complex and its relevance to the acquisition of sulphur in vivo. Mol. Microbiol. 43, 653-663
    • (2002) Mol. Microbiol. , vol.43 , pp. 653-663
    • Wooff, E.1    Michell, S.L.2    Gordon, S.V.3    Chambers, M.A.4    Bardarov, S.5    Jacobs Jr., W.R.6    Hewinson, R.G.7    Wheeler, P.R.8
  • 64
    • 80052740653 scopus 로고    scopus 로고
    • The PE and PPE proteins of Mycobacterium tuberculosis
    • Mukhopadhyay, S., and Balaji, K. N. (2011) The PE and PPE proteins of Mycobacterium tuberculosis. Tuberculosis (Edinb.) 91, 441-447
    • (2011) Tuberculosis (Edinb.) , vol.91 , pp. 441-447
    • Mukhopadhyay, S.1    Balaji, K.N.2
  • 65
    • 84866951194 scopus 로고    scopus 로고
    • Tubercle bacilli rely on a type VIII army for pathogenicity
    • Stoop, E. J., Bitter, W., and van der Sar, A. M. (2012) Tubercle bacilli rely on a type VIII army for pathogenicity. Trends Microbiol. 20, 477-484
    • (2012) Trends Microbiol. , vol.20 , pp. 477-484
    • Stoop, E.J.1    Bitter, W.2    Van Der Sar, A.M.3
  • 67
    • 79953270009 scopus 로고    scopus 로고
    • Mycobacterial PE/PPE proteins at the host-pathogen interface
    • Sampson, S. L. (2011) Mycobacterial PE/PPE proteins at the host-pathogen interface. Clin. Dev. Immunol. 2011, 497203
    • (2011) Clin. Dev. Immunol. , vol.2011 , pp. 497203
    • Sampson, S.L.1
  • 68
    • 78651578834 scopus 로고    scopus 로고
    • Mammalian cell entry gene family of Mycobacterium tuberculosis
    • Zhang, F., and Xie, J. P. (2011) Mammalian cell entry gene family of Mycobacterium tuberculosis. Mol. Cell. Biochem. 352, 1-10
    • (2011) Mol. Cell. Biochem. , vol.352 , pp. 1-10
    • Zhang, F.1    Xie, J.P.2
  • 69
    • 33746783675 scopus 로고    scopus 로고
    • Computational identification of beta-barrel outer-membrane proteins in Mycobacterium tuberculosis predicted proteomes as putative vaccine candidates
    • Pajon, R., Yero, D., Lage, A., Llanes, A., and Borroto, C. J. (2006) Computational identification of beta-barrel outer-membrane proteins in Mycobacterium tuberculosis predicted proteomes as putative vaccine candidates. Tuberculosis (Edinb.) 86, 290-302
    • (2006) Tuberculosis (Edinb.) , vol.86 , pp. 290-302
    • Pajon, R.1    Yero, D.2    Lage, A.3    Llanes, A.4    Borroto, C.J.5
  • 71
    • 84865627142 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis Mce1 protein complex initiates rapid induction of transcription of genes involved in substrate trafficking
    • Stavrum, R., Valvatne, H., Stavrum, A. K., Riley, L. W., Ulvestad, E., Jonassen, I., Doherty, T. M., and Grewal, H. M. (2012) Mycobacterium tuberculosis Mce1 protein complex initiates rapid induction of transcription of genes involved in substrate trafficking. Genes Immun. 13, 496-502
    • (2012) Genes Immun. , vol.13 , pp. 496-502
    • Stavrum, R.1    Valvatne, H.2    Stavrum, A.K.3    Riley, L.W.4    Ulvestad, E.5    Jonassen, I.6    Doherty, T.M.7    Grewal, H.M.8
  • 73
    • 36048982541 scopus 로고    scopus 로고
    • Membrane subproteomic analysis of Mycobacterium bovis bacillus Calmette-Guerin
    • Zheng, J., Wei, C., Leng, W., Dong, J., Li, R., Li, W., Wang, J., Zhang, Z., and Jin, Q. (2007) Membrane subproteomic analysis of Mycobacterium bovis bacillus Calmette-Guerin. Proteomics 7, 3919-3931
    • (2007) Proteomics , vol.7 , pp. 3919-3931
    • Zheng, J.1    Wei, C.2    Leng, W.3    Dong, J.4    Li, R.5    Li, W.6    Wang, J.7    Zhang, Z.8    Jin, Q.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.