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Volumn 28, Issue 5, 2004, Pages 645-659

Lipoproteins of Mycobacterium tuberculosis: An abundant and functionally diverse class of cell envelope components

Author keywords

Bioinformatics; Genome; Lipoprotein; Mycobacterium tuberculosis; Periplasm; Virulence factor

Indexed keywords

LIPID; LIPOPROTEIN; MEMBRANE PROTEIN; PEPTIDE DERIVATIVE;

EID: 7944226058     PISSN: 01686445     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.femsre.2004.06.002     Document Type: Review
Times cited : (157)

References (129)
  • 1
    • 0033581124 scopus 로고    scopus 로고
    • Global burden of tuberculosis. Estimated incidence, prevalence, and mortality by country
    • Dye, C., Scheele, S., Dolin, P., Pathania, V., Raviglione, M.C. for the WHO Global Surveillance and Monitoring Project. (1999) Global burden of tuberculosis. Estimated incidence, prevalence, and mortality by country. JAMA 282, 677-686
    • (1999) JAMA , vol.282 , pp. 677-686
    • Dye, C.1    Scheele, S.2    Dolin, P.3    Pathania, V.4    Raviglione, M.C.5
  • 4
    • 0002259015 scopus 로고
    • Lipids: Complex lipids, their chemistry, biosynthesis and roles
    • C. Ratledge J.L. Stanford Academic Press London
    • D.E. Minnikin Lipids: Complex lipids, their chemistry, biosynthesis and roles C. Ratledge J.L. Stanford The Biology of the Mycobacteria 1982 Academic Press London 95 184
    • (1982) The Biology of the Mycobacteria , pp. 95-184
    • Minnikin, D.E.1
  • 6
    • 0032452982 scopus 로고    scopus 로고
    • The envelope layers of mycobacteria with reference to their pathogenicity
    • M. Daffe, and P. Draper The envelope layers of mycobacteria with reference to their pathogenicity Adv. Microb. Physiol. 39 1998 131 203
    • (1998) Adv. Microb. Physiol. , vol.39 , pp. 131-203
    • Daffe, M.1    Draper, P.2
  • 7
    • 0033864778 scopus 로고    scopus 로고
    • Molecular mechanics of the mycobacterial cell wall: From horizontal layers to vertical scaffolds
    • B.A. Dmitriev, S. Ehlers, E.T. Rietschel, and P.J. Brennan Molecular mechanics of the mycobacterial cell wall: from horizontal layers to vertical scaffolds Int. J. Med. Microbiol. 290 2000 251 258
    • (2000) Int. J. Med. Microbiol. , vol.290 , pp. 251-258
    • Dmitriev, B.A.1    Ehlers, S.2    Rietschel, E.T.3    Brennan, P.J.4
  • 8
    • 77956860575 scopus 로고
    • Lipoproteins, structure, function, biosynthesis and model for protein export
    • V. Braun, and H.C. Wu Lipoproteins, structure, function, biosynthesis and model for protein export New Compr. Biochem. 27 1994 319 341
    • (1994) New Compr. Biochem. , vol.27 , pp. 319-341
    • Braun, V.1    Wu, H.C.2
  • 9
    • 0028987131 scopus 로고
    • Lipoproteins of Gram-positive bacteria
    • I.C. Sutcliffe, and R.R.B. Russell Lipoproteins of Gram-positive bacteria J. Bacteriol. 177 1995 1123 1128
    • (1995) J. Bacteriol. , vol.177 , pp. 1123-1128
    • Sutcliffe, I.C.1    Russell, R.R.B.2
  • 10
    • 0020353685 scopus 로고
    • Glyceride-cysteine lipoproteins and secretion by Gram-positive bacteria
    • J.B.K. Nielsen, and J.O. Lampen Glyceride-cysteine lipoproteins and secretion by Gram-positive bacteria J. Bacteriol. 152 1982 315 322
    • (1982) J. Bacteriol. , vol.152 , pp. 315-322
    • Nielsen, J.B.K.1    Lampen, J.O.2
  • 11
    • 0023996324 scopus 로고
    • Distinctive properties of signal sequences from bacterial lipoproteins
    • D. Klein, R.L. Somorja, and P.C.K. Lau Distinctive properties of signal sequences from bacterial lipoproteins Protein Eng. 2 1988 15 20
    • (1988) Protein Eng. , vol.2 , pp. 15-20
    • Klein, D.1    Somorja, R.L.2    Lau, P.C.K.3
  • 12
    • 0024393453 scopus 로고
    • The structure of signal peptides from bacterial lipoproteins
    • G. von Heijne The structure of signal peptides from bacterial lipoproteins Protein Eng. 2 1989 531 534
    • (1989) Protein Eng. , vol.2 , pp. 531-534
    • Von Heijne, G.1
  • 13
    • 0033818171 scopus 로고    scopus 로고
    • Signal peptide-dependent protein transport in Bacillus subtilis: A genome-based survey of the secretome
    • H. Tjalsma, A. Bolhuis, J.D.H. Jongbloed, S. Bron, and J.M. van Dijl Signal peptide-dependent protein transport in Bacillus subtilis: a genome-based survey of the secretome Microbiol. Mol. Biol. Rev. 64 2000 515 547
    • (2000) Microbiol. Mol. Biol. Rev. , vol.64 , pp. 515-547
    • Tjalsma, H.1    Bolhuis, A.2    Jongbloed, J.D.H.3    Bron, S.4    Van Dijl, J.M.5
  • 14
    • 0036066456 scopus 로고    scopus 로고
    • Pattern searches for the identification of putative lipoprotein genes in Gram-positive bacterial genomes
    • I.C. Sutcliffe, and D.J. Harrington Pattern searches for the identification of putative lipoprotein genes in Gram-positive bacterial genomes Microbiology 148 2002 2065 2077
    • (2002) Microbiology , vol.148 , pp. 2065-2077
    • Sutcliffe, I.C.1    Harrington, D.J.2
  • 15
    • 0033043496 scopus 로고    scopus 로고
    • Lipid modification of prelipoproteins is dispensable for growth but essential for efficient protein secretion in Bacillus subtilis: Characterization of the lgt gene
    • S. Leskelä, E. Wahlstrom, V.P. Kontinen, and M. Sarvas Lipid modification of prelipoproteins is dispensable for growth but essential for efficient protein secretion in Bacillus subtilis: characterization of the lgt gene Mol. Microbiol. 31 1999 1075 1085
    • (1999) Mol. Microbiol. , vol.31 , pp. 1075-1085
    • Leskelä, S.1    Wahlstrom, E.2    Kontinen, V.P.3    Sarvas, M.4
  • 16
    • 0035948224 scopus 로고    scopus 로고
    • Lipid modification of prelipoproteins is dispensable for growth in vitro but essential for virulence in Streptococcus pneumoniae
    • C.M. Petit, J.R. Brown, K. Ingraham, A.P. Bryant, and D.J. Holmes Lipid modification of prelipoproteins is dispensable for growth in vitro but essential for virulence in Streptococcus pneumoniae FEMS Microbiol. Lett. 200 2001 229 233
    • (2001) FEMS Microbiol. Lett. , vol.200 , pp. 229-233
    • Petit, C.M.1    Brown, J.R.2    Ingraham, K.3    Bryant, A.P.4    Holmes, D.J.5
  • 19
    • 1542782546 scopus 로고    scopus 로고
    • Maturation of lipoproteins by Type II signal peptidase is required for phagosomal escape of Listeria monocytogenes
    • H. Réglier-Poupet, C. Frehel, I. Dubail, J.-L. Beretti, P. Berch, A. Charbit, and C. Raynaud Maturation of lipoproteins by Type II signal peptidase is required for phagosomal escape of Listeria monocytogenes J. Biol. Chem. 278 2003 49469 49477
    • (2003) J. Biol. Chem. , vol.278 , pp. 49469-49477
    • Réglier-Poupet, H.1    Frehel, C.2    Dubail, I.3    Beretti, J.-L.4    Berch, P.5    Charbit, A.6    Raynaud, C.7
  • 21
    • 0030609131 scopus 로고    scopus 로고
    • Identification of Staphylococcus aureus virulence genes in a murine model of bacteraemia using signature-tagged mutagenesis
    • J.-M. Mei, F. Nourbakhsh, C.W. Ford, and D.W. Holden Identification of Staphylococcus aureus virulence genes in a murine model of bacteraemia using signature-tagged mutagenesis Mol. Microbiol. 26 1998 399 407
    • (1998) Mol. Microbiol. , vol.26 , pp. 399-407
    • Mei, J.-M.1    Nourbakhsh, F.2    Ford, C.W.3    Holden, D.W.4
  • 22
    • 0025823848 scopus 로고
    • Lipoprotein antigens of Mycobacterium tuberculosis
    • D.B. Young, and T.R. Garbe Lipoprotein antigens of Mycobacterium tuberculosis Res. Microbiol. 142 1991 55 65
    • (1991) Res. Microbiol. , vol.142 , pp. 55-65
    • Young, D.B.1    Garbe, T.R.2
  • 23
    • 0027185234 scopus 로고
    • Characterization of a temperature-sensitive mutant of salmonella-typhimurium defective in apolipoprotein n-acyltransferase
    • S.D. Gupta, K. Gan, M.B. Schmid, and H.C. Wu Characterization of a temperature-sensitive mutant of salmonella-typhimurium defective in apolipoprotein n-acyltransferase J. Biol. Chem. 268 1993 16551 16556
    • (1993) J. Biol. Chem. , vol.268 , pp. 16551-16556
    • Gupta, S.D.1    Gan, K.2    Schmid, M.B.3    Wu, H.C.4
  • 26
    • 0033385551 scopus 로고    scopus 로고
    • Interactions between mycoplasma lipoproteins and the host immune system
    • I. Chambaud, H. Wróblewski, and A. Blanchard Interactions between mycoplasma lipoproteins and the host immune system Trends Microbiol. 7 1999 493 499
    • (1999) Trends Microbiol. , vol.7 , pp. 493-499
    • Chambaud, I.1    Wróblewski, H.2    Blanchard, A.3
  • 27
    • 0036091972 scopus 로고    scopus 로고
    • DOLOP - Database of bacterial lipoproteins
    • M.M. Babu, and K. Sankaran DOLOP - database of bacterial lipoproteins Bioinformatics 8 2002 641 643
    • (2002) Bioinformatics , vol.8 , pp. 641-643
    • Babu, M.M.1    Sankaran, K.2
  • 28
    • 1842688875 scopus 로고    scopus 로고
    • Putative lipoproteins of Streptococcus agalactiae identified by bioinformatic genome analysis
    • I.C. Sutcliffe, and D.J. Harrington Putative lipoproteins of Streptococcus agalactiae identified by bioinformatic genome analysis Antonie Van Leeuwenhoek 85 2004 305 315
    • (2004) Antonie Van Leeuwenhoek , vol.85 , pp. 305-315
    • Sutcliffe, I.C.1    Harrington, D.J.2
  • 30
    • 0001244666 scopus 로고    scopus 로고
    • ScanProsite: A reference implementation of a PROSITE scanning tool
    • A. Gattiker, E. Gasteiger, and A. Bairoch ScanProsite: a reference implementation of a PROSITE scanning tool Appl. Bioinform. 1 2002 107 108
    • (2002) Appl. Bioinform. , vol.1 , pp. 107-108
    • Gattiker, A.1    Gasteiger, E.2    Bairoch, A.3
  • 32
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • H. Nielsen, J. Engelbrecht, S. Brunak, and von Heijne G. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites Protein Eng. 10 1997 1 6
    • (1997) Protein Eng. , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    Von Heijne, G.4
  • 34
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • A. Krogh, B. Larsson, G. von Heijne, and E.L.L. Sonnhammer Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes J. Mol. Biol. 305 2001 567 580
    • (2001) J. Mol. Biol. , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    Von Heijne, G.3    Sonnhammer, E.L.L.4
  • 35
    • 0033941358 scopus 로고    scopus 로고
    • Extracytoplasmic proteins of Mycobacterium tuberculosis - Mature secreted proteins often start with aspartic acid and proline
    • H.G. Wiker, M.A. Wilson, and G.K. Schoolnik Extracytoplasmic proteins of Mycobacterium tuberculosis - mature secreted proteins often start with aspartic acid and proline Microbiology 146 2000 1525 1533
    • (2000) Microbiology , vol.146 , pp. 1525-1533
    • Wiker, H.G.1    Wilson, M.A.2    Schoolnik, G.K.3
  • 39
    • 0038634975 scopus 로고    scopus 로고
    • Improvement of the GenTHREADER method for genomic fold recognition
    • L.J. McGuffin, and D.T. Jones Improvement of the GenTHREADER method for genomic fold recognition Bioinformatics 19 2003 874 881
    • (2003) Bioinformatics , vol.19 , pp. 874-881
    • McGuffin, L.J.1    Jones, D.T.2
  • 40
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice
    • J.D. Thompson, D.G. Higgins, and T.J. Gibson CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice Nucleic Acids Res. 22 1994 4673 4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 41
    • 0033515437 scopus 로고    scopus 로고
    • Inventory, assembly and analysis of Bacillus subtilis ABC transport systems
    • Y. Quentin, G. Fichant, and F. Denizot Inventory, assembly and analysis of Bacillus subtilis ABC transport systems J. Mol. Biol. 287 1999 467 484
    • (1999) J. Mol. Biol. , vol.287 , pp. 467-484
    • Quentin, Y.1    Fichant, G.2    Denizot, F.3
  • 42
    • 0033819143 scopus 로고    scopus 로고
    • The ATP binding cassette (ABC) transport systems of Mycobacterium tuberculosis
    • M. Braibant, P. Gilot, and J. Content The ATP binding cassette (ABC) transport systems of Mycobacterium tuberculosis FEMS Microbiol. Rev. 24 2000 449 467
    • (2000) FEMS Microbiol. Rev. , vol.24 , pp. 449-467
    • Braibant, M.1    Gilot, P.2    Content, J.3
  • 43
    • 0035019469 scopus 로고    scopus 로고
    • ABC transporters: Physiology, structure and mechanism - An overview
    • C.F. Higgins ABC transporters: physiology, structure and mechanism - an overview Res. Microbiol. 152 2001 205 210
    • (2001) Res. Microbiol. , vol.152 , pp. 205-210
    • Higgins, C.F.1
  • 45
    • 0034922904 scopus 로고    scopus 로고
    • Induction of cell-mediated immunity against Mycobacterium tuberculosis using DNA vaccines encoding cytotoxic and helper T-cell epitopes of the 38-kilodalton protein
    • D.P.A.J. Fonseca, B. Benaissa-Trouw, M. Van Engelen, C.A. Kraaijeveld, H. Snippe, and A.F.M. Verheul Induction of cell-mediated immunity against Mycobacterium tuberculosis using DNA vaccines encoding cytotoxic and helper T-cell epitopes of the 38-kilodalton protein Infect. Immun. 69 2001 4839 4845
    • (2001) Infect. Immun. , vol.69 , pp. 4839-4845
    • Fonseca, D.P.A.J.1    Benaissa-Trouw, B.2    Van Engelen, M.3    Kraaijeveld, C.A.4    Snippe, H.5    Verheul, A.F.M.6
  • 46
    • 0034663498 scopus 로고    scopus 로고
    • Induction of antibody and T-cell responses by immunization with ISCOMS containing the 38-kilodalton protein of Mycobacterium tuberculosis
    • D.P.A.J. da Fonseca, J. Frerichs, M. Singh, H. Snippe, and A.F.M. Verheul Induction of antibody and T-cell responses by immunization with ISCOMS containing the 38-kilodalton protein of Mycobacterium tuberculosis Vaccine 19 2001 122 131
    • (2001) Vaccine , vol.19 , pp. 122-131
    • Da Fonseca, D.P.A.J.1    Frerichs, J.2    Singh, M.3    Snippe, H.4    Verheul, A.F.M.5
  • 48
    • 0000812428 scopus 로고    scopus 로고
    • Identification of a virulence gene cluster of Mycobacterium tuberculosis by signature-tagged transposon mutagenesis
    • L.R. Camacho, D. Ensergueix, E. Perez, B. Gicquel, and C. Guilhot Identification of a virulence gene cluster of Mycobacterium tuberculosis by signature-tagged transposon mutagenesis Mol. Microbiol. 34 1999 257 267
    • (1999) Mol. Microbiol. , vol.34 , pp. 257-267
    • Camacho, L.R.1    Ensergueix, D.2    Perez, E.3    Gicquel, B.4    Guilhot, C.5
  • 49
    • 0028923695 scopus 로고
    • In-vivo growth-characteristics of leucine and methionine auxotrophic mutants of Mycobacterium bovis BCG generated by transposon mutagenesis
    • R.A. McAdam, T.R. Weisbrod, J. Martin, J.D. Scuderi, A.M Brown, J.D. Cirillo, B.R. Bloom, and W.R. Jacobs In-vivo growth-characteristics of leucine and methionine auxotrophic mutants of Mycobacterium bovis BCG generated by transposon mutagenesis Infect. Immun. 63 1995 1004 1012
    • (1995) Infect. Immun. , vol.63 , pp. 1004-1012
    • McAdam, R.A.1    Weisbrod, T.R.2    Martin, J.3    Scuderi, J.D.4    Brown, A.M.5    Cirillo, J.D.6    Bloom, B.R.7    Jacobs, W.R.8
  • 50
    • 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
    • E. Wooff, S.L. Michell, S.V. Gordon, M.A. Chambers, S. Bardarov, W.R. Jacobs, R.G. Hewinson, and P.R. Wheeler Functional genomics reveals the sole sulphate transporter of the Mycobacterium tuberculosis complex and its relevance to the acquisition of sulphur in vivo Mol. Micro. 43 2002 653 663
    • (2002) Mol. Micro. , vol.43 , pp. 653-663
    • Wooff, E.1    Michell, S.L.2    Gordon, S.V.3    Chambers, M.A.4    Bardarov, S.5    Jacobs, W.R.6    Hewinson, R.G.7    Wheeler, P.R.8
  • 51
    • 0345701347 scopus 로고    scopus 로고
    • Genes required for mycobacterial growth defined by high density mutagenesis
    • C.M. Sassetti, D.H. Boyd, and E.J. Rubin Genes required for mycobacterial growth defined by high density mutagenesis Mol. Microbiol. 48 2003 77 84
    • (2003) Mol. Microbiol. , vol.48 , pp. 77-84
    • Sassetti, C.M.1    Boyd, D.H.2    Rubin, E.J.3
  • 52
    • 0037344575 scopus 로고    scopus 로고
    • Mechanisms of iron regulation in mycobacteria: Role in physiology and virulence
    • G.M. Rodriguez, and I. Smith Mechanisms of iron regulation in mycobacteria: role in physiology and virulence Mol. Micro. 47 2003 1485 1494
    • (2003) Mol. Micro. , vol.47 , pp. 1485-1494
    • Rodriguez, G.M.1    Smith, I.2
  • 54
    • 0030935653 scopus 로고    scopus 로고
    • Cloning and sequence analysis of a class a β-lactamase from Mycobacterium tuberculosis H37Ra
    • C.J. Hackbarth, I. Unsal, and H.F. Chambers Cloning and sequence analysis of a class A β-lactamase from Mycobacterium tuberculosis H37Ra Antimicrob. Agents Chemother. 41 1997 1182 1185
    • (1997) Antimicrob. Agents Chemother. , vol.41 , pp. 1182-1185
    • Hackbarth, C.J.1    Unsal, I.2    Chambers, H.F.3
  • 55
    • 0036260378 scopus 로고    scopus 로고
    • The clavulanic acid biosynthetic cluster of Streptomyces clavuligerus: Genetic organization of the region upstream of the car gene
    • E. Mellado, L.M. Lorenzana, M. RodrIÍguez-Sáiz, B. DIÍez, P. Liras, and J.L. Barredo The clavulanic acid biosynthetic cluster of Streptomyces clavuligerus: genetic organization of the region upstream of the car gene Microbiology 148 2002 1427 1438
    • (2002) Microbiology , vol.148 , pp. 1427-1438
    • Mellado, E.1    Lorenzana, L.M.2    Rodriíguez-Sáiz, M.3    Diíez, B.4    Liras, P.5    Barredo, J.L.6
  • 56
    • 0036898699 scopus 로고    scopus 로고
    • Biochemisty and comparative genomics of SxxK superfamily acyltransferases offer a clue to the mycobacterial paradox: Presence of penicillin-susceptible target proteins versus lack of efficiency of penicillin as therapeutic agent
    • C. Goffin, and J-M. Ghuysen Biochemisty and comparative genomics of SxxK superfamily acyltransferases offer a clue to the mycobacterial paradox: presence of penicillin-susceptible target proteins versus lack of efficiency of penicillin as therapeutic agent Microbiol. Mol. Biol. Rev. 66 2002 702 738
    • (2002) Microbiol. Mol. Biol. Rev. , vol.66 , pp. 702-738
    • Goffin, C.1    Ghuysen, J.-M.2
  • 58
    • 0036263307 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis genes induced during infection of human macrophages
    • E. Dubnau, P. Fontan, R. Manganelli, S. Soares-Appel, and I. Smith Mycobacterium tuberculosis genes induced during infection of human macrophages Infect. Immun. 70 2002 2787 2795
    • (2002) Infect. Immun. , vol.70 , pp. 2787-2795
    • Dubnau, E.1    Fontan, P.2    Manganelli, R.3    Soares-Appel, S.4    Smith, I.5
  • 59
    • 0032515092 scopus 로고    scopus 로고
    • Identification and subcellular localization of a novel Cu,Zn superoxide dismutase of Mycobacterium tuberculosis
    • C.H.H. Wu, J.-J. Tsai-Wu, Y.-T. Huang, C.-Y. Lin, G.-G. Lioua, and F.-J.S. Lee Identification and subcellular localization of a novel Cu,Zn superoxide dismutase of Mycobacterium tuberculosis FEBS Lett. 439 1998 192 196
    • (1998) FEBS Lett. , vol.439 , pp. 192-196
    • Wu, C.H.H.1    Tsai-Wu, J.-J.2    Huang, Y.-T.3    Lin, C.-Y.4    Lioua, G.-G.5    Lee, F.-J.S.6
  • 61
    • 0034917354 scopus 로고    scopus 로고
    • Cu,Zn superoxide dismutase of Mycobacterium tuberculosis contributes to survival in activated macrophages that are generating an oxidative burst
    • D.L. Piddington, F.C. Fang, T. Laessig, A.M. Cooper, I.M. Orme, and N.A. Buchmeier Cu,Zn superoxide dismutase of Mycobacterium tuberculosis contributes to survival in activated macrophages that are generating an oxidative burst Infect. Immun. 69 2001 4980 4987
    • (2001) Infect. Immun. , vol.69 , pp. 4980-4987
    • Piddington, D.L.1    Fang, F.C.2    Laessig, T.3    Cooper, A.M.4    Orme, I.M.5    Buchmeier, N.A.6
  • 63
    • 0037422617 scopus 로고    scopus 로고
    • Expression of Th1-mediated immunity in mouse lungs induces a Mycobacterium tuberculosis transcription pattern characteristic of nonreplicating persistence
    • L.B. Shi, Y.-J. Jung, S. Tyagi, M.L. Gennaro, and R.J. North Expression of Th1-mediated immunity in mouse lungs induces a Mycobacterium tuberculosis transcription pattern characteristic of nonreplicating persistence Proc. Natl. Acad. Sci. USA 100 2003 241 246
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 241-246
    • Shi, L.B.1    Jung, Y.-J.2    Tyagi, S.3    Gennaro, M.L.4    North, R.J.5
  • 64
  • 66
    • 0031859798 scopus 로고    scopus 로고
    • Schizosaccharomyces pombe isp4 encodes a transporter representing a novel family of oligopeptide transporters
    • M.A. Lubkowitz, D. Barnes, M. Breslav, A. Burchfield, F. Naider, and J.M. Becker Schizosaccharomyces pombe isp4 encodes a transporter representing a novel family of oligopeptide transporters Mol. Microbiol. 28 1998 729 741
    • (1998) Mol. Microbiol. , vol.28 , pp. 729-741
    • Lubkowitz, M.A.1    Barnes, D.2    Breslav, M.3    Burchfield, A.4    Naider, F.5    Becker, J.M.6
  • 67
    • 0031923498 scopus 로고    scopus 로고
    • Molecular analysis of the gene encoding F-420-dependent glucose-6-phosphate dehydrogenase from Mycobacterium smegmatis
    • E. Purwantini, and L. Daniels Molecular analysis of the gene encoding F-420-dependent glucose-6-phosphate dehydrogenase from Mycobacterium smegmatis J. Bacteriol. 180 1998 2212 2219
    • (1998) J. Bacteriol. , vol.180 , pp. 2212-2219
    • Purwantini, E.1    Daniels, L.2
  • 68
  • 69
    • 0942287201 scopus 로고    scopus 로고
    • Gram-positive DsbE proteins function differently from Gram-negative DsbE homologs. a structure to function analysis of DsbE from Mycobacterium tuberculosis
    • C.W. Goulding, M.I. Apostol, S. Gleiter, A. Parseghiani, J. Bardwell, M. Gennaro, and D. Eisenberg Gram-positive DsbE proteins function differently from Gram-negative DsbE homologs. A structure to function analysis of DsbE from Mycobacterium tuberculosis J. Biol. Chem. 279 2004 3516 3524
    • (2004) J. Biol. Chem. , vol.279 , pp. 3516-3524
    • Goulding, C.W.1    Apostol, M.I.2    Gleiter, S.3    Parseghiani, A.4    Bardwell, J.5    Gennaro, M.6    Eisenberg, D.7
  • 70
    • 0036032176 scopus 로고    scopus 로고
    • The multicopper oxidase of Pseudomonas aeruginosa is a ferroxidase with a central role in iron acquisition
    • W.M. Huston, M.P. Jennings, and A.G. McEwan The multicopper oxidase of Pseudomonas aeruginosa is a ferroxidase with a central role in iron acquisition Mol. Microbiol. 45 2002 1741 1750
    • (2002) Mol. Microbiol. , vol.45 , pp. 1741-1750
    • Huston, W.M.1    Jennings, M.P.2    McEwan, A.G.3
  • 71
    • 0029064062 scopus 로고
    • Homology between the MPB70 and MPB83 proteins of Mycobacterium bovis BCG
    • M. Harboe, S. Nagai, H.G. Wiker, K. Sletten, and S. Haga Homology between the MPB70 and MPB83 proteins of Mycobacterium bovis BCG Scand. J. Immunol. 42 1995 46 51
    • (1995) Scand. J. Immunol. , vol.42 , pp. 46-51
    • Harboe, M.1    Nagai, S.2    Wiker, H.G.3    Sletten, K.4    Haga, S.5
  • 73
    • 0030969807 scopus 로고    scopus 로고
    • Characterisation of a lipoprotein in Mycobacterium bovis (BCG) with sequence similarity to the secreted protein MPB70
    • W. Vosloo, P. Tippoo, J.E. Hughes, N. Harriman, M. Emms, D.W. Beatty, H. Zappe, and L.M. Steyn Characterisation of a lipoprotein in Mycobacterium bovis (BCG) with sequence similarity to the secreted protein MPB70 Gene 188 1997 123 128
    • (1997) Gene , vol.188 , pp. 123-128
    • Vosloo, W.1    Tippoo, P.2    Hughes, J.E.3    Harriman, N.4    Emms, M.5    Beatty, D.W.6    Zappe, H.7    Steyn, L.M.8
  • 75
    • 0029974805 scopus 로고    scopus 로고
    • Molecular characterization of MPT83: A seroreactive antigen of Mycobacterium tuberculosis with homology to MPT70
    • R.G. Hewinson, S.L. Michell, W.P. Russell, R.A. McAdam, and W.R. Jacobs Molecular characterization of MPT83: A seroreactive antigen of Mycobacterium tuberculosis with homology to MPT70 Scand. J. Immunol. 43 1996 490 499
    • (1996) Scand. J. Immunol. , vol.43 , pp. 490-499
    • Hewinson, R.G.1    Michell, S.L.2    Russell, W.P.3    McAdam, R.A.4    Jacobs, W.R.5
  • 78
    • 0035845653 scopus 로고    scopus 로고
    • Characterization of the Mycobacterium tuberculosis region containing the mpt83 and mpt70 genes
    • M.D. Juárez, A. Torres, and C. Espitia Characterization of the Mycobacterium tuberculosis region containing the mpt83 and mpt70 genes FEMS Microbiol. Lett. 203 2001 95 102
    • (2001) FEMS Microbiol. Lett. , vol.203 , pp. 95-102
    • Juárez, M.D.1    Torres, A.2    Espitia, C.3
  • 81
    • 0028929007 scopus 로고
    • Relationship of secretion pattern and MPB70 homology with osteoblast-specific factor-2 to osteitis following Mycobacterium bovis BCG vaccination
    • J.C. Ulstrup, S. Jeansson, H.G. Wiker, and M. Harboe Relationship of secretion pattern and MPB70 homology with osteoblast-specific factor-2 to osteitis following Mycobacterium bovis BCG vaccination Infect. Immun. 63 1995 672 675
    • (1995) Infect. Immun. , vol.63 , pp. 672-675
    • Ulstrup, J.C.1    Jeansson, S.2    Wiker, H.G.3    Harboe, M.4
  • 82
    • 0027424110 scopus 로고
    • Cloning of an Mycobacterium tuberculosis DNA fragment associated with entry and survival inside cells
    • S. Arruda, G. Bomfim, R. Knights, T. Huimabyron, and L.W. Riley Cloning of an Mycobacterium tuberculosis DNA fragment associated with entry and survival inside cells Science 261 1995 1454 1457
    • (1995) Science , vol.261 , pp. 1454-1457
    • Arruda, S.1    Bomfim, G.2    Knights, R.3    Huimabyron, T.4    Riley, L.W.5
  • 83
    • 0032871598 scopus 로고    scopus 로고
    • The mammalian cell entry operon 1 (mce1) of Mycobacterium leprae and Mycobacterium tuberculosis
    • H.G. Wiker, E. Spierings, M.A.B. Kolkman, T.H.M. Ottenhoff, and M. Harboe The mammalian cell entry operon 1 (mce1) of Mycobacterium leprae and Mycobacterium tuberculosis Microb. Pathog. 27 1999 173 177
    • (1999) Microb. Pathog. , vol.27 , pp. 173-177
    • Wiker, H.G.1    Spierings, E.2    Kolkman, M.A.B.3    Ottenhoff, T.H.M.4    Harboe, M.5
  • 84
    • 0032815631 scopus 로고    scopus 로고
    • Disruption of the mycobacterial cell entry gene of Mycobacterium bovis BCG results in a mutant that exhibits a reduced invasiveness for epithelial cells
    • B. Flesselles, N.N. Anand, J. Remani, S.M. Loosmore, and M.H. Klein Disruption of the mycobacterial cell entry gene of Mycobacterium bovis BCG results in a mutant that exhibits a reduced invasiveness for epithelial cells FEMS Microbiol. Lett. 177 1999 237 242
    • (1999) FEMS Microbiol. Lett. , vol.177 , pp. 237-242
    • Flesselles, B.1    Anand, N.N.2    Remani, J.3    Loosmore, S.M.4    Klein, M.H.5
  • 86
    • 0037013820 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis mammalian cell entry operon (mce) homologs in Mycobacterium other than tuberculosis (MOTT)
    • Y. Haile, D.A. Caugant, G. Bjune, and H.G. Wiker Mycobacterium tuberculosis mammalian cell entry operon (mce) homologs in Mycobacterium other than tuberculosis (MOTT) FEMS Immunol. Med. Microbiol. 33 2002 125 132
    • (2002) FEMS Immunol. Med. Microbiol. , vol.33 , pp. 125-132
    • Haile, Y.1    Caugant, D.A.2    Bjune, G.3    Wiker, H.G.4
  • 88
    • 0032696091 scopus 로고    scopus 로고
    • Cloning, expression and immunological reactivity of two mammalian cell entry proteins encoded by the mce1 operon of Mycobacterium tuberculosis
    • S. Ahmad, P.K. Akbar, H.G. Wiker, M. Harboe, and A.S. Mustafa Cloning, expression and immunological reactivity of two mammalian cell entry proteins encoded by the mce1 operon of Mycobacterium tuberculosis Scand. J. Immunol. 50 1999 510 518
    • (1999) Scand. J. Immunol. , vol.50 , pp. 510-518
    • Ahmad, S.1    Akbar, P.K.2    Wiker, H.G.3    Harboe, M.4    Mustafa, A.S.5
  • 89
    • 0036775772 scopus 로고    scopus 로고
    • Comparative and functional genomics of the Mycobacterium tuberculosis complex
    • S.T. Cole Comparative and functional genomics of the Mycobacterium tuberculosis complex Microbiology 148 2002 2919 2928
    • (2002) Microbiology , vol.148 , pp. 2919-2928
    • Cole, S.T.1
  • 90
    • 0036084382 scopus 로고    scopus 로고
    • Mycobacterium avium genes expressed during growth in human macrophages detected by selective capture of transcribed sequences (SCOTS)
    • J.Y. Hou, J.E. Graham, and J.E. Clark-Curtiss Mycobacterium avium genes expressed during growth in human macrophages detected by selective capture of transcribed sequences (SCOTS) Infect. Immun. 70 2002 3714 3726
    • (2002) Infect. Immun. , vol.70 , pp. 3714-3726
    • Hou, J.Y.1    Graham, J.E.2    Clark-Curtiss, J.E.3
  • 91
    • 0037329291 scopus 로고    scopus 로고
    • Interaction of the sensor module of Mycobacterium tuberculosis H37Rv KdpD with members of the Lpr family
    • A.J.C. Steyn, J. Joseph, and B.R. Bloom Interaction of the sensor module of Mycobacterium tuberculosis H37Rv KdpD with members of the Lpr family Mol. Microbiol. 47 2003 1074 1089
    • (2003) Mol. Microbiol. , vol.47 , pp. 1074-1089
    • Steyn, A.J.C.1    Joseph, J.2    Bloom, B.R.3
  • 92
    • 0030697416 scopus 로고    scopus 로고
    • KapB is a lipoprotein required for KinB signal transduction and activation of the phosphorelay to sporulation in Bacillus subtilis.
    • V. Dartois, T. Djavakhishvili, and J.A. Hoch KapB is a lipoprotein required for KinB signal transduction and activation of the phosphorelay to sporulation in Bacillus subtilis. Mol. Microbiol. 26 1997 1097 1108
    • (1997) Mol. Microbiol. , vol.26 , pp. 1097-1108
    • Dartois, V.1    Djavakhishvili, T.2    Hoch, J.A.3
  • 93
    • 0030682524 scopus 로고    scopus 로고
    • A novel mycobacterial antigen relevant to cellular immunity belongs to a family of secreted lipoproteins
    • F. Oftung, H.G. Wiker, A. Deggerdal, and A.S. Mustafa A novel mycobacterial antigen relevant to cellular immunity belongs to a family of secreted lipoproteins Scand. J. Immunol. 46 1997 445 451
    • (1997) Scand. J. Immunol. , vol.46 , pp. 445-451
    • Oftung, F.1    Wiker, H.G.2    Deggerdal, A.3    Mustafa, A.S.4
  • 94
    • 0034039869 scopus 로고    scopus 로고
    • The gene encoding P27 lipoprotein and a putative antibiotic-resistance gene form an operon in Mycobacterium tuberculosis and Mycobacterium bovis
    • F. Bigi, A. Alito, M.I. Romano, M. Zumarraga, K. Caimi, and A. Cataldi The gene encoding P27 lipoprotein and a putative antibiotic-resistance gene form an operon in Mycobacterium tuberculosis and Mycobacterium bovis Microbiol. 146 2000 1011 1018
    • (2000) Microbiol. , vol.146 , pp. 1011-1018
    • Bigi, F.1    Alito, A.2    Romano, M.I.3    Zumarraga, M.4    Caimi, K.5    Cataldi, A.6
  • 95
    • 0343920728 scopus 로고    scopus 로고
    • Cloning of the gene encoding a 22-kilodalton cell surface antigen of Mycobacterium bovis BCG and analysis of its potential for DNA vaccination against tuberculosis
    • P. Lefèvre, O. Denis, L. De Wit, A. Tanghe, P. Vandenbussche, J. Content, and K. Huygen Cloning of the gene encoding a 22-kilodalton cell surface antigen of Mycobacterium bovis BCG and analysis of its potential for DNA vaccination against tuberculosis Infect. Immun. 68 2000 1040 1047
    • (2000) Infect. Immun. , vol.68 , pp. 1040-1047
    • Lefèvre, P.1    Denis, O.2    De Wit, L.3    Tanghe, A.4    Vandenbussche, P.5    Content, J.6    Huygen, K.7
  • 96
    • 0037767314 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis recombinant 27-kilodalton lipoprotein induces a strong Th1-type immune response deleterious to protection
    • A.-H. Hovav, J. Mullerad, L. Davidovitch, L. Fishman, F. Bigi, A. Cataldi, and H. Bercovier The Mycobacterium tuberculosis recombinant 27-kilodalton lipoprotein induces a strong Th1-type immune response deleterious to protection Infect. Immun. 71 2003 3146 3154
    • (2003) Infect. Immun. , vol.71 , pp. 3146-3154
    • Hovav, A.-H.1    Mullerad, J.2    Davidovitch, L.3    Fishman, L.4    Bigi, F.5    Cataldi, A.6    Bercovier, H.7
  • 100
    • 0034130307 scopus 로고    scopus 로고
    • Bacterial dormancy and culturability: The role of autocrine growth factors
    • D.B. Kell, and M. Young Bacterial dormancy and culturability: the role of autocrine growth factors Curr. Opin. Microbiol. 3 2000 238 243
    • (2000) Curr. Opin. Microbiol. , vol.3 , pp. 238-243
    • Kell, D.B.1    Young, M.2
  • 102
    • 0042161746 scopus 로고    scopus 로고
    • Resuscitation factors from mycobacteria: Homologs of Micrococcus luteus proteins
    • W. Zhu, B.B. Plikaytis, and T.M. Shinnick Resuscitation factors from mycobacteria: homologs of Micrococcus luteus proteins Tuberculosis 83 2003 261 269
    • (2003) Tuberculosis , vol.83 , pp. 261-269
    • Zhu, W.1    Plikaytis, B.B.2    Shinnick, T.M.3
  • 103
    • 0347511902 scopus 로고    scopus 로고
    • Individual Mycobacterium tuberculosis resuscitation-promoting factor homologues are dispensable for growth in vitro and in vivo
    • J.M. Tufariello, W.R. Jacobs Jr., and J. Chan Individual Mycobacterium tuberculosis resuscitation-promoting factor homologues are dispensable for growth in vitro and in vivo Infect. Immun. 72 2004 515 526
    • (2004) Infect. Immun. , vol.72 , pp. 515-526
    • Tufariello, J.M.1    Jacobs Jr., W.R.2    Chan, J.3
  • 104
    • 0035854480 scopus 로고    scopus 로고
    • Crystal structures of YBHB and YBCL from Escherichia coli, two bacterial homologues to a Raf kinase inhibitor protein
    • L. Serre, K.P. de Jesus, C. Zelwer, N. Bureaud, F. Schoentgen, and H. Bénédetti Crystal structures of YBHB and YBCL from Escherichia coli, two bacterial homologues to a Raf kinase inhibitor protein J. Mol. Biol. 310 2001 617 634
    • (2001) J. Mol. Biol. , vol.310 , pp. 617-634
    • Serre, L.1    De Jesus, K.P.2    Zelwer, C.3    Bureaud, N.4    Schoentgen, F.5    Bénédetti, H.6
  • 106
    • 0034194181 scopus 로고    scopus 로고
    • The eukaryotic-like Ser/Thr protein kinases of Mycobacterium tuberculosis
    • Y. Av-Gay, and M. Everett The eukaryotic-like Ser/Thr protein kinases of Mycobacterium tuberculosis Trends Microbiol. 8 2000 238 244
    • (2000) Trends Microbiol. , vol.8 , pp. 238-244
    • Av-Gay, Y.1    Everett, M.2
  • 107
    • 0024580999 scopus 로고
    • Nucleotide sequence of the 19 kDa antigen gene from Mycobacterium tuberculosis
    • K.R. Ashbridge, R.J. Booth, J.D. Watson, and R. Lathigra Nucleotide sequence of the 19 kDa antigen gene from Mycobacterium tuberculosis Nucleic Acids Res. 17 1989 1249
    • (1989) Nucleic Acids Res. , vol.17 , pp. 1249
    • Ashbridge, K.R.1    Booth, R.J.2    Watson, J.D.3    Lathigra, R.4
  • 108
    • 0026683498 scopus 로고
    • Nucleotide sequence analysis and serologic characterization of the Mycobacterium intracellulare homolog of the Mycobacterium tuberculosis 19-kDa antigen
    • J. Nair, D.A. Rouse, and S.L. Morris Nucleotide sequence analysis and serologic characterization of the Mycobacterium intracellulare homolog of the Mycobacterium tuberculosis 19-kDa antigen Mol. Microbiol. 6 1992 1431 1439
    • (1992) Mol. Microbiol. , vol.6 , pp. 1431-1439
    • Nair, J.1    Rouse, D.A.2    Morris, S.L.3
  • 110
    • 0029871336 scopus 로고    scopus 로고
    • Lack of production of the 19-kDa glycolipoprotein in certain strains of Mycobacterium tuberculosis
    • R. Lathigra, Y. Zhang, M. Hill, M.J. Garcia, P.S. Jackett, and J. Ivanyi Lack of production of the 19-kDa glycolipoprotein in certain strains of Mycobacterium tuberculosis Res. Microbiol. 147 1996 237 249
    • (1996) Res. Microbiol. , vol.147 , pp. 237-249
    • Lathigra, R.1    Zhang, Y.2    Hill, M.3    Garcia, M.J.4    Jackett, P.S.5    Ivanyi, J.6
  • 111
    • 0027514448 scopus 로고
    • Expression of the Mycobacterium tuberculosis 19-kilodalton antigen in Mycobacterium smegmatis: Immunological analysis and evidence of glycosylation
    • T. Garbe, D. Harris, M. Vordermeier, R. Lathigra, J. Ivanyi, and D. Young Expression of the Mycobacterium tuberculosis 19-kilodalton antigen in Mycobacterium smegmatis: immunological analysis and evidence of glycosylation Infect. Immun. 61 1993 260 267
    • (1993) Infect. Immun. , vol.61 , pp. 260-267
    • Garbe, T.1    Harris, D.2    Vordermeier, M.3    Lathigra, R.4    Ivanyi, J.5    Young, D.6
  • 112
    • 0029896457 scopus 로고    scopus 로고
    • Bacterial glycoproteins: A link between glycosylation and proteolytic cleavage of a 19 kDa antigen from Mycobacterium tuberculosis
    • J.L. Herrmann, P. O'Gaora, A. Gallagher, J.E.R. Thole, and D.B. Young Bacterial glycoproteins: A link between glycosylation and proteolytic cleavage of a 19 kDa antigen from Mycobacterium tuberculosis EMBO J. 15 1996 3547 3554
    • (1996) EMBO J. , vol.15 , pp. 3547-3554
    • Herrmann, J.L.1    O'Gaora, P.2    Gallagher, A.3    Thole, J.E.R.4    Young, D.B.5
  • 114
    • 0033679243 scopus 로고    scopus 로고
    • Evaluation of T-cell responses to peptides and lipopeptides with MHC class I binding motifs derived from the amino acid sequence of the 19-kDa lipoprotein of Mycobacterium tuberculosis
    • D.P.A.J. Fonseca, D. Joosten, H. Snippe, and A.F.M. Verheul Evaluation of T-cell responses to peptides and lipopeptides with MHC class I binding motifs derived from the amino acid sequence of the 19-kDa lipoprotein of Mycobacterium tuberculosis Mol. Immunol. 37 2000 413 422
    • (2000) Mol. Immunol. , vol.37 , pp. 413-422
    • Fonseca, D.P.A.J.1    Joosten, D.2    Snippe, H.3    Verheul, A.F.M.4
  • 116
    • 0035423453 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis 19-kDa lipoprotein promotes neutrophil activation
    • C. Neufert, R.K. Pai, E.H. Noss, M. Berger, W.H. Boom, and C.V. Harding Mycobacterium tuberculosis 19-kDa lipoprotein promotes neutrophil activation J. Immunol. 167 2001 1542 1549
    • (2001) J. Immunol. , vol.167 , pp. 1542-1549
    • Neufert, C.1    Pai, R.K.2    Noss, E.H.3    Berger, M.4    Boom, W.H.5    Harding, C.V.6
  • 118
    • 0344643405 scopus 로고    scopus 로고
    • The 19-kDa Mycobacterium tuberculosis protein induces macrophage apoptosis through toll-like receptor-2
    • M. Lopez, L.M. Sly, Y. Luu, D. Young, H. Cooper, and N.E. Reiner The 19-kDa Mycobacterium tuberculosis protein induces macrophage apoptosis through toll-like receptor-2 J. Immunol. 170 2003 2409 2416
    • (2003) J. Immunol. , vol.170 , pp. 2409-2416
    • Lopez, M.1    Sly, L.M.2    Luu, Y.3    Young, D.4    Cooper, H.5    Reiner, N.E.6
  • 119
  • 120
    • 0030728443 scopus 로고    scopus 로고
    • MTC28, a novel 28-kilodalton proline-rich secreted antigen specific for the Mycobacterium tuberculosis complex
    • C. Manca, K. Lyashchenko, R. Colangeli, and M.L. Gennaro MTC28, a novel 28-kilodalton proline-rich secreted antigen specific for the Mycobacterium tuberculosis complex Infect. Immun. 65 1997 4951 4957
    • (1997) Infect. Immun. , vol.65 , pp. 4951-4957
    • Manca, C.1    Lyashchenko, K.2    Colangeli, R.3    Gennaro, M.L.4
  • 122
    • 0036081140 scopus 로고    scopus 로고
    • IdeR, an essential gene in Mycobacterium tuberculosis: Role of IdeR in iron-dependent gene expression, iron metabolism, and oxidative stress response
    • G.M. Rodriguez, M.I. Voskuil, B. Gold, G.K. Schoolnik, and I. Smith ideR, an essential gene in Mycobacterium tuberculosis: role of IdeR in iron-dependent gene expression, iron metabolism, and oxidative stress response Infect. Immun. 70 2002 3371 3381
    • (2002) Infect. Immun. , vol.70 , pp. 3371-3381
    • Rodriguez, G.M.1    Voskuil, M.I.2    Gold, B.3    Schoolnik, G.K.4    Smith, I.5
  • 123
    • 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
    • P. Lefèvre, M. Braibant, L. DeWit, M. Kalai, D. Röeper, J. Grötzinger, J.P. Delville, P. Peirs, J. Ooms, K. Huygen, and J. Content 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 1997 2900 2906
    • (1997) J. Bacteriol. , vol.179 , pp. 2900-2906
    • Lefèvre, P.1    Braibant, M.2    Dewit, L.3    Kalai, M.4    Röeper, D.5    Grötzinger, J.6    Delville, J.P.7    Peirs, P.8    Ooms, J.9    Huygen, K.10    Content, J.11
  • 124
    • 0026653748 scopus 로고
    • Phosphate starvation enhances expression of the immunodominant 38-kilodalton protein antigen of Mycobacterium tuberculosis: Demonstration by immunogold electron-microscopy
    • C. Espitia, M. Elinos, R. Hernández-Pando, and R. Mancilla Phosphate starvation enhances expression of the immunodominant 38-kilodalton protein antigen of Mycobacterium tuberculosis: demonstration by immunogold electron-microscopy Infect. Immun. 60 1992 2998 3001
    • (1992) Infect. Immun. , vol.60 , pp. 2998-3001
    • Espitia, C.1    Elinos, M.2    Hernández-Pando, R.3    Mancilla, R.4
  • 126
    • 0025270327 scopus 로고
    • Evidence that protein antigen b of Mycobacterium tuberculosis is involved in phosphate metabolism
    • A.B. Andersen, L. Ljungqvist, and M. Olsen Evidence that protein antigen b of Mycobacterium tuberculosis is involved in phosphate metabolism J. Gen. Microbiol. 136 1990 477 480
    • (1990) J. Gen. Microbiol. , vol.136 , pp. 477-480
    • Andersen, A.B.1    Ljungqvist, L.2    Olsen, M.3
  • 127
    • 0029965091 scopus 로고    scopus 로고
    • Definition of the full extent of glycosylation of the 45-kilodalton glycoprotein of Mycobacterium tuberculosis
    • K.M. Dobos, K.H. Khoo, K.M. Swiderek, P.J. Brennan, and J.T. Belisle Definition of the full extent of glycosylation of the 45-kilodalton glycoprotein of Mycobacterium tuberculosis J. Bacteriol. 178 1996 2498 2506
    • (1996) J. Bacteriol. , vol.178 , pp. 2498-2506
    • Dobos, K.M.1    Khoo, K.H.2    Swiderek, K.M.3    Brennan, P.J.4    Belisle, J.T.5
  • 128
    • 0034685684 scopus 로고    scopus 로고
    • Analysis of post-translational modification of mycobacterial proteins using a cassette expression system
    • J.L. Herrmann, R. Delahay, A. Gallagher, B. Robertson, and D. Young Analysis of post-translational modification of mycobacterial proteins using a cassette expression system FEBS Lett. 473 2000 358 362
    • (2000) FEBS Lett. , vol.473 , pp. 358-362
    • Herrmann, J.L.1    Delahay, R.2    Gallagher, A.3    Robertson, B.4    Young, D.5


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