메뉴 건너뛰기




Volumn 7, Issue 2, 2000, Pages 141-146

Crystal structure of the secreted form of antigen 85C reveals potential targets for mycobacterial drugs and vaccines

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; ANTIMYCOBACTERIAL AGENT; BACTERIAL ANTIGEN; BCG VACCINE; CORD FACTOR; ETHAMBUTOL; FIBRONECTIN; ISONIAZID; MYCOLIC ACID;

EID: 0033960935     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/72413     Document Type: Article
Times cited : (168)

References (44)
  • 1
    • 0013823748 scopus 로고
    • Extracellular proteins of tubercle bacilli. IV. Alpha and beta antigens as major extracellular protein products and as cellular components of a strain (H37Rv) of
    • Fukui, Y., Mirai, T., Uchida, T. & Yoneda, M. Extracellular proteins of tubercle bacilli. IV. Alpha and beta antigens as major extracellular protein products and as cellular components of a strain (H37Rv) of Mycobacterium tuberculosis. Biken J.8, 189-199(1965).
    • (1965) Mycobacterium Tuberculosis. Biken J. , vol.8 , pp. 189-199
    • Fukui, Y.1    Mirai, T.2    Uchida, T.3    Yoneda, M.4
  • 2
    • 0031007903 scopus 로고    scopus 로고
    • Role of the major antigen of Mycobacterium tuberculosis in cell wall biogenesis
    • Belisle, J.T. et al. Role of the major antigen of Mycobacterium tuberculosis in cell wall biogenesis. Science 276.1420-1422 (1997).
    • (1997) Science , vol.276 , pp. 1420-1422
    • Belisle, J.T.1
  • 4
    • 0032982736 scopus 로고    scopus 로고
    • Inactivation of the antigen 85C gene profoundly affects the mycolate content and alters the permeability of the Mycobacterium tuberculosis cell envelope
    • Jackson, M. et al. Inactivation of the antigen 85C gene profoundly affects the mycolate content and alters the permeability of the Mycobacterium tuberculosis cell envelope. Mol. Microbiol. 31.1573-1587 (1999).
    • (1999) Mol. Microbiol. , vol.31 , pp. 1573-1587
    • Jackson, M.1
  • 5
    • 33847557568 scopus 로고
    • Hydrazine derivatives of isonicotinic acid (Rimifon, Marsilid) in the treatment of active progressive caseous-pneumonic tuberculosis
    • Robitzek, E.H. & Selikoff, I.J. Hydrazine derivatives of isonicotinic acid (Rimifon, Marsilid) in the treatment of active progressive caseous-pneumonic tuberculosis. Am. Rev. Tuberc. Pu/m. Dis. 65,765 (1952).
    • (1952) Am. Rev. Tuberc. Pu/m. Dis. , vol.65 , pp. 765
    • Robitzek, E.H.1    Selikoff, I.J.2
  • 6
    • 0029943128 scopus 로고    scopus 로고
    • Molecular mechanisms of drug resistance in Mycobacterium tuberculosis
    • Blanchard, J.S. Molecular mechanisms of drug resistance in Mycobacterium tuberculosis. Annu. Rev. Biochem. 65, 215-239 (1996).
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 215-239
    • Blanchard, J.S.1
  • 7
    • 0028156861 scopus 로고
    • InhA, a gene encoding a target for isoniazid and ethionamide in Mycobacterium tuberculosis
    • Banerjee, A. et si. inhA, a gene encoding a target for isoniazid and ethionamide in Mycobacterium tuberculosis. Science 263, 227-230 (1994).
    • (1994) Science , vol.263 , pp. 227-230
    • Banerjee, A.1
  • 8
    • 0024431530 scopus 로고
    • Inhibition of synthesis of arabinogalactan in Mycobacterium smegmatis
    • Takayama, K.& Kilburn, J.O. Inhibition of synthesis of arabinogalactan in Mycobacterium smegmatis. Antimicrob Agents Chemother. 33, 1493-1499 (1989).
    • (1989) Antimicrob Agents Chemother. , vol.33 , pp. 1493-1499
    • Takayama, K.1    Kilburn, J.O.2
  • 9
    • 0021994252 scopus 로고
    • Role of cord factor in the modulation of infection caused by mycobacteria
    • Suva, C.L., Ekizlerian, S.M. & Fazioli, R. Role of cord factor in the modulation of infection caused by mycobacteria. Am. 1. Pathol. 118,238-247 (1985).
    • (1985) Am. 1. Pathol. , vol.118 , pp. 238-247
    • Suva, C.L.1    Ekizlerian, S.M.2    Fazioli, R.3
  • 10
    • 0030874881 scopus 로고    scopus 로고
    • Upases and α/β hydrolase fold
    • Schrag, J.D. & Cygler, M. upases and α/β hydrolase fold. Methods Enzymol. 284, 85-107(1997).
    • (1997) Methods Enzymol. , vol.284 , pp. 85-107
    • Schrag, J.D.1    Cygler, M.2
  • 11
    • 0027288357 scopus 로고
    • Proteases-structures, mechanism and inhibitors
    • Powers, J.C. et al. Proteases-structures, mechanism and inhibitors. Agents Actions Suppl. 42,3-18 (1993).
    • (1993) Agents Actions Suppl. , vol.42 , pp. 3-18
    • Powers, J.C.1
  • 12
    • 0017324044 scopus 로고
    • Serine proteases: Structure and mechanism of catalysis
    • Kraut, J. Serine proteases: structure and mechanism of catalysis. Annu. Rev. Biochem. 46, 331-358 (1977).
    • (1977) Annu. Rev. Biochem. , vol.46 , pp. 331-358
    • Kraut, J.1
  • 13
    • 0029161231 scopus 로고
    • The 2.46 A resolution structure of the pancreatic lipase-colipase complex inhibited bya C11 alkyl phosphonate
    • Egloff, M.P. et al. The 2.46 A resolution structure of the pancreatic lipase-colipase complex inhibited bya C11 alkyl phosphonate. Biochemistry34, 2751-2762 (1995).
    • (1995) Biochemistry , vol.34 , pp. 2751-2762
    • Egloff, M.P.1
  • 14
    • 0029417196 scopus 로고
    • Crystallographic and molecular-modeling studies of lipase B from Candida antarctica reveal a stereospecificity pocket for secondary alcohols
    • Uppenberg, J. et al. Crystallographic and molecular-modeling studies of lipase B from Candida antarctica reveal a stereospecificity pocket for secondary alcohols. Biochemistry 3t. 16838-16851 (1995).
    • (1995) Biochemistry , vol.3 , pp. 16838-16851
    • Uppenberg, J.1
  • 15
    • 0029912405 scopus 로고    scopus 로고
    • Peptide aldehyde complexes with wheat serine carboxypeptidase II: Implications for the catalytic mechanism and substrate specificity
    • Bullock, T.L., Breddam, K. & Remington, S.J. Peptide aldehyde complexes with wheat serine carboxypeptidase II: implications for the catalytic mechanism and substrate specificity. J. Mol. Biol. 255, 714-725 (1996).
    • (1996) J. Mol. Biol. , vol.255 , pp. 714-725
    • Bullock, T.L.1    Breddam, K.2    Remington, S.J.3
  • 16
    • 0030984483 scopus 로고    scopus 로고
    • Covalent inactivation of upases
    • Ransac, S. et al. Covalent inactivation of upases. Methods Enzymol. 286, 190-231 (1997).
    • (1997) Methods Enzymol. , vol.286 , pp. 190-231
    • Ransac, S.1
  • 17
    • 0028173919 scopus 로고
    • Inactivation of Staphylococcus hyicus lipase by hexadecylsulfonyl fluoride: Evidence for an active site serine
    • Leuveling Tjeenk, M. et al. Inactivation of Staphylococcus hyicus lipase by hexadecylsulfonyl fluoride: evidence for an active site serine. Protein Eng. 7, 579 (1994).
    • (1994) Protein Eng. , vol.7 , pp. 579
    • Leuveling Tjeenk, M.1
  • 18
    • 0015504876 scopus 로고
    • Action of organophosphates and sulfonyl halides on porcine pancreatic lipase
    • Maylie, M.F., Charles, M.& Desnuelle P. Action of organophosphates and sulfonyl halides on porcine pancreatic lipase. Biochim. Biophys. Acta 276,162-175 (1972).
    • (1972) Biochim. Biophys. Acta , vol.276 , pp. 162-175
    • Maylie, M.F.1    Charles, M.2    Desnuelle, P.3
  • 19
    • 0031574909 scopus 로고    scopus 로고
    • Atomic resolution (1.0 A) crystal structure of Fusarium so/an/ cutinase: Stereochemical analysis
    • Longhi, S., Czjzek, M., Lamzin, V., Nicolas. A. & Cambillau C. Atomic resolution (1.0 A) crystal structure of Fusarium so/an/ cutinase: stereochemical analysis. J. Mol. Biol. 268,779-799 (1997).
    • (1997) J. Mol. Biol. , vol.268 , pp. 779-799
    • Longhi, S.1    Czjzek, M.2    Lamzin, V.3    Nicolas, A.4    Cambillau, C.5
  • 20
    • 0027957435 scopus 로고
    • Cutinase, a lipolytic enzyme with a preformed oxyanion hole
    • Martinez, C. Cutinase, a lipolytic enzyme with a preformed oxyanion hole. Biochemistry 33, 83-89 (1994).
    • (1994) Biochemistry , vol.33 , pp. 83-89
    • Martinez, C.1
  • 21
    • 0023689742 scopus 로고
    • Characterization of fibronectin-binding antigens released by Mycobacterium tuberculosis and Mycobacterium bovis BCG
    • Abou-Zeid, C.etal. Characterization of fibronectin-binding antigens released by Mycobacterium tuberculosis and Mycobacterium bovis BCG. Infect. Immun. 56, 3046-3051 (1988).
    • (1988) Infect. Immun. , vol.56 , pp. 3046-3051
    • Abou-Zeid, C.1
  • 22
    • 0025946883 scopus 로고
    • Phagocytosis of Mycobacterium leprae by human monocyte-derived macrophages is mediated by complement receptors CR1 (CD35). CR3 (CD11b/CD18), and CR4 (CD11C/CD18) and IFN-γ activation inhibits complement receptor function and phagocytosis of this bacterium
    • Schlesinger L.S.& Horowitz, M.A. Phagocytosis of Mycobacterium leprae by human monocyte-derived macrophages is mediated by complement receptors CR1 (CD35). CR3 (CD11b/CD18), and CR4 (CD11C/CD18) and IFN-γ activation inhibits complement receptor function and phagocytosis of this bacterium. J. Immunol. 147, 1983-1994(1991).
    • (1991) J. Immunol. , vol.147 , pp. 1983-1994
    • Schlesinger, L.S.1    Horowitz, M.A.2
  • 23
    • 0030777141 scopus 로고    scopus 로고
    • A macrophage invasion mechanism of pathogenic mycobacteria
    • Schorey, J.S., Carroll, M.C.& Brown, E.J. A macrophage invasion mechanism of pathogenic mycobacteria. Science 277,1091-1093 (1997).
    • (1997) Science , vol.277 , pp. 1091-1093
    • Schorey, J.S.1    Carroll, M.C.2    Brown, E.J.3
  • 24
    • 0032579246 scopus 로고    scopus 로고
    • The novel fibronectin-binding motif and key residues of mycobacteria
    • Naito, M., Ohara, N., Matsumoto, S.& Yamada, T. The novel fibronectin-binding motif and key residues of mycobacteria. J. Biol. Chem. 273,2905 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 2905
    • Naito, M.1    Ohara, N.2    Matsumoto, S.3    Yamada, T.4
  • 25
    • 0024585104 scopus 로고
    • Effect of zinc deficiency on the appearance of two immunodominant protein antigens (32 kDa and 65 kDa) in culture filtrates of mycobacteria
    • De Bruyn, J., Bosmans, R., Nyabenda, J.& Van Vooren, J.P. Effect of zinc deficiency on the appearance of two immunodominant protein antigens (32 kDa and 65 kDa) in culture filtrates of mycobacteria. J. Gen. 135,79-84 (1989).
    • (1989) J. Gen. , vol.135 , pp. 79-84
    • De Bruyn, J.1    Bosmans, R.2    Nyabenda, J.3    Van Vooren, J.P.4
  • 26
    • 0013823748 scopus 로고
    • Extracellular proteins of tubercle bacilli. IV. Alpha and beta antigens as major extracellular protein products and as cellular components of a strain (H37Rv) of
    • Fukui, Y.. Hirai, T., Uchida, T.& Yoneda, M. Extracellular proteins of tubercle bacilli. IV. Alpha and beta antigens as major extracellular protein products and as cellular components of a strain (H37Rv) of Mycobacterium tuberculosis. Biken 7.8,189-199(1965).
    • (1965) Mycobacterium Tuberculosis. Biken , vol.7-8 , pp. 189-199
    • Fukui, Y.1    Hirai, T.2    Uchida, T.3    Yoneda, M.4
  • 30
    • 0023892078 scopus 로고
    • Characteristics and specificity of acquired immunologie memory to Mycobacterium tuberculosis infection
    • Orme, I.M. Characteristics and specificity of acquired immunologie memory to Mycobacterium tuberculosis infection. J. Immunol. 140, 3589-3593 (1988).
    • (1988) J. Immunol. , vol.140 , pp. 3589-3593
    • Orme, I.M.1
  • 31
    • 0031753529 scopus 로고    scopus 로고
    • Delineation of human antibody responses to culture filtrate antigens of Mycobacterium tuberculosis
    • Samanich, K.M. et si. Delineation of human antibody responses to culture filtrate antigens of Mycobacterium tuberculosis. J. Infect. Dis. 178, 1534-1538 (1998).
    • (1998) J. Infect. Dis. , vol.178 , pp. 1534-1538
    • Samanich, K.M.1
  • 32
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z.& Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 27, 307-326 (1997).
    • (1997) Methods Enzymol. , vol.27 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 33
    • 0028103275 scopus 로고
    • CCP4 Suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4. CCP4 Suite: programs for protein crystallography. Acta Crystallogr. D 50,760-763 (1994).
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 35
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography& NMR system (version 0.9): A new software suite for macromolecular structure determination
    • Brünger, A.T. et al. Crystallography& NMR system (version 0.9): a new software suite for macromolecular structure determination. Acts Crystallogr. D 54, 905-921 (1998).
    • (1998) Acts Crystallogr. D , vol.54 , pp. 905-921
    • Brünger, A.T.1
  • 36
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy atom parameter refinement for the multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • de La Fortelle, E.& Bricogne, G. Maximum-likelihood heavy atom parameter refinement for the multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol. 276,472-494 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 472-494
    • De La Fortelle, E.1    Bricogne, G.2
  • 37
    • 0002473587 scopus 로고    scopus 로고
    • Phase combination and cross validation in iterated density-modification calculations
    • Cowtan, K.D. & P. Main, P. Phase combination and cross validation in iterated density-modification calculations. Acta Crystallogr. D 52,43-48 (1996).
    • (1996) Acta Crystallogr. D , vol.52 , pp. 43-48
    • Cowtan, K.D.1    Pmain, P.2
  • 38
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.Y., Cowan, S.W.& Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47,110-119 (1991).
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 39
    • 84920325457 scopus 로고
    • AMoRe: An Automated Package for Molecular Replacement
    • Navaza, J. AMoRe: an Automated Package for Molecular Replacement. Acta Crystallogr. A 50,157-163 (1994).
    • (1994) Acta Crystallogr. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 40
    • 0027609916 scopus 로고
    • Setor: Hardware lighted three-dimensional solid model representations of macromolecules
    • Evans, S.V. Setor: hardware lighted three-dimensional solid model representations of macromolecules. J. Mol. Graph. 11,134-138(1993).
    • (1993) J. Mol. Graph. , vol.11 , pp. 134-138
    • Evans, S.V.1
  • 41
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex, N.& Peitsch, M.C. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18,2714-2723 (1997).
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 44
    • 0026605537 scopus 로고
    • CLUSTAL V: Improved software for multiple sequence alignment
    • Higgins, D.G., Bleasby, A.J.& Fuchs, R. CLUSTAL V: improved software for multiple sequence alignment. Comput. Applic. Biosci. 8,189-191 (1992).
    • (1992) Comput. Applic. Biosci. , vol.8 , pp. 189-191
    • Higgins, D.G.1    Bleasby, A.J.2    Fuchs, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.