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Volumn 177, Issue 1, 2006, Pages 422-429

Mycobacterium tuberculosis LprA is a lipoprotein agonist of TLR2 that regulates innate immunity and APC function

Author keywords

[No Author keywords available]

Indexed keywords

B7 ANTIGEN; BACTERIAL PROTEIN; CD40 ANTIGEN; GAMMA INTERFERON; HISTIDINE; INTERLEUKIN 10; INTERLEUKIN 12; LIPOPROTEIN; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2; PROTEIN LPQH; PROTEIN LPRA; PROTEIN LPRG; TOLL LIKE RECEPTOR 2; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG;

EID: 33745298718     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: 10.4049/jimmunol.177.1.422     Document Type: Article
Times cited : (181)

References (56)
  • 2
    • 0034443265 scopus 로고    scopus 로고
    • Maturation of human dendritic cells by cell wall skeleton of Mycobacterium bovis bacillus Calmette-Guerin: Involvement of Toll-like receptors
    • Tsuji, S., M. Matsumoto, O. Takeuchi, S. Akira, I. Azuma, A. Hayashi, K. Toyoshima, and T. Seya. 2000. Maturation of human dendritic cells by cell wall skeleton of Mycobacterium bovis bacillus Calmette-Guerin: involvement of Toll-like receptors. Infect. Immun. 68: 6883-6890.
    • (2000) Infect. Immun. , vol.68 , pp. 6883-6890
    • Tsuji, S.1    Matsumoto, M.2    Takeuchi, O.3    Akira, S.4    Azuma, I.5    Hayashi, A.6    Toyoshima, K.7    Seya, T.8
  • 4
    • 0035865232 scopus 로고    scopus 로고
    • Microbial lipopeptides stimulate dendritic cell maturation via Toll-like receptor 2
    • Hertz, C., S. Kiertscher, P. Godowski, D. Bouis, M. Norgard, M. Roth, and R. Modlin. 2001. Microbial lipopeptides stimulate dendritic cell maturation via Toll-like receptor 2. J. Immunol. 166: 2444-2450.
    • (2001) J. Immunol. , vol.166 , pp. 2444-2450
    • Hertz, C.1    Kiertscher, S.2    Godowski, P.3    Bouis, D.4    Norgard, M.5    Roth, M.6    Modlin, R.7
  • 5
    • 0033215123 scopus 로고    scopus 로고
    • Human Toll-like receptors mediate cellular activation by Mycobacterium tuberculosis
    • Means, T. K., S. Wang, E. Lien, A. Yoshimura, D. T. Golenbock, and M. J. Fenton. 1999. Human Toll-like receptors mediate cellular activation by Mycobacterium tuberculosis. J. Immunol. 163: 3920-3927.
    • (1999) J. Immunol. , vol.163 , pp. 3920-3927
    • Means, T.K.1    Wang, S.2    Lien, E.3    Yoshimura, A.4    Golenbock, D.T.5    Fenton, M.J.6
  • 6
    • 0033458799 scopus 로고    scopus 로고
    • Toll-like receptor-2 mediates mycobacteria-induced proinflammatory signaling in macrophages
    • Underbill, D. M., A. Ozinsky, K. D. Smith, and A. Aderem. 1999. Toll-like receptor-2 mediates mycobacteria-induced proinflammatory signaling in macrophages. Proc. Natl. Acad. Sci. USA 96: 14459-14463.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14459-14463
    • Underbill, D.M.1    Ozinsky, A.2    Smith, K.D.3    Aderem, A.4
  • 7
    • 0742272507 scopus 로고    scopus 로고
    • The role of Toll-like receptors in combating mycobacteria
    • Krutzik, S. R., and R. L. Modlin. 2004. The role of Toll-like receptors in combating mycobacteria. Semin. Immunol 16: 35-41.
    • (2004) Semin. Immunol , vol.16 , pp. 35-41
    • Krutzik, S.R.1    Modlin, R.L.2
  • 9
    • 0142179315 scopus 로고    scopus 로고
    • Mice lacking myeloid differentiation factor 88 display profound defects in host resistance and immune responses to Mycobacterium avium infection not exhibited by Toll-like receptor 2 (TLR2)- and TLR4-deficient animals
    • Feng, C. G., C. A. Scanga, C. M. Collazo-Custodio, A. W. Cheever, S. Hieny, P. Caspar, and A. Sher. 2003. Mice lacking myeloid differentiation factor 88 display profound defects in host resistance and immune responses to Mycobacterium avium infection not exhibited by Toll-like receptor 2 (TLR2)- and TLR4-deficient animals. J. Immunol. 171: 4758-4764.
    • (2003) J. Immunol. , vol.171 , pp. 4758-4764
    • Feng, C.G.1    Scanga, C.A.2    Collazo-Custodio, C.M.3    Cheever, A.W.4    Hieny, S.5    Caspar, P.6    Sher, A.7
  • 10
    • 14044253038 scopus 로고    scopus 로고
    • Fatal Mycobacterium tuberculosis infection despite adaptive immune response in the absence of MyD88
    • Fremond, C. M., V. Yeremeev, D. M. Nicolle, M. Jacobs, V. F. Quesniaux, and B. Ryffel. 2004. Fatal Mycobacterium tuberculosis infection despite adaptive immune response in the absence of MyD88. J. Clin. Invest. 114: 1790-1799.
    • (2004) J. Clin. Invest. , vol.114 , pp. 1790-1799
    • Fremond, C.M.1    Yeremeev, V.2    Nicolle, D.M.3    Jacobs, M.4    Quesniaux, V.F.5    Ryffel, B.6
  • 12
    • 1842588021 scopus 로고    scopus 로고
    • MyD88-deficient mice display a profound loss in resistance to Mycobacterium tuberculosis associated with partially impaired Th1 cytokine and nitric oxide synthase 2 expression
    • Scanga, C. A., A. Bafica, C. G. Feng, A. W. Cheever, S. Hieny, and A. Sher. 2004. MyD88-deficient mice display a profound loss in resistance to Mycobacterium tuberculosis associated with partially impaired Th1 cytokine and nitric oxide synthase 2 expression. Infect. Immun. 72: 2400-2404.
    • (2004) Infect. Immun. , vol.72 , pp. 2400-2404
    • Scanga, C.A.1    Bafica, A.2    Feng, C.G.3    Cheever, A.W.4    Hieny, S.5    Sher, A.6
  • 15
    • 0037378655 scopus 로고    scopus 로고
    • Cutting edge: A Toll-like receptor 2 polymorphism that is associated with lepromatous leprosy is unable to mediate mycobacterial signaling
    • Bochud, P. Y., T. R. Hawn, and A. Aderem. 2003. Cutting edge: a Toll-like receptor 2 polymorphism that is associated with lepromatous leprosy is unable to mediate mycobacterial signaling. J. Immunol. 170: 3451-3454.
    • (2003) J. Immunol. , vol.170 , pp. 3451-3454
    • Bochud, P.Y.1    Hawn, T.R.2    Aderem, A.3
  • 17
    • 0036784614 scopus 로고    scopus 로고
    • Cutting edge: Toll-like receptor (TLR)2- and TLR4-mediated pathogen recognition in resistance to airborne infection with Mycobacterium tuberculosis
    • Reiling, N., C. Holscher, A. Fehrenbach, S. Kroger, C. J. Kirschning, S. Goyert, and S. Ehlers. 2002. Cutting edge: Toll-like receptor (TLR)2- and TLR4-mediated pathogen recognition in resistance to airborne infection with Mycobacterium tuberculosis. J. Immunol. 169: 3480-3484.
    • (2002) J. Immunol. , vol.169 , pp. 3480-3484
    • Reiling, N.1    Holscher, C.2    Fehrenbach, A.3    Kroger, S.4    Kirschning, C.J.5    Goyert, S.6    Ehlers, S.7
  • 19
    • 1642375617 scopus 로고    scopus 로고
    • Toll-like receptor 2 (TLR2)-dependent-positive and TLR2-independent- negative regulation of proinflammatory cytokines by mycobacterial lipomannans
    • Quesniaux, V. J., D. M. Nicolle, D. Torres, L. Kremer, Y. Guerardel, J. Nigou, G. Puzo, F. Erard, and B. Ryffel. 2004. Toll-like receptor 2 (TLR2)-dependent-positive and TLR2-independent-negative regulation of proinflammatory cytokines by mycobacterial lipomannans. J. Immunol. 172: 4425-4434.
    • (2004) J. Immunol. , vol.172 , pp. 4425-4434
    • Quesniaux, V.J.1    Nicolle, D.M.2    Torres, D.3    Kremer, L.4    Guerardel, Y.5    Nigou, J.6    Puzo, G.7    Erard, F.8    Ryffel, B.9
  • 21
    • 0043032571 scopus 로고    scopus 로고
    • Acylation state of the phosphatidyl inositol hexamannosides from Mycobacterium bovis BCG and Mycobacterium tuberculosis H37Rv and its implication in TLR response
    • Gilleron, M., V. F. Quesniaux, and G. Puzo. 2003. Acylation state of the phosphatidyl inositol hexamannosides from Mycobacterium bovis BCG and Mycobacterium tuberculosis H37Rv and its implication in TLR response. J. Biol. Chem. 278: 29880-29889.
    • (2003) J. Biol. Chem. , vol.278 , pp. 29880-29889
    • Gilleron, M.1    Quesniaux, V.F.2    Puzo, G.3
  • 22
    • 0035879108 scopus 로고    scopus 로고
    • Toll-like receptor 2-dependent inhibition of macrophage class II MHC expression and antigen processing by 19 kD lipoprotein of Mycobacterium tuberculosis
    • Noss, E. H., R. K. Pai, T. J. Sellati, J. D. Radolf, J. Belisle, D. T. Golenbock, W. H. Boom, and C. V. Harding. 2001. Toll-like receptor 2-dependent inhibition of macrophage class II MHC expression and antigen processing by 19 kD lipoprotein of Mycobacterium tuberculosis. J. Immunol. 167: 910-918.
    • (2001) J. Immunol. , vol.167 , pp. 910-918
    • Noss, E.H.1    Pai, R.K.2    Sellati, T.J.3    Radolf, J.D.4    Belisle, J.5    Golenbock, D.T.6    Boom, W.H.7    Harding, C.V.8
  • 23
    • 0037530648 scopus 로고    scopus 로고
    • Inhibition of IFN-γ-induced class II transactivator expression by a 19-kDa lipoprotein from Mycobacterium tuberculosis: A potential mechanism for immune evasion
    • Pai, R. K., M. Convery, T. A. Hamilton, W. H. Boom, and C. V. Harding. 2003. Inhibition of IFN-γ-induced class II transactivator expression by a 19-kDa lipoprotein from Mycobacterium tuberculosis: a potential mechanism for immune evasion. J. Immunol. 171: 175-184.
    • (2003) J. Immunol. , vol.171 , pp. 175-184
    • Pai, R.K.1    Convery, M.2    Hamilton, T.A.3    Boom, W.H.4    Harding, C.V.5
  • 25
    • 4043072746 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis LprG (Rv1411c): A novel TLR-2 ligand that inhibits human macrophage class II MHC antigen processing
    • Gehring, A. J., K. M. Dobos, J. T. Belisle, C. V. Harding, and W. H. Boom. 2004. Mycobacterium tuberculosis LprG (Rv1411c): a novel TLR-2 ligand that inhibits human macrophage class II MHC antigen processing. J. Immunol. 173: 2660-2668.
    • (2004) J. Immunol. , vol.173 , pp. 2660-2668
    • Gehring, A.J.1    Dobos, K.M.2    Belisle, J.T.3    Harding, C.V.4    Boom, W.H.5
  • 26
    • 0028067877 scopus 로고
    • Lipid modification of bacterial prolipoprotein: Transfer of diacylglyceryl moiety from phosphatidylglycerol
    • Sankaran, K., and H. C. Wu. 1994. Lipid modification of bacterial prolipoprotein: transfer of diacylglyceryl moiety from phosphatidylglycerol. J. Biol. Chem. 269: 19701-19706.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19701-19706
    • Sankaran, K.1    Wu, H.C.2
  • 28
    • 0020322927 scopus 로고
    • Mechanism of signal peptide cleavage in the biosynthesis of the major lipoprotein of the Escherichia coli outer membrane
    • Hussain, M., S. Ichihara, and S. Mizushima. 1982. Mechanism of signal peptide cleavage in the biosynthesis of the major lipoprotein of the Escherichia coli outer membrane. J. Biol. Chem. 257: 5177-5182.
    • (1982) J. Biol. Chem. , vol.257 , pp. 5177-5182
    • Hussain, M.1    Ichihara, S.2    Mizushima, S.3
  • 29
    • 7944226058 scopus 로고    scopus 로고
    • Lipoproteins of Mycobacterium tuberculosis: An abundant and functionally diverse class of cell envelope components
    • Sutcliffe, I. C., and D. J. Harrington. 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
  • 30
    • 4644257442 scopus 로고    scopus 로고
    • Lipoproteins, not lipopolysaccharide, are the key mediators of the proinflammatory response elicited by heat-killed Brucella abortus
    • Giambartolomei, G. H., A. Zwerdling, J. Cassataro, L. Bruno, C. A. Fossati, and M. T. Philipp. 2004. Lipoproteins, not lipopolysaccharide, are the key mediators of the proinflammatory response elicited by heat-killed Brucella abortus. J. Immunol. 173: 4635-4642.
    • (2004) J. Immunol. , vol.173 , pp. 4635-4642
    • Giambartolomei, G.H.1    Zwerdling, A.2    Cassataro, J.3    Bruno, L.4    Fossati, C.A.5    Philipp, M.T.6
  • 31
    • 0037090077 scopus 로고    scopus 로고
    • Two lipoproteins extracted from Escherichia coli K-12 LCD25 lipopolysaccharide are the major components responsible for Toll-like receptor 2-mediated signaling
    • Lee, H. K., J. Lee, and P. S. Tobias. 2002. Two lipoproteins extracted from Escherichia coli K-12 LCD25 lipopolysaccharide are the major components responsible for Toll-like receptor 2-mediated signaling. J. Immunol. 168: 4012-4017.
    • (2002) J. Immunol. , vol.168 , pp. 4012-4017
    • Lee, H.K.1    Lee, J.2    Tobias, P.S.3
  • 32
    • 0036918723 scopus 로고    scopus 로고
    • Differential recognition of structural details of bacterial lipopeptides by Toll-like receptors
    • Morr, M., O. Takeuchi, S. Akira, M. M. Simon, and P. F. Muhlradt. 2002. Differential recognition of structural details of bacterial lipopeptides by Toll-like receptors. Eur. J. Immunol. 32: 3337-3347.
    • (2002) Eur. J. Immunol. , vol.32 , pp. 3337-3347
    • Morr, M.1    Takeuchi, O.2    Akira, S.3    Simon, M.M.4    Muhlradt, P.F.5
  • 34
    • 0034650420 scopus 로고    scopus 로고
    • Cutting edge: Preferentially the R-stereoisomer of the mycoplasmal lipopeptide macrophage-activating lipopeptide-2 activates immune cells through a Toll-like receptor 2- and MyD88-dependent signaling pathway
    • Takeuchi, O., A. Kaufmann, K. Grote, T. Kawai, K. Hoshino, M. Morr, P. F. Muhlradt, and S. Akira. 2000. Cutting edge: preferentially the R-stereoisomer of the mycoplasmal lipopeptide macrophage-activating lipopeptide-2 activates immune cells through a Toll-like receptor 2- and MyD88-dependent signaling pathway. J. Immunol. 164: 554-557.
    • (2000) J. Immunol. , vol.164 , pp. 554-557
    • Takeuchi, O.1    Kaufmann, A.2    Grote, K.3    Kawai, T.4    Hoshino, K.5    Morr, M.6    Muhlradt, P.F.7    Akira, S.8
  • 36
    • 4344662389 scopus 로고    scopus 로고
    • Role of the polypeptide region of a 33 kDa mycobacterial lipoprotein for efficient IL-12 production
    • Yamashita, Y., Y. Maeda, F. Takeshita, P. J. Brennan, and M. Makino. 2004. Role of the polypeptide region of a 33 kDa mycobacterial lipoprotein for efficient IL-12 production. Cell. Immunol. 229: 13-20.
    • (2004) Cell. Immunol. , vol.229 , pp. 13-20
    • Yamashita, Y.1    Maeda, Y.2    Takeshita, F.3    Brennan, P.J.4    Makino, M.5
  • 38
    • 2942590448 scopus 로고    scopus 로고
    • Synthetic lipopeptide adjuvants and Toll-like receptor 2-structure-activity relationships
    • Spohn, R., U. Buwitt-Beckmann, R. Brock, G. Jung, A. J. Ulmer, and K. H. Wiesmuller. 2004. Synthetic lipopeptide adjuvants and Toll-like receptor 2-structure-activity relationships. Vaccine 22: 2494-2499.
    • (2004) Vaccine , vol.22 , pp. 2494-2499
    • Spohn, R.1    Buwitt-Beckmann, U.2    Brock, R.3    Jung, G.4    Ulmer, A.J.5    Wiesmuller, K.H.6
  • 39
    • 0029896457 scopus 로고    scopus 로고
    • Bacterial glycoproteins: A link between glycosylation and proteolytic cleavage of a 19 kDa antigen from Mycobacterium tuberculosis
    • Herrmann, J. L., P. O'Gaora, A. Gallagher, J. E. Thole, and D. B. Young. 1996. Bacterial glycoproteins: a link between glycosylation and proteolytic cleavage of a 19 kDa antigen from Mycobacterium tuberculosis. EMBO J. 15: 3547-3554.
    • (1996) EMBO J. , vol.15 , pp. 3547-3554
    • Herrmann, J.L.1    O'Gaora, P.2    Gallagher, A.3    Thole, J.E.4    Young, D.B.5
  • 40
    • 0345059167 scopus 로고    scopus 로고
    • Sweet new world: Glycoproteins in bacterial pathogens
    • Schmidt, M. A., L. W. Riley, and I. Benz. 2003. Sweet new world: glycoproteins in bacterial pathogens. Trends Microbiol. 11: 554-561.
    • (2003) Trends Microbiol. , vol.11 , pp. 554-561
    • Schmidt, M.A.1    Riley, L.W.2    Benz, I.3
  • 41
    • 0042635767 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis exerts gene-selective inhibition of transcriptional responses to IFN-γ, without inhibiting STAT1 function
    • Kincaid, E. Z., and J. D. Ernst. 2003. Mycobacterium tuberculosis exerts gene-selective inhibition of transcriptional responses to IFN-γ, without inhibiting STAT1 function. J. Immunol. 171: 2042-2049.
    • (2003) J. Immunol. , vol.171 , pp. 2042-2049
    • Kincaid, E.Z.1    Ernst, J.D.2
  • 42
    • 7044222877 scopus 로고    scopus 로고
    • Prolonged Toll-like receptor signaling by Mycobacterium tuberculosis and its 19-kilodalton lipoprotein inhibits γ interferon-induced regulation of selected genes in macrophages
    • Pai, R. K., M. E. Pennini, A. A. Tobian, D. H. Canaday, W. H. Boom, and C. V. Harding. 2004. Prolonged Toll-like receptor signaling by Mycobacterium tuberculosis and its 19-kilodalton lipoprotein inhibits γ interferon-induced regulation of selected genes in macrophages. Infect. Immun. 72: 6603-6614.
    • (2004) Infect. Immun. , vol.72 , pp. 6603-6614
    • Pai, R.K.1    Pennini, M.E.2    Tobian, A.A.3    Canaday, D.H.4    Boom, W.H.5    Harding, C.V.6
  • 43
    • 0042766347 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis 19-kilodalton lipoprotein inhibits γ interferon-regulated HLA-DR and FcγR1 on human macrophages through Toll-like receptor 2
    • Gehring, A. J., R. E. Rojas, D. H. Canaday, D. L. Lakey, C. V. Harding, and W. H. Boom. 2003. The Mycobacterium tuberculosis 19-kilodalton lipoprotein inhibits γ interferon-regulated HLA-DR and FcγR1 on human macrophages through Toll-like receptor 2. Infect. Immun. 71: 4487-4497.
    • (2003) Infect. Immun. , vol.71 , pp. 4487-4497
    • Gehring, A.J.1    Rojas, R.E.2    Canaday, D.H.3    Lakey, D.L.4    Harding, C.V.5    Boom, W.H.6
  • 44
    • 1842484130 scopus 로고    scopus 로고
    • Inhibition of major histocompatibility complex II expression and antigen processing in murine alveolar macrophages by Mycobacterium bovis BCG and the 19-kilodalton mycobacterial lipoprotein
    • Fulton, S. A., S. M. Reba, R. K. Pai, M. Pennini, M. Torres, C. V. Harding, and W. H. Boom. 2004. Inhibition of major histocompatibility complex II expression and antigen processing in murine alveolar macrophages by Mycobacterium bovis BCG and the 19-kilodalton mycobacterial lipoprotein. Infect. Immun. 72: 2101-2110.
    • (2004) Infect. Immun. , vol.72 , pp. 2101-2110
    • Fulton, S.A.1    Reba, S.M.2    Pai, R.K.3    Pennini, M.4    Torres, M.5    Harding, C.V.6    Boom, W.H.7
  • 45
    • 17844362500 scopus 로고    scopus 로고
    • Mycobacteria inhibition of IFN-γ induced HLA-DR gene expression by up-regulating histone deacetylation at the promoter region in human THP-1 monocytic cells
    • Wang, Y., H. M. Curry, B. S. Zwilling, and W. P. Lafuse. 2005. Mycobacteria inhibition of IFN-γ induced HLA-DR gene expression by up-regulating histone deacetylation at the promoter region in human THP-1 monocytic cells. J. Immunol. 174: 5687-5694.
    • (2005) J. Immunol. , vol.174 , pp. 5687-5694
    • Wang, Y.1    Curry, H.M.2    Zwilling, B.S.3    Lafuse, W.P.4
  • 47
    • 0037033073 scopus 로고    scopus 로고
    • Lipopolysaccharide rapidly traffics to and from the Golgi apparatus with the Toll-like receptor 4-MD-2-CD14 complex in a process that is distinct from the initiation of signal transduction
    • Latz, E., A. Visintin, E. Lien, K. A. Fitzgerald, B. G. Monks, E. A. Kurt-Jones, D. T. Golenbock, and T. Espevik. 2002. Lipopolysaccharide rapidly traffics to and from the Golgi apparatus with the Toll-like receptor 4-MD-2-CD14 complex in a process that is distinct from the initiation of signal transduction. J. Biol. Chem. 277: 47834-47843.
    • (2002) J. Biol. Chem. , vol.277 , pp. 47834-47843
    • Latz, E.1    Visintin, A.2    Lien, E.3    Fitzgerald, K.A.4    Monks, B.G.5    Kurt-Jones, E.A.6    Golenbock, D.T.7    Espevik, T.8
  • 48
    • 0022340655 scopus 로고
    • Transformation of mouse bone marrow cells by transfection with a human oncogene related to c-myc is associated with the endogenous production of macrophage colony stimulating factor 1
    • Sklar, M. D., A. Tereba, B. D. Chen, and W. S. Walker. 1985. Transformation of mouse bone marrow cells by transfection with a human oncogene related to c-myc is associated with the endogenous production of macrophage colony stimulating factor 1. J. Cell. Physiol. 125: 403-412.
    • (1985) J. Cell. Physiol. , vol.125 , pp. 403-412
    • Sklar, M.D.1    Tereba, A.2    Chen, B.D.3    Walker, W.S.4
  • 49
    • 0033970577 scopus 로고    scopus 로고
    • Enhanced production of recombinant Mycobacterium tuberculosis antigens in Escherichia coli by replacement of low-usage codons
    • Lakey, D. L., R. K. Voladri, K. M. Edwards, C. Hager, B. Samten, R. S. Wallis, P. F. Barnes, and D. S. Kemodle. 2000. Enhanced production of recombinant Mycobacterium tuberculosis antigens in Escherichia coli by replacement of low-usage codons. Infect. Immun. 68: 233-238.
    • (2000) Infect. Immun. , vol.68 , pp. 233-238
    • Lakey, D.L.1    Voladri, R.K.2    Edwards, K.M.3    Hager, C.4    Samten, B.5    Wallis, R.S.6    Barnes, P.F.7    Kemodle, D.S.8
  • 50
    • 0030959144 scopus 로고    scopus 로고
    • High-level heterologous expression and secretion in rapidly growing nonpathogenic mycobacteria of four major Mycobacterium tuberculosis extracellular proteins considered to be leading vaccine candidates and drug targets
    • Harth, G., B. Y. Lee, and M. A. Horwitz. 1997. High-level heterologous expression and secretion in rapidly growing nonpathogenic mycobacteria of four major Mycobacterium tuberculosis extracellular proteins considered to be leading vaccine candidates and drug targets. Infect. Immun. 65: 2321-2328.
    • (1997) Infect. Immun. , vol.65 , pp. 2321-2328
    • Harth, G.1    Lee, B.Y.2    Horwitz, M.A.3
  • 51
    • 0027514448 scopus 로고
    • Expression of the Mycobacterium tuberculosis 19-kilodalton antigen in Mycobacterium smegmatis: Immunological analysis and evidence of glycosylation
    • Garbe, T., D. Harris, M. Vordermeier, R. Lathigra, J. Ivanyi, and D. Young. 1993. Expression of the Mycobacterium tuberculosis 19-kilodalton antigen in Mycobacterium smegmatis: immunological analysis and evidence of glycosylation. Infect. Immun. 61: 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
  • 52
    • 23244440497 scopus 로고    scopus 로고
    • Export-mediated assembly of mycobacterial glycoproteins parallels eukaryotic pathways
    • VanderVen, B. C., J. D. Harder, D. C. Crick, and J. T. Belisle. 2005. Export-mediated assembly of mycobacterial glycoproteins parallels eukaryotic pathways. Science 309: 941-943.
    • (2005) Science , vol.309 , pp. 941-943
    • Vanderven, B.C.1    Harder, J.D.2    Crick, D.C.3    Belisle, J.T.4
  • 54
    • 2342430991 scopus 로고    scopus 로고
    • Molecular mechanisms of endotoxin tolerance
    • Fan, H., and J. A. Cook. 2004. Molecular mechanisms of endotoxin tolerance. J. Endotoxin Res. 10: 71-84.
    • (2004) J. Endotoxin Res. , vol.10 , pp. 71-84
    • Fan, H.1    Cook, J.A.2
  • 55
    • 2942721674 scopus 로고    scopus 로고
    • ST2 is an inhibitor of interleukin 1 receptor and Toll-like receptor 4 signaling and maintains endotoxin tolerance
    • Brint, E. K., D. Xu, H. Liu, A. Dunne, A. N. McKenzie, L. A. O'Neill, and F. Y. Liew. 2004. ST2 is an inhibitor of interleukin 1 receptor and Toll-like receptor 4 signaling and maintains endotoxin tolerance. Nat. Immunol. 5: 373-379.
    • (2004) Nat. Immunol. , vol.5 , pp. 373-379
    • Brint, E.K.1    Xu, D.2    Liu, H.3    Dunne, A.4    McKenzie, A.N.5    O'Neill, L.A.6    Liew, F.Y.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.