메뉴 건너뛰기




Volumn 278, Issue 18, 2011, Pages 3277-3286

Matrix metalloproteinase proteolysis of the mycobacterial HSP65 protein as a potential source of immunogenic peptides in human tuberculosis

Author keywords

HSP65; MMP; Mycobacterium; proteolysis; tuberculosis

Indexed keywords

CHAPERONE; GELATINASE A; GELATINASE B; GLYCOSYLPHOSPHATIDYLINOSITOL; HEAT SHOCK PROTEIN 65; MATRIX METALLOPROTEINASE; MATRIX METALLOPROTEINASE 14; MATRIX METALLOPROTEINASE 15; MATRIX METALLOPROTEINASE 16; MATRIX METALLOPROTEINASE 17; MATRIX METALLOPROTEINASE 24; MATRIX METALLOPROTEINASE 25; NEUTROPHIL COLLAGENASE; UNCLASSIFIED DRUG;

EID: 80052461153     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2011.08244.x     Document Type: Article
Times cited : (11)

References (40)
  • 1
    • 79951899229 scopus 로고    scopus 로고
    • For better or for worse: The immune response against Mycobacterium tuberculosis balances pathology and protection
    • Dorhoi A, Reece ST, &, Kaufmann SH, (2011) For better or for worse: the immune response against Mycobacterium tuberculosis balances pathology and protection. Immunol Rev 240, 235-251.
    • (2011) Immunol Rev , vol.240 , pp. 235-251
    • Dorhoi, A.1    Reece, S.T.2    Kaufmann, S.H.3
  • 2
    • 45849103095 scopus 로고    scopus 로고
    • Insights into early mycobacterial pathogenesis from the zebrafish
    • Lesley R, &, Ramakrishnan L, (2008) Insights into early mycobacterial pathogenesis from the zebrafish. Curr Opin Microbiol 11, 277-283.
    • (2008) Curr Opin Microbiol , vol.11 , pp. 277-283
    • Lesley, R.1    Ramakrishnan, L.2
  • 3
    • 79955111092 scopus 로고    scopus 로고
    • Macrophages and control of granulomatous inflammation in tuberculosis
    • Flynn JL, Chan J, &, Lin PL, (2011) Macrophages and control of granulomatous inflammation in tuberculosis. Mucosal Immunol 4, 271-278.
    • (2011) Mucosal Immunol , vol.4 , pp. 271-278
    • Flynn, J.L.1    Chan, J.2    Lin, P.L.3
  • 5
    • 75649141266 scopus 로고    scopus 로고
    • Tuberculous granuloma induction via interaction of a bacterial secreted protein with host epithelium
    • Volkman HE, Pozos TC, Zheng J, Davis JM, Rawls JF, &, Ramakrishnan L, (2010) Tuberculous granuloma induction via interaction of a bacterial secreted protein with host epithelium. Science 327, 466-469.
    • (2010) Science , vol.327 , pp. 466-469
    • Volkman, H.E.1    Pozos, T.C.2    Zheng, J.3    Davis, J.M.4    Rawls, J.F.5    Ramakrishnan, L.6
  • 7
    • 33846186853 scopus 로고    scopus 로고
    • Monocyte-astrocyte networks regulate matrix metalloproteinase gene expression and secretion in central nervous system tuberculosis in vitro and in vivo
    • Harris JE, Nuttall RK, Elkington PT, Green JA, Horncastle DE, Graeber MB, Edwards DR, &, Friedland JS, (2007) Monocyte-astrocyte networks regulate matrix metalloproteinase gene expression and secretion in central nervous system tuberculosis in vitro and in vivo. J Immunol 178, 1199-1207.
    • (2007) J Immunol , vol.178 , pp. 1199-1207
    • Harris, J.E.1    Nuttall, R.K.2    Elkington, P.T.3    Green, J.A.4    Horncastle, D.E.5    Graeber, M.B.6    Edwards, D.R.7    Friedland, J.S.8
  • 8
    • 0242410826 scopus 로고    scopus 로고
    • Unopposed matrix metalloproteinase-9 expression in human tuberculous granuloma and the role of TNF-alpha-dependent monocyte networks
    • Price NM, Gilman RH, Uddin J, Recavarren S, &, Friedland JS, (2003) Unopposed matrix metalloproteinase-9 expression in human tuberculous granuloma and the role of TNF-alpha-dependent monocyte networks. J Immunol 171, 5579-5586.
    • (2003) J Immunol , vol.171 , pp. 5579-5586
    • Price, N.M.1    Gilman, R.H.2    Uddin, J.3    Recavarren, S.4    Friedland, J.S.5
  • 12
    • 0036512208 scopus 로고    scopus 로고
    • New functions for the matrix metalloproteinases in cancer progression
    • Egeblad M, &, Werb Z, (2002) New functions for the matrix metalloproteinases in cancer progression. Nat Rev Cancer 2, 161-174.
    • (2002) Nat Rev Cancer , vol.2 , pp. 161-174
    • Egeblad, M.1    Werb, Z.2
  • 13
    • 77149164774 scopus 로고    scopus 로고
    • Matrix metalloproteinases: What do they not do? New substrates and biological roles identified by murine models and proteomics
    • Rodriguez D, Morrison CJ, &, Overall CM, (2010) Matrix metalloproteinases: what do they not do? New substrates and biological roles identified by murine models and proteomics Biochim Biophys Acta 1803, 39-54.
    • (2010) Biochim Biophys Acta , vol.1803 , pp. 39-54
    • Rodriguez, D.1    Morrison, C.J.2    Overall, C.M.3
  • 14
  • 15
    • 77049113770 scopus 로고    scopus 로고
    • The tissue inhibitors of metalloproteinases (TIMPs): An ancient family with structural and functional diversity
    • Brew K, &, Nagase H, (2010) The tissue inhibitors of metalloproteinases (TIMPs): an ancient family with structural and functional diversity. Biochim Biophys Acta 1803, 55-71.
    • (2010) Biochim Biophys Acta , vol.1803 , pp. 55-71
    • Brew, K.1    Nagase, H.2
  • 16
    • 9244227956 scopus 로고    scopus 로고
    • Crystal structure of the 65-kilodalton heat shock protein, chaperonin 60.2, of Mycobacterium tuberculosis
    • Qamra R, &, Mande SC, (2004) Crystal structure of the 65-kilodalton heat shock protein, chaperonin 60.2, of Mycobacterium tuberculosis. J Bacteriol 186, 8105-8113.
    • (2004) J Bacteriol , vol.186 , pp. 8105-8113
    • Qamra, R.1    Mande, S.C.2
  • 17
    • 0035183063 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis chaperonin 60.1 is a more potent cytokine stimulator than chaperonin 60.2 (Hsp 65) and contains a CD14-binding domain
    • Lewthwaite JC, Coates AR, Tormay P, Singh M, Mascagni P, Poole S, Roberts M, Sharp L, &, Henderson B, (2001) Mycobacterium tuberculosis chaperonin 60.1 is a more potent cytokine stimulator than chaperonin 60.2 (Hsp 65) and contains a CD14-binding domain. Infect Immun 69, 7349-7355.
    • (2001) Infect Immun , vol.69 , pp. 7349-7355
    • Lewthwaite, J.C.1    Coates, A.R.2    Tormay, P.3    Singh, M.4    Mascagni, P.5    Poole, S.6    Roberts, M.7    Sharp, L.8    Henderson, B.9
  • 19
    • 77953405498 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis upregulates microglial matrix metalloproteinase-1 and -3 expression and secretion via NF-kappaB- and Activator Protein-1-dependent monocyte networks
    • et al.
    • Green JA, Elkington PT, Pennington CJ, Roncaroli F, Dholakia S, Moores RC, Bullen A, Porter JC, Agranoff D, Edwards DR, et al. (2010) Mycobacterium tuberculosis upregulates microglial matrix metalloproteinase-1 and -3 expression and secretion via NF-kappaB- and Activator Protein-1-dependent monocyte networks. J Immunol 184, 6492-6503.
    • (2010) J Immunol , vol.184 , pp. 6492-6503
    • Green, J.A.1    Elkington, P.T.2    Pennington, C.J.3    Roncaroli, F.4    Dholakia, S.5    Moores, R.C.6    Bullen, A.7    Porter, J.C.8    Agranoff, D.9    Edwards, D.R.10
  • 20
    • 66949171433 scopus 로고    scopus 로고
    • Matrix metalloproteinase-1 is regulated in tuberculosis by a p38 MAPK-dependent, p-aminosalicylic acid-sensitive signaling cascade
    • Rand L, Green JA, Saraiva L, Friedland JS, &, Elkington PT, (2009) Matrix metalloproteinase-1 is regulated in tuberculosis by a p38 MAPK-dependent, p-aminosalicylic acid-sensitive signaling cascade. J Immunol 182, 5865-5872.
    • (2009) J Immunol , vol.182 , pp. 5865-5872
    • Rand, L.1    Green, J.A.2    Saraiva, L.3    Friedland, J.S.4    Elkington, P.T.5
  • 21
    • 43049084341 scopus 로고    scopus 로고
    • MT4-(MMP17) and MT6-MMP (MMP25), a unique set of membrane-anchored matrix metalloproteinases: Properties and expression in cancer
    • Sohail A, Sun Q, Zhao H, Bernardo MM, Cho JA, &, Fridman R, (2008) MT4-(MMP17) and MT6-MMP (MMP25), a unique set of membrane-anchored matrix metalloproteinases: properties and expression in cancer. Cancer Metastasis Rev 27, 289-302.
    • (2008) Cancer Metastasis Rev , vol.27 , pp. 289-302
    • Sohail, A.1    Sun, Q.2    Zhao, H.3    Bernardo, M.M.4    Cho, J.A.5    Fridman, R.6
  • 22
    • 77957021680 scopus 로고    scopus 로고
    • High throughput substrate phage display for protease profiling
    • Ratnikov B, Cieplak P, &, Smith JW, (2009) High throughput substrate phage display for protease profiling. Methods Mol Biol 539, 93-114.
    • (2009) Methods Mol Biol , vol.539 , pp. 93-114
    • Ratnikov, B.1    Cieplak, P.2    Smith, J.W.3
  • 24
    • 64049085808 scopus 로고    scopus 로고
    • Matrix metalloproteinase proteolysis of the myelin basic protein isoforms is a source of immunogenic peptides in autoimmune multiple sclerosis
    • Shiryaev SA, Savinov AY, Cieplak P, Ratnikov BI, Motamedchaboki K, Smith JW, &, Strongin AY, (2009) Matrix metalloproteinase proteolysis of the myelin basic protein isoforms is a source of immunogenic peptides in autoimmune multiple sclerosis. PLoS ONE 4, e4952.
    • (2009) PLoS ONE , vol.4
    • Shiryaev, S.A.1    Savinov, A.Y.2    Cieplak, P.3    Ratnikov, B.I.4    Motamedchaboki, K.5    Smith, J.W.6    Strongin, A.Y.7
  • 27
    • 0029923793 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis invades and replicates within type II alveolar cells
    • Bermudez LE, &, Goodman J, (1996) Mycobacterium tuberculosis invades and replicates within type II alveolar cells. Infect Immun 64, 1400-1406.
    • (1996) Infect Immun , vol.64 , pp. 1400-1406
    • Bermudez, L.E.1    Goodman, J.2
  • 28
    • 67651215965 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis Cpn60.2 and DnaK are located on the bacterial surface, where Cpn60.2 facilitates efficient bacterial association with macrophages
    • Hickey TB, Thorson LM, Speert DP, Daffe M, &, Stokes RW, (2009) Mycobacterium tuberculosis Cpn60.2 and DnaK are located on the bacterial surface, where Cpn60.2 facilitates efficient bacterial association with macrophages. Infect Immun 77, 3389-3401.
    • (2009) Infect Immun , vol.77 , pp. 3389-3401
    • Hickey, T.B.1    Thorson, L.M.2    Speert, D.P.3    Daffe, M.4    Stokes, R.W.5
  • 30
    • 0032734065 scopus 로고    scopus 로고
    • Identification of promiscuous epitopes from the Mycobacterial 65-kilodalton heat shock protein recognized by human CD4(+) T cells of the Mycobacterium leprae memory repertoire
    • Mustafa AS, Lundin KE, Meloen RH, Shinnick TM, &, Oftung F, (1999) Identification of promiscuous epitopes from the Mycobacterial 65-kilodalton heat shock protein recognized by human CD4(+) T cells of the Mycobacterium leprae memory repertoire. Infect Immun 67, 5683-5689.
    • (1999) Infect Immun , vol.67 , pp. 5683-5689
    • Mustafa, A.S.1    Lundin, K.E.2    Meloen, R.H.3    Shinnick, T.M.4    Oftung, F.5
  • 31
    • 0036431514 scopus 로고    scopus 로고
    • Identification of an I-Ad restricted peptide on the 65-kilodalton heat shock protein of Mycobacterium avium
    • Nagabhushanam V, Purcell AW, Mannering S, Germano S, Praszkier J, &, Cheers C, (2002) Identification of an I-Ad restricted peptide on the 65-kilodalton heat shock protein of Mycobacterium avium. Immunol Cell Biol 80, 574-583.
    • (2002) Immunol Cell Biol , vol.80 , pp. 574-583
    • Nagabhushanam, V.1    Purcell, A.W.2    Mannering, S.3    Germano, S.4    Praszkier, J.5    Cheers, C.6
  • 33
    • 79955101596 scopus 로고    scopus 로고
    • Initiation and regulation of T-cell responses in tuberculosis
    • Urdahl KB, Shafiani S, &, Ernst JD, (2011) Initiation and regulation of T-cell responses in tuberculosis. Mucosal Immunol 4, 288-293.
    • (2011) Mucosal Immunol , vol.4 , pp. 288-293
    • Urdahl, K.B.1    Shafiani, S.2    Ernst, J.D.3
  • 35
    • 0037189494 scopus 로고    scopus 로고
    • A unique substrate binding mode discriminates membrane type-1 matrix metalloproteinase from other matrix metalloproteinases
    • Kridel SJ, Sawai H, Ratnikov BI, Chen EI, Li W, Godzik A, Strongin AY, &, Smith JW, (2002) A unique substrate binding mode discriminates membrane type-1 matrix metalloproteinase from other matrix metalloproteinases. J Biol Chem 277, 23788-23793.
    • (2002) J Biol Chem , vol.277 , pp. 23788-23793
    • Kridel, S.J.1    Sawai, H.2    Ratnikov, B.I.3    Chen, E.I.4    Li, W.5    Godzik, A.6    Strongin, A.Y.7    Smith, J.W.8
  • 36
    • 0038269103 scopus 로고    scopus 로고
    • A residue in the S2 subsite controls substrate selectivity of matrix metalloproteinase-2 and matrix metalloproteinase-9
    • Chen EI, Li W, Godzik A, Howard EW, &, Smith JW, (2003) A residue in the S2 subsite controls substrate selectivity of matrix metalloproteinase-2 and matrix metalloproteinase-9. J Biol Chem 278, 17158-17163.
    • (2003) J Biol Chem , vol.278 , pp. 17158-17163
    • Chen, E.I.1    Li, W.2    Godzik, A.3    Howard, E.W.4    Smith, J.W.5
  • 37
    • 33646584823 scopus 로고    scopus 로고
    • Recent advances in MMP inhibitor design
    • Fisher JF, &, Mobashery S, (2006) Recent advances in MMP inhibitor design. Cancer Metastasis Rev 25, 115-136.
    • (2006) Cancer Metastasis Rev , vol.25 , pp. 115-136
    • Fisher, J.F.1    Mobashery, S.2
  • 38
    • 0029026723 scopus 로고
    • Active-site titration of peptidases
    • Knight CG, (1995) Active-site titration of peptidases. Methods Enzymol 248, 85-101.
    • (1995) Methods Enzymol , vol.248 , pp. 85-101
    • Knight, C.G.1
  • 39
    • 0034663597 scopus 로고    scopus 로고
    • Application of multiple sequence alignment profiles to improve protein secondary structure prediction
    • Cuff JA, &, Barton GJ, (2000) Application of multiple sequence alignment profiles to improve protein secondary structure prediction. Proteins 40, 502-511.
    • (2000) Proteins , vol.40 , pp. 502-511
    • Cuff, J.A.1    Barton, G.J.2
  • 40
    • 1542358787 scopus 로고    scopus 로고
    • Prediction and functional analysis of native disorder in proteins from the three kingdoms of life
    • Ward JJ, Sodhi JS, McGuffin LJ, Buxton BF, &, Jones DT, (2004) Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. J Mol Biol 337, 635-645.
    • (2004) J Mol Biol , vol.337 , pp. 635-645
    • Ward, J.J.1    Sodhi, J.S.2    McGuffin, L.J.3    Buxton, B.F.4    Jones, D.T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.