메뉴 건너뛰기




Volumn 43, Issue 5-6, 2007, Pages 249-254

Expression analysis of proteases of Mycobacterium leprae in human skin lesions

Author keywords

Expression; Leprosy; Lesion; Mycobacterium leprae; Proteases; RT PCR

Indexed keywords

BACTERIAL ENZYME; HYPERIMMUNE GLOBULIN; PROTEINASE;

EID: 34548653876     PISSN: 08824010     EISSN: 10961208     Source Type: Journal    
DOI: 10.1016/j.micpath.2007.05.011     Document Type: Article
Times cited : (9)

References (20)
  • 1
    • 0029879578 scopus 로고    scopus 로고
    • Pathogenic mechanisms induced by microbial proteases in microbial infections
    • Maeda H., and Yamammoto T. Pathogenic mechanisms induced by microbial proteases in microbial infections. Biol Chem Hoppe Seyler 377 (1996) 217-226
    • (1996) Biol Chem Hoppe Seyler , vol.377 , pp. 217-226
    • Maeda, H.1    Yamammoto, T.2
  • 2
    • 0028783299 scopus 로고
    • Are bacterial proteinases pathogenic factors?
    • Travis J., Potempa J., and Maeda H. Are bacterial proteinases pathogenic factors?. Trends Microbiol 3 (1995) 405-407
    • (1995) Trends Microbiol , vol.3 , pp. 405-407
    • Travis, J.1    Potempa, J.2    Maeda, H.3
  • 3
    • 0034702898 scopus 로고    scopus 로고
    • The mycosins of Mycobacterium tuberculosis H37Rv: a family of subtilisin-like serine proteases
    • Brown G.D., Dave J.A., Gey van Pittius N.C., Stevens L., Ehlers M.R.W., and Beyers A.D. The mycosins of Mycobacterium tuberculosis H37Rv: a family of subtilisin-like serine proteases. Gene 254 (2000) 147-155
    • (2000) Gene , vol.254 , pp. 147-155
    • Brown, G.D.1    Dave, J.A.2    Gey van Pittius, N.C.3    Stevens, L.4    Ehlers, M.R.W.5    Beyers, A.D.6
  • 5
    • 0035701315 scopus 로고    scopus 로고
    • The decaying genome of Mycobacterium leprae
    • Eiglmeier K., Parkhill J., Honoré N., et al. The decaying genome of Mycobacterium leprae. Lepr Rev 72 (2001) 387-398
    • (2001) Lepr Rev , vol.72 , pp. 387-398
    • Eiglmeier, K.1    Parkhill, J.2    Honoré, N.3
  • 6
    • 34548695934 scopus 로고    scopus 로고
    • Ribeiro-Guimarães ML, Pessolani MCV. Comparative genomics of mycobacterial proteases. Microb Pathog (2007), doi:10.1016/j.micpath.2007.05.010.
  • 7
    • 0026565319 scopus 로고
    • A neutral glycoprotease of Pasteurella haemolytica Al specifically cleaves O-sialoglycoproteins
    • Abdullah K.M., Udoh E.A., Shewen P.E., and Mellors A. A neutral glycoprotease of Pasteurella haemolytica Al specifically cleaves O-sialoglycoproteins. Infect Immun 60 (1992) 56-62
    • (1992) Infect Immun , vol.60 , pp. 56-62
    • Abdullah, K.M.1    Udoh, E.A.2    Shewen, P.E.3    Mellors, A.4
  • 8
    • 0029997773 scopus 로고    scopus 로고
    • Expression and functional characterisation of the clpC gene of Mycobacterium leprae: ClpC protein elicits human response antibody response
    • Misra N., Habib S., Ranjan A., Hasnain S.E., and Nath I. Expression and functional characterisation of the clpC gene of Mycobacterium leprae: ClpC protein elicits human response antibody response. Gene 172 (1996) 99-104
    • (1996) Gene , vol.172 , pp. 99-104
    • Misra, N.1    Habib, S.2    Ranjan, A.3    Hasnain, S.E.4    Nath, I.5
  • 10
    • 0033966029 scopus 로고    scopus 로고
    • Comparative evaluation of low-molecular-mass proteins from Mycobacterium tuberculosis identifies members of the ESAT-6 family as immunodominant T-cell antigens
    • Skjot R.L., Oettinger T., Rosenkrands I., Ravn P., Brock I., Jacobsen S., et al. Comparative evaluation of low-molecular-mass proteins from Mycobacterium tuberculosis identifies members of the ESAT-6 family as immunodominant T-cell antigens. Infect Immun 68 (2000) 214-220
    • (2000) Infect Immun , vol.68 , pp. 214-220
    • Skjot, R.L.1    Oettinger, T.2    Rosenkrands, I.3    Ravn, P.4    Brock, I.5    Jacobsen, S.6
  • 11
    • 14544279302 scopus 로고    scopus 로고
    • A protein secretion pathway critical for Mycobacterium tuberculosis virulence is conserved and functional in Mycobacterium smegmatis
    • Converse S.E., and Cox J.S. A protein secretion pathway critical for Mycobacterium tuberculosis virulence is conserved and functional in Mycobacterium smegmatis. J Bacteriol 187 (2005) 1238-1245
    • (2005) J Bacteriol , vol.187 , pp. 1238-1245
    • Converse, S.E.1    Cox, J.S.2
  • 12
    • 29644438456 scopus 로고    scopus 로고
    • Dissection of ESAT-6 system 1 of Mycobacterium tuberculosis and impact on immunogenicity and virulence
    • Brodin P., Majlessi L., Marsollier L., de Jonge M.I., Bottai D., Demangel C., et al. Dissection of ESAT-6 system 1 of Mycobacterium tuberculosis and impact on immunogenicity and virulence. Infect Immun 74 (2006) 88-98
    • (2006) Infect Immun , vol.74 , pp. 88-98
    • Brodin, P.1    Majlessi, L.2    Marsollier, L.3    de Jonge, M.I.4    Bottai, D.5    Demangel, C.6
  • 13
    • 0442323293 scopus 로고    scopus 로고
    • Immunological crossreactivity of the Mycobacterium leprae CFP-10 with its homologue in Mycobacterium tuberculosis
    • Geluk A., van Meijgaarden K.E., Franken K.L.M.C., Wieles B., Arend S.M., Faber W.R., et al. Immunological crossreactivity of the Mycobacterium leprae CFP-10 with its homologue in Mycobacterium tuberculosis. Scand J Immunol 59 (2004) 66-70
    • (2004) Scand J Immunol , vol.59 , pp. 66-70
    • Geluk, A.1    van Meijgaarden, K.E.2    Franken, K.L.M.C.3    Wieles, B.4    Arend, S.M.5    Faber, W.R.6
  • 14
    • 0039280024 scopus 로고    scopus 로고
    • HtrA heat shock protease interacts with phospholipid membranes and undergoes conformational changes
    • Skórko-Glonek J., Lipinska B., Krzewski K., Zolese G., Bertoli E., and Tanfani F. HtrA heat shock protease interacts with phospholipid membranes and undergoes conformational changes. J Biol Chem 272 (1997) 8974-8982
    • (1997) J Biol Chem , vol.272 , pp. 8974-8982
    • Skórko-Glonek, J.1    Lipinska, B.2    Krzewski, K.3    Zolese, G.4    Bertoli, E.5    Tanfani, F.6
  • 15
    • 34147144087 scopus 로고    scopus 로고
    • Burkholderia cenocepacia requires a periplasmic HtrA protease for growth under thermal and osmotic stress and for survival in vivo
    • Flannagan R.S., Aubert D., Kooi C., Sokol P.A., and Valvanoi M.A. Burkholderia cenocepacia requires a periplasmic HtrA protease for growth under thermal and osmotic stress and for survival in vivo. Infect Immun 75 (2007) 1679-1689
    • (2007) Infect Immun , vol.75 , pp. 1679-1689
    • Flannagan, R.S.1    Aubert, D.2    Kooi, C.3    Sokol, P.A.4    Valvanoi, M.A.5
  • 16
    • 7044235500 scopus 로고    scopus 로고
    • The protective effect of the Mycobacterium bovis BCG vaccine is increased by coadministration with the Mycobacterium tuberculosis 72-kilodalton fusion polyprotein Mtb72F in M. tuberculosis-infected Guinea Pigs
    • Brandt L., Skeiky Y.A.W., Alderson M.R., Lobet Y., Dalemans W., Turner O.C., et al. The protective effect of the Mycobacterium bovis BCG vaccine is increased by coadministration with the Mycobacterium tuberculosis 72-kilodalton fusion polyprotein Mtb72F in M. tuberculosis-infected Guinea Pigs. Infect Immun 72 (2004) 6622-6632
    • (2004) Infect Immun , vol.72 , pp. 6622-6632
    • Brandt, L.1    Skeiky, Y.A.W.2    Alderson, M.R.3    Lobet, Y.4    Dalemans, W.5    Turner, O.C.6
  • 17
    • 0032524095 scopus 로고    scopus 로고
    • Membrane protein proteolysis assayed by fluorescence quenching: assay of O-sialoglycoprotein endopeptidase
    • Jiang P., and Mellors A. Membrane protein proteolysis assayed by fluorescence quenching: assay of O-sialoglycoprotein endopeptidase. Anal Biochem 259 (1998) 8-15
    • (1998) Anal Biochem , vol.259 , pp. 8-15
    • Jiang, P.1    Mellors, A.2
  • 18
    • 24944569292 scopus 로고    scopus 로고
    • Mapping the laminin-binding and adhesive domain of the cell surface-associated Hlp/LBP protein from Mycobacterium leprae
    • Lima C.S., Zulianello L., Marques M.A., Kim H., Portugal M.I., Antunes S.L., et al. Mapping the laminin-binding and adhesive domain of the cell surface-associated Hlp/LBP protein from Mycobacterium leprae. Microbes Infect 7 (2005) 1097-1109
    • (2005) Microbes Infect , vol.7 , pp. 1097-1109
    • Lima, C.S.1    Zulianello, L.2    Marques, M.A.3    Kim, H.4    Portugal, M.I.5    Antunes, S.L.6
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications
    • Towbin H., Staehelin T., and Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA 76 (1979) 4350-4354
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.