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Volumn 142, Issue 6, 1996, Pages 1375-1383

A major T-cell-inducing cytosolic 23 kDa protein antigen of the vaccine candidate Mycobacterium habana is superoxide dismutase

Author keywords

23 kDa protein; Mycobacterium habana; Superoxide dismutase; T cell response; Vaccine

Indexed keywords

AMMONIUM SULFATE; MYCOBACTERIUM ANTIGEN; MYCOBACTERIUM VACCINE; SCHIFF BASE; SUPEROXIDE DISMUTASE;

EID: 0029946790     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/13500872-142-6-1375     Document Type: Article
Times cited : (14)

References (51)
  • 1
    • 0027998549 scopus 로고
    • Effects of temperature stress on expression of fimbriae and superoxide dismutase by Porphyromonas gingivalis
    • Amano, A., Sharma, A., Sojar, H. T., Kutramitsu, H. K. & Genco, R. J. (1994). Effects of temperature stress on expression of fimbriae and superoxide dismutase by Porphyromonas gingivalis. Inject Immun 62, 4682-4685.
    • (1994) Inject Immun , vol.62 , pp. 4682-4685
    • Amano, A.1    Sharma, A.2    Sojar, H.T.3    Kutramitsu, H.K.4    Genco, R.J.5
  • 3
    • 0021158356 scopus 로고
    • The role of oxygen and its derivatives in microbial pathogenesis and host defense
    • Beaman, L. & Beaman, B. L. (1984). The role of oxygen and its derivatives in microbial pathogenesis and host defense. Annu Rev Microbiol 38, 27-48.
    • (1984) Annu Rev Microbiol , vol.38 , pp. 27-48
    • Beaman, L.1    Beaman, B.L.2
  • 4
    • 0020685136 scopus 로고
    • Purification and properties of a unique superoxide dismutase from Nocardia asteroides
    • Beaman, B. L., Scates, S. M., Moring, S. E., Deen, R. & Misra, H. P. (1982). Purification and properties of a unique superoxide dismutase from Nocardia asteroides. J Biol Chem 258, 91-96.
    • (1982) J Biol Chem , vol.258 , pp. 91-96
    • Beaman, B.L.1    Scates, S.M.2    Moring, S.E.3    Deen, R.4    Misra, H.P.5
  • 5
    • 0015153416 scopus 로고
    • Superoxide dismutase: Improved assays and an assay applicable to acrylamide gels
    • Beauchamp, C. & Fridovieh, I. (1971). Superoxide dismutase: improved assays and an assay applicable to acrylamide gels. Anal Biochem 44, 276-287.
    • (1971) Anal Biochem , vol.44 , pp. 276-287
    • Beauchamp, C.1    Fridovieh, I.2
  • 6
    • 0014385564 scopus 로고
    • Isolation of mononuclear cells and granulocytes from human blood
    • Boyum, A. (1968). Isolation of mononuclear cells and granulocytes from human blood. Scand J Clin Lab Invest (Suppl) 21, 77-89.
    • (1968) Scand J Clin Lab Invest (Suppl) , vol.21 , pp. 77-89
    • Boyum, A.1
  • 7
    • 0018370835 scopus 로고
    • Properties of energy transducing system in different types of membrane preparations from Mycobacterium phlei - Preparation, resolution and reconstitution
    • Brodie, A. F., Kalra, V. K., Lee, S. H. & Cohen, N. S. (1979). Properties of energy transducing system in different types of membrane preparations from Mycobacterium phlei - preparation, resolution and reconstitution. Methods Enzymol 55, 175-199.
    • (1979) Methods Enzymol , vol.55 , pp. 175-199
    • Brodie, A.F.1    Kalra, V.K.2    Lee, S.H.3    Cohen, N.S.4
  • 9
    • 0028932184 scopus 로고
    • X-ray structure analysis of the iron dependent superoxide dismutase from Mycobacterium tuberculosis at 2.0 Å resolution reveals novel dimer-dimer interactions
    • Cooper, J. B., McIntyre, K., Badasso, M. O., Wood, S. P., Zhang, Y., Garbe, T. R. & Young, D. (1995). X-ray structure analysis of the iron dependent superoxide dismutase from Mycobacterium tuberculosis at 2.0 Å resolution reveals novel dimer-dimer interactions. J Mol Biol 246, 531-544.
    • (1995) J Mol Biol , vol.246 , pp. 531-544
    • Cooper, J.B.1    McIntyre, K.2    Badasso, M.O.3    Wood, S.P.4    Zhang, Y.5    Garbe, T.R.6    Young, D.7
  • 10
    • 0029154710 scopus 로고
    • Evidence for glycosylation sites on the 45 kDa glycoprotein of Mycobacterium tuberculosis
    • Dobos, K. M., Sniderek, K., Khoo, K.-H., Brennan, P. J. & Belisle, J. T. (1995). Evidence for glycosylation sites on the 45 kDa glycoprotein of Mycobacterium tuberculosis. Infect Immun 63, 2846-2853.
    • (1995) Infect Immun , vol.63 , pp. 2846-2853
    • Dobos, K.M.1    Sniderek, K.2    Khoo, K.-H.3    Brennan, P.J.4    Belisle, J.T.5
  • 11
    • 0025234334 scopus 로고
    • Protein analysis using high-resolution two-dimensional polyacrylamide gel electrophoresis
    • Dunbar, B. S., Kimura, H. & Timmons, T. M. (1990). Protein analysis using high-resolution two-dimensional polyacrylamide gel electrophoresis. Methods Enzymol 182, 441-459.
    • (1990) Methods Enzymol , vol.182 , pp. 441-459
    • Dunbar, B.S.1    Kimura, H.2    Timmons, T.M.3
  • 12
    • 0028900798 scopus 로고
    • Antigenic and structural similarities between Mycobacterium tuberculosis 50- to 55-kilodalton and M. bovis BCG 45- to 47-kilodalton antigens
    • Espitia, C., Espinosa, R., Saavedra, R., Mancilla, R., Romain, F., Laqueyrerie, A. & Moreno, C. (1995). Antigenic and structural similarities between Mycobacterium tuberculosis 50- to 55-kilodalton and M. bovis BCG 45- to 47-kilodalton antigens. Infect Immun 63, 580-584.
    • (1995) Infect Immun , vol.63 , pp. 580-584
    • Espitia, C.1    Espinosa, R.2    Saavedra, R.3    Mancilla, R.4    Romain, F.5    Laqueyrerie, A.6    Moreno, C.7
  • 13
    • 0025715617 scopus 로고
    • Modern vaccines: Mycobacterial diseases
    • Fine, P. E. M. & Rodriguez, L. C. (1990). Modern vaccines: mycobacterial diseases. Lancet 335, 1016-1020.
    • (1990) Lancet , vol.335 , pp. 1016-1020
    • Fine, P.E.M.1    Rodriguez, L.C.2
  • 14
    • 0022480378 scopus 로고
    • Superoxide dismutases
    • Fridovich, I. (1986). Superoxide dismutases. Adv Enzymol 58, 61-97.
    • (1986) Adv Enzymol , vol.58 , pp. 61-97
    • Fridovich, I.1
  • 15
    • 0028070015 scopus 로고
    • Vaccination with pure Mycobacterium leprae protein inhibits M. leprae multiplication in mouse foot pads
    • Gelber, R. H., Mehra, V., Bloom, B., Murray, L. P., Siu, P., Tsang, M. & Brennan, P. J. (1994). Vaccination with pure Mycobacterium leprae protein inhibits M. leprae multiplication in mouse foot pads. Infect Immun 62, 4250-4255.
    • (1994) Infect Immun , vol.62 , pp. 4250-4255
    • Gelber, R.H.1    Mehra, V.2    Bloom, B.3    Murray, L.P.4    Siu, P.5    Tsang, M.6    Brennan, P.J.7
  • 16
    • 0028038426 scopus 로고
    • MHC-dependent antigen processing and peptide presentation: Providing ligands for T lymphocyte activation
    • Germain, R. N. (1994). MHC-dependent antigen processing and peptide presentation: providing ligands for T lymphocyte activation. Cell 76, 287-299.
    • (1994) Cell , vol.76 , pp. 287-299
    • Germain, R.N.1
  • 17
    • 0018609529 scopus 로고
    • Mycobacterium habana, a new immunogenic strain in experimental tuberculosis
    • Gupta, H. P., Singh, N. B., Mathur, I. S. & Gupta, S. K. (1979). Mycobacterium habana, a new immunogenic strain in experimental tuberculosis. Indian J Exp Biol 17, 1190-1193.
    • (1979) Indian J Exp Biol , vol.17 , pp. 1190-1193
    • Gupta, H.P.1    Singh, N.B.2    Mathur, I.S.3    Gupta, S.K.4
  • 19
    • 0018969994 scopus 로고
    • Some sulfhydryl properties and primary structure of human erythrocyte superoxide dismutase
    • Jabusch, J. R., Forb, D. L., Kerschensteiner, D. A. & Deutsch, H. F. (1980). Some sulfhydryl properties and primary structure of human erythrocyte superoxide dismutase. Biochemistry 19, 2310-2319.
    • (1980) Biochemistry , vol.19 , pp. 2310-2319
    • Jabusch, J.R.1    Forb, D.L.2    Kerschensteiner, D.A.3    Deutsch, H.F.4
  • 20
    • 0015821893 scopus 로고
    • A rapid method for isolation of functional thymus derived murine lymphocytes
    • Julius, M., Simpson, E. & Herzenberg, L. (1973). A rapid method for isolation of functional thymus derived murine lymphocytes. Eur J Immunol 3, 645-649.
    • (1973) Eur J Immunol , vol.3 , pp. 645-649
    • Julius, M.1    Simpson, E.2    Herzenberg, L.3
  • 21
    • 0024424736 scopus 로고
    • Identification of Mycobacterium leprae antigens in tissues of leprosy patients using monoclonal antibodies
    • Khanolkar, S. R., Mackenzie, C. D., Lucas, S. B., Hussen, A., Girdhar, B. K., Katoch, K. & McAdam, K. P. W. J. (1989). Identification of Mycobacterium leprae antigens in tissues of leprosy patients using monoclonal antibodies. Int J Lepr 57, 652-658.
    • (1989) Int J Lepr , vol.57 , pp. 652-658
    • Khanolkar, S.R.1    Mackenzie, C.D.2    Lucas, S.B.3    Hussen, A.4    Girdhar, B.K.5    Katoch, K.6    McAdam, K.P.W.J.7
  • 22
    • 0026759679 scopus 로고
    • Results of the third immunology of leprosy/immunology of tuberculosis antimycobacterial monoclonal antibody workshop
    • Khanolkar-Young, S. & Workshop Participants. (1992). Results of the third immunology of leprosy/immunology of tuberculosis antimycobacterial monoclonal antibody workshop. Infect Immun 60, 3925-3927.
    • (1992) Infect Immun , vol.60 , pp. 3925-3927
    • Khanolkar-Young, S.1
  • 23
    • 0017058080 scopus 로고
    • Superoxide dismutase from Mycobacterium tuberculosis
    • Kusunose, E., Ichihara, K., Noda, Y. & Kusunose, M. (1976). Superoxide dismutase from Mycobacterium tuberculosis. J Biochem 80, 1343-1352.
    • (1976) J Biochem , vol.80 , pp. 1343-1352
    • Kusunose, E.1    Ichihara, K.2    Noda, Y.3    Kusunose, M.4
  • 24
    • 0019366310 scopus 로고
    • Superoxide dismutase in cell free extracts from Mycobacterium leprae grown in armadillo liver
    • Kusunose, E., Kusunose, M., Ichihara, K. & Izumi, S. (1981). Superoxide dismutase in cell free extracts from Mycobacterium leprae grown in armadillo liver. FEMS Microbiol Lett 10, 49-52.
    • (1981) FEMS Microbiol Lett , vol.10 , pp. 49-52
    • Kusunose, E.1    Kusunose, M.2    Ichihara, K.3    Izumi, S.4
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 26
    • 0025285296 scopus 로고
    • The specific 18 kilodalton antigen of Mycobacteriurn leprae is present in Mycobacterium habana and functions as a heat-shock protein
    • Lamb, F. I., Singh, N. B. & Colston, M. J. (1990). The specific 18 kilodalton antigen of Mycobacteriurn leprae is present in Mycobacterium habana and functions as a heat-shock protein. J Immunol 144, 1922-1925.
    • (1990) J Immunol , vol.144 , pp. 1922-1925
    • Lamb, F.I.1    Singh, N.B.2    Colston, M.J.3
  • 27
    • 0019320450 scopus 로고
    • Behavior of glycoproteins with empirical molecular weight estimation methods. I. in sodium dodecyl sulfate
    • Leach, B. S., Collawn, J. F., Jr & Fish, W. W. (1980). Behavior of glycoproteins with empirical molecular weight estimation methods. I. In sodium dodecyl sulfate. Biochemistry 19, 5734-5741.
    • (1980) Biochemistry , vol.19 , pp. 5734-5741
    • Leach, B.S.1    Collawn Jr., J.F.2    Fish, W.W.3
  • 28
    • 0018178434 scopus 로고
    • A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples
    • Markwell, M. A. K., Haas, S. M., Bieber, L. L. & Tolbert, N. E. (1978). A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples. Anal Biochem 87, 206-210.
    • (1978) Anal Biochem , vol.87 , pp. 206-210
    • Markwell, M.A.K.1    Haas, S.M.2    Bieber, L.L.3    Tolbert, N.E.4
  • 29
    • 0023664635 scopus 로고
    • Sequence from picomole quantities of protein electroblotted onto polyvinylidene difluoride membranes
    • Matsudaira, P. (1987). Sequence from picomole quantities of protein electroblotted onto polyvinylidene difluoride membranes. J Biol Chem 262, 10035-10038.
    • (1987) J Biol Chem , vol.262 , pp. 10035-10038
    • Matsudaira, P.1
  • 30
    • 0020356135 scopus 로고
    • Synthesis of either Fe or Mn superoxide dismutase with an apparently identical protein moiety by an anaerobic bacterium dependent on the metal supplied
    • Meier, B., Barra, D., Bossa, F., Calabrese, L. & Rotilio, G. (1982). Synthesis of either Fe or Mn superoxide dismutase with an apparently identical protein moiety by an anaerobic bacterium dependent on the metal supplied. J Biol Chem 257, 13977-13980.
    • (1982) J Biol Chem , vol.257 , pp. 13977-13980
    • Meier, B.1    Barra, D.2    Bossa, F.3    Calabrese, L.4    Rotilio, G.5
  • 31
    • 0025874048 scopus 로고
    • Peroxynitrite induced membrane lipid peroxidation: The cytotoxic potential of superoxide and nitric oxide
    • Radi, R., Beckman, J. S., Bush, K. M. & Freeman, B. A. (1991). Peroxynitrite induced membrane lipid peroxidation: the cytotoxic potential of superoxide and nitric oxide. Arch Biochem Biophys 288, 481-487.
    • (1991) Arch Biochem Biophys , vol.288 , pp. 481-487
    • Radi, R.1    Beckman, J.S.2    Bush, K.M.3    Freeman, B.A.4
  • 32
    • 0013931934 scopus 로고
    • Classification of leprosy according to immunity: A five group system
    • Ridley, D. S. & Jopling, W. H. (1966). Classification of leprosy according to immunity: a five group system. Int J Lepr 34, 255-273.
    • (1966) Int J Lepr , vol.34 , pp. 255-273
    • Ridley, D.S.1    Jopling, W.H.2
  • 33
    • 0003318044 scopus 로고
    • Separation by precipitation: Salting out at high salt concentration
    • New York: Springer-Verlag
    • Scopes, R. K. (1987). Separation by precipitation: salting out at high salt concentration. In Protein Purification: Principles and Practice, pp. 43-52. New York: Springer-Verlag.
    • (1987) Protein Purification: Principles and Practice , pp. 43-52
    • Scopes, R.K.1
  • 34
    • 0024551907 scopus 로고
    • Vaccination of mice against Mycobacterium leprae infection
    • Singh, N. B., Lowe, A. C. R. E., Rees, R. J. W. & Colston, M. J. (1989). Vaccination of mice against Mycobacterium leprae infection. Infect Immun 57, 653-655.
    • (1989) Infect Immun , vol.57 , pp. 653-655
    • Singh, N.B.1    Lowe, A.C.R.E.2    Rees, R.J.W.3    Colston, M.J.4
  • 35
    • 0025744291 scopus 로고
    • Induction of lepromin positivity in monkeys by a candidate antileprosy vaccine: Mycobacterium babana
    • Singh, N. B., Srivastava, A., Gupta, H. P., Ashok & Srivastava, S. (1992). Induction of lepromin positivity in monkeys by a candidate antileprosy vaccine: Mycobacterium babana. Int J Lepr 59, 317-320.
    • (1992) Int J Lepr , vol.59 , pp. 317-320
    • Singh, N.B.1    Srivastava, A.2    Gupta, H.P.3    Ashok4    Srivastava, S.5
  • 36
    • 0023190394 scopus 로고
    • Comparative study of immunizing and delayed hypersensitivity eliciting antigens of Mycobacterium leprae, M. tuberculosis, M. vaccae, and M. bovis BCG
    • Sinha, S., Sreevatsa, Gupta, S. K. & Sengupta, U. (1987). Comparative study of immunizing and delayed hypersensitivity eliciting antigens of Mycobacterium leprae, M. tuberculosis, M. vaccae, and M. bovis BCG. Int J Lepr 55, 42-53.
    • (1987) Int J Lepr , vol.55 , pp. 42-53
    • Sinha, S.1    Sreevatsa2    Gupta, S.K.3    Sengupta, U.4
  • 37
    • 0027366226 scopus 로고
    • Purification of Helicobacter pylori superoxide dismutase and cloning and sequencing of the gene
    • Spiegelhalder, C., Gerstenecker, B., Kersten, A., Schiltz, E. & Kist, M. (1993). Purification of Helicobacter pylori superoxide dismutase and cloning and sequencing of the gene. Infect Immun 61, 5315-5325.
    • (1993) Infect Immun , vol.61 , pp. 5315-5325
    • Spiegelhalder, C.1    Gerstenecker, B.2    Kersten, A.3    Schiltz, E.4    Kist, M.5
  • 38
    • 0026325332 scopus 로고
    • Unique characteristics of superoxide dismutase of a strictly anaerobic archaebacterium Methanobacterium thermoautatrophicum
    • Takao, M., Yasui, A. & Oikawa, A. (1991). Unique characteristics of superoxide dismutase of a strictly anaerobic archaebacterium Methanobacterium thermoautatrophicum. J Biol Chem 266, 14151-14154.
    • (1991) J Biol Chem , vol.266 , pp. 14151-14154
    • Takao, M.1    Yasui, A.2    Oikawa, A.3
  • 39
    • 0024415922 scopus 로고
    • Nucleotide and deduced amino acid sequence of Mycobacterium leprae manganese superoxide dismutase
    • Thangaraj, H. S., Lamb, F. I., Davis, E. O. & Colston, M. J. (1989). Nucleotide and deduced amino acid sequence of Mycobacterium leprae manganese superoxide dismutase. Nucleic Acids Res 17, 8378.
    • (1989) Nucleic Acids Res , vol.17 , pp. 8378
    • Thangaraj, H.S.1    Lamb, F.I.2    Davis, E.O.3    Colston, M.J.4
  • 40
    • 0025362029 scopus 로고
    • Identification, sequencing, and expression of Mycobacterium leprae superoxide dismutase, a major antigen
    • Thangaraj, H. S., Lamb, F. I., Davis, E. O., Jenner, P. J., Jeyakumar, L. H. & Colston, M. J. (1990). Identification, sequencing, and expression of Mycobacterium leprae superoxide dismutase, a major antigen. Infect Immun 58, 1937-1942.
    • (1990) Infect Immun , vol.58 , pp. 1937-1942
    • Thangaraj, H.S.1    Lamb, F.I.2    Davis, E.O.3    Jenner, P.J.4    Jeyakumar, L.H.5    Colston, M.J.6
  • 41
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., Staehelin, T. & Gordon, J. (1979). Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA 76, 4350-4354.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 42
    • 0026597312 scopus 로고
    • On the track of 'killer' TB
    • Weiss, R. (1992). On the track of 'killer' TB. Science 235, 148-150.
    • (1992) Science , vol.235 , pp. 148-150
    • Weiss, R.1
  • 43
    • 0019294940 scopus 로고
    • Superoxide dismutase, peroxidatic activity and catalase in Mycobacterium leprae purified from armadillo liver
    • Wheeler, P. R. & Gregory, D. (1980). Superoxide dismutase, peroxidatic activity and catalase in Mycobacterium leprae purified from armadillo liver. J Gen Microbiol 121, 457-464.
    • (1980) J Gen Microbiol , vol.121 , pp. 457-464
    • Wheeler, P.R.1    Gregory, D.2
  • 45
    • 0019882018 scopus 로고
    • Silver staining of proteins in polyacrylamide gels
    • Wray, W., Boulikas, T., Wray, V. P. & Hancock, R. (1981). Silver staining of proteins in polyacrylamide gels. Anal Biochem 118, 197-203.
    • (1981) Anal Biochem , vol.118 , pp. 197-203
    • Wray, W.1    Boulikas, T.2    Wray, V.P.3    Hancock, R.4
  • 46
    • 0027498296 scopus 로고
    • Leprosy, tuberculosis, and new genetics
    • Young, D. B. & Cole, S. T. (1993). Leprosy, tuberculosis, and new genetics. J Bacteriol 175, 1-6.
    • (1993) J Bacteriol , vol.175 , pp. 1-6
    • Young, D.B.1    Cole, S.T.2
  • 47
    • 0021813679 scopus 로고
    • Monoclonal antibodies to a 28 kD protein antigen of Mycobacterium leprae
    • Young, D. B., Fohn, M. J., Khanolkar, S. R. & Buchanan, T. M. (1985). Monoclonal antibodies to a 28 kD protein antigen of Mycobacterium leprae. Clin Exp Immunol 60, 546-562.
    • (1985) Clin Exp Immunol , vol.60 , pp. 546-562
    • Young, D.B.1    Fohn, M.J.2    Khanolkar, S.R.3    Buchanan, T.M.4
  • 50
    • 0025965210 scopus 로고
    • Genetic analysis of superoxide dismutase, the 23 kilodalton antigen of Mycobacterium tuberculosis
    • Zhang, Y., Lathigra, R., Garbe, T., Catty, D. & Young, D. (1991). Genetic analysis of superoxide dismutase, the 23 kilodalton antigen of Mycobacterium tuberculosis. Mol Microbiol 5, 381-391.
    • (1991) Mol Microbiol , vol.5 , pp. 381-391
    • Zhang, Y.1    Lathigra, R.2    Garbe, T.3    Catty, D.4    Young, D.5
  • 51
    • 0028130261 scopus 로고
    • The superoxide dismutase gene. A target for detection and identification of mycobacteria by PCR
    • Zolg, J. W. & Philippi-Schulz, S. (1994). The superoxide dismutase gene. A target for detection and identification of mycobacteria by PCR. J Clin Microbiol 32, 2801-2812.
    • (1994) J Clin Microbiol , vol.32 , pp. 2801-2812
    • Zolg, J.W.1    Philippi-Schulz, S.2


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