메뉴 건너뛰기




Volumn 7, Issue 1, 1996, Pages 33-38

Expression and purification of anthrax toxin protective antigen from Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

ANTHRAX; BACILLUS ANTHRACIS; BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; MAMMALIA;

EID: 0030087551     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.1996.0005     Document Type: Article
Times cited : (30)

References (24)
  • 2
    • 0020681139 scopus 로고
    • Evidence for plasmid mediated toxin production in Bacillus anthracis
    • 2. Mikesell, O. P., Ivins, B. E., Ristroph, J. D., and Dreier, T. M. (1983) Evidence for plasmid mediated toxin production in Bacillus anthracis. Infect. Immun. 39, 371-376.
    • (1983) Infect. Immun. , vol.39 , pp. 371-376
    • Mikesell, O.P.1    Ivins, B.E.2    Ristroph, J.D.3    Dreier, T.M.4
  • 3
    • 0022891493 scopus 로고
    • Macrophages are sensitive to anthrax lethal toxin through an acid dependent process
    • 3. Friedlander, A. M. (1986) Macrophages are sensitive to anthrax lethal toxin through an acid dependent process. J. Biol. Chem. 261, 7123-7126.
    • (1986) J. Biol. Chem. , vol.261 , pp. 7123-7126
    • Friedlander, A.M.1
  • 4
    • 73049164375 scopus 로고
    • Purification of factor I and recognition of a third factor of anthrax toxin
    • 4. Stanley, J. L., and Smith, H. (1961) Purification of factor I and recognition of a third factor of anthrax toxin. J. Gen. Microbiol. 26, 49-66.
    • (1961) J. Gen. Microbiol. , vol.26 , pp. 49-66
    • Stanley, J.L.1    Smith, H.2
  • 5
    • 0000947082 scopus 로고
    • Anthrax toxin edema factor: A bacterial adenylate cyclase that increases cyclic AMP concentration of eukaryotic cells
    • 5. Leppla, S. H. (1982) Anthrax toxin edema factor: A bacterial adenylate cyclase that increases cyclic AMP concentration of eukaryotic cells. Proc. Natl. Acad. Sci. USA 79, 3162-3166.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 3162-3166
    • Leppla, S.H.1
  • 6
    • 0028172211 scopus 로고
    • The chymotrypsin sensitive site FFD (315), in anthrax toxin PA is required for translocation of lethal factor
    • 6. Singh, Y., Klimpel, K. R., Arora, N., Sharma, M., and Leppla, S. H. (1994) The chymotrypsin sensitive site FFD (315), in anthrax toxin PA is required for translocation of lethal factor. J. Biol. Chem. 269, 29039-29046.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29039-29046
    • Singh, Y.1    Klimpel, K.R.2    Arora, N.3    Sharma, M.4    Leppla, S.H.5
  • 7
    • 0028088404 scopus 로고
    • Anthrax toxin lethal factor contains a zinc metalloprotease consensus sequence which is required for lethal toxin activity
    • 7. Klimpel, K. R., Arora, N., and Leppla, S. H. (1994) Anthrax toxin lethal factor contains a zinc metalloprotease consensus sequence which is required for lethal toxin activity. Mol. Microbiol. 13, 1093-1100.
    • (1994) Mol. Microbiol. , vol.13 , pp. 1093-1100
    • Klimpel, K.R.1    Arora, N.2    Leppla, S.H.3
  • 8
    • 0027097608 scopus 로고
    • Biochemical and physiological changes induced by anthrax lethal toxin in J774 macrophages like cells
    • 8. Hanna, P. C., Kochi, S., and Collier, R. J. (1992) Biochemical and physiological changes induced by anthrax lethal toxin in J774 macrophages like cells. Mol. Biol. Cell. 3, 1269-1277.
    • (1992) Mol. Biol. Cell. , vol.3 , pp. 1269-1277
    • Hanna, P.C.1    Kochi, S.2    Collier, R.J.3
  • 9
    • 0021205725 scopus 로고
    • Anthrax: The disease in relation to vaccines
    • 9. Hambleton, P., Carman, J. A., and Melling, J. (1984) Anthrax: The disease in relation to vaccines. Vaccine 2, 125-132.
    • (1984) Vaccine , vol.2 , pp. 125-132
    • Hambleton, P.1    Carman, J.A.2    Melling, J.3
  • 10
    • 0023924122 scopus 로고
    • Recent advances in the development of an improved human anthrax vaccine
    • 10. Ivins, B. E., and Welkos, S. L. (1987) Recent advances in the development of an improved human anthrax vaccine. Eur. J. Epidemiol. 4, 12-19.
    • (1987) Eur. J. Epidemiol. , vol.4 , pp. 12-19
    • Ivins, B.E.1    Welkos, S.L.2
  • 11
    • 0023758535 scopus 로고
    • Sequence and analysis of the DNA encoding protective antigen of Bacillus anthracis
    • 11. Welkos, S. L., Lowe, J. R. Eden-McCutchan, F., Vodkin, M., Leppla, S. H., and Schmidt, J. J. (1988) Sequence and analysis of the DNA encoding protective antigen of Bacillus anthracis. Gene 69, 287-300.
    • (1988) Gene , vol.69 , pp. 287-300
    • Welkos, S.L.1    Lowe, J.R.2    Eden-McCutchan, F.3    Vodkin, M.4    Leppla, S.H.5    Schmidt, J.J.6
  • 12
    • 0023022205 scopus 로고
    • Cloning and expression of the Bacillus anthracis protective antigen gene in Bacillus subtilis
    • 12. Ivins, B. E., and Welkos, S. H. (1986) Cloning and expression of the Bacillus anthracis protective antigen gene in Bacillus subtilis. Infect. Immun. 54, 537-542.
    • (1986) Infect. Immun. , vol.54 , pp. 537-542
    • Ivins, B.E.1    Welkos, S.H.2
  • 13
    • 0020826341 scopus 로고
    • Cloning of the protective antigen gene of Bacillus anthracis
    • 13. Vodkin, M. H., and Leppla, S. H. (1983) Cloning of the protective antigen gene of Bacillus anthracis. Cell 34, 693-697.
    • (1983) Cell , vol.34 , pp. 693-697
    • Vodkin, M.H.1    Leppla, S.H.2
  • 14
    • 0025095447 scopus 로고
    • Expression of the Bacillus anthracis protective antigen gene by baculovirus and vaccinia virus recombinants
    • 14. Iacono-Connors, L. C., Schmaljohn, C. S., and Dalrymple, J. M. (1990) Expression of the Bacillus anthracis protective antigen gene by baculovirus and vaccinia virus recombinants. Infect. Immun. 58, 366-372.
    • (1990) Infect. Immun. , vol.58 , pp. 366-372
    • Iacono-Connors, L.C.1    Schmaljohn, C.S.2    Dalrymple, J.M.3
  • 15
    • 0024837128 scopus 로고
    • A deleted variant of Bacillus anthracis protective antigen is non-toxic and blocks anthrax toxin action invivo
    • 15. Singh, Y., Chaudhary, V. K., and Leppla, S. H. (1989) A deleted variant of Bacillus anthracis protective antigen is non-toxic and blocks anthrax toxin action invivo. J. Biol. Chem. 264, 19103-19107.
    • (1989) J. Biol. Chem. , vol.264 , pp. 19103-19107
    • Singh, Y.1    Chaudhary, V.K.2    Leppla, S.H.3
  • 16
    • 0020554080 scopus 로고
    • Mechanisms of protein localization
    • 16. Silhavy, T. J., Benson, S. A., and Emr, S. D. (1983) Mechanisms of protein localization. Microbiol. Rev. 47, 313-344.
    • (1983) Microbiol. Rev. , vol.47 , pp. 313-344
    • Silhavy, T.J.1    Benson, S.A.2    Emr, S.D.3
  • 17
    • 0018884457 scopus 로고
    • Secretion and membrane localization of proteins in Escherichia coli
    • 17. Inovye, M., and Halegoua, S. (1979) Secretion and membrane localization of proteins in Escherichia coli. CRC Crit. Rev. Biochem. 7, 339-371.
    • (1979) CRC Crit. Rev. Biochem. , vol.7 , pp. 339-371
    • Inovye, M.1    Halegoua, S.2
  • 18
    • 0025858389 scopus 로고
    • The carboxyl-terminal end of protective antigen is required for receptor binding and anthrax toxin activity
    • 18. Singh, Y., Klimpel, K. R., Quinn, C. P., Chaudhary, V. K., and Leppla, S. H. (1991) The carboxyl-terminal end of protective antigen is required for receptor binding and anthrax toxin activity. J. Biol. Chem. 266, 15493-15497.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15493-15497
    • Singh, Y.1    Klimpel, K.R.2    Quinn, C.P.3    Chaudhary, V.K.4    Leppla, S.H.5
  • 19
    • 1842340098 scopus 로고
    • Cytotoxic activity of a recombinant fusion protein between interleukin 4 and pseudomonas exotoxin
    • 19. Ogata, M., Chaudhary, V. K., FitzGerald, D. J., and Pastan, I. (1989) Cytotoxic activity of a recombinant fusion protein between interleukin 4 and Pseudomonas exotoxin. Proc. Natl. Acad. Sci. USA 86, 4215-4219.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 4215-4219
    • Ogata, M.1    Chaudhary, V.K.2    FitzGerald, D.J.3    Pastan, I.4
  • 20
    • 0001403642 scopus 로고
    • A colorimetric method for the assay of soluble succinic dehydrogenase and pyridine nucleotide-linked dehydrogenases
    • 20. Ells, A. H. (1959) A colorimetric method for the assay of soluble succinic dehydrogenase and pyridine nucleotide-linked dehydrogenases. Arch. Biochem. Biophys. 85, 561-562.
    • (1959) Arch. Biochem. Biophys. , vol.85 , pp. 561-562
    • Ells, A.H.1
  • 21
    • 0001049825 scopus 로고
    • Micro-iodometric assay of penicillinase
    • 21. Novick, R. P. (1962) Micro-iodometric assay of penicillinase. Biochem. J. 83, 236-240.
    • (1962) Biochem. J. , vol.83 , pp. 236-240
    • Novick, R.P.1
  • 23
    • 0024214705 scopus 로고
    • Production and purification of anthrax toxin
    • Harshman, S., Ed., Academic Press, San Diego
    • 23. Leppla,S. H. (1988) Production and purification of anthrax toxin, in "Methods in Enzymology" (Harshman, S., Ed.), Vol. 165, pp. 103-116, Academic Press, San Diego.
    • (1988) Methods in Enzymology , vol.165 , pp. 103-116
    • Leppla, S.H.1
  • 24
    • 0023911589 scopus 로고
    • Purification of anthrax toxin components by high performance anion-exchange, gel filtration and hydrophobic-interaction chromatography
    • 24. Quinn, C. P., Shone, C. C., Turnbull, P. C. B., and Melling, J. (1988) Purification of anthrax toxin components by high performance anion-exchange, gel filtration and hydrophobic-interaction chromatography. Biochem. J. 252, 753-758.
    • (1988) Biochem. J. , vol.252 , pp. 753-758
    • Quinn, C.P.1    Shone, C.C.2    Turnbull, P.C.B.3    Melling, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.