메뉴 건너뛰기




Volumn 50, Issue 19, 2011, Pages 3936-3945

Unfolding distinguishes the Vibrio cholerae cytolysin precursor from the mature form of the toxin

Author keywords

[No Author keywords available]

Indexed keywords

BIOPHYSICAL CHARACTERIZATION; CHEMICAL DENATURANTS; COLLOID-OSMOTIC LYSIS; CONFORMATIONAL PLASTICITY; CONFORMATIONAL PROPERTIES; CYTOLYTIC TOXIN; DENATURING CONDITIONS; EUKARYOTIC CELLS; EXTRACELLULAR SPACE; N-TERMINALS; PERIPLASM; PHYSIOLOGICAL CONDITION; TRANSMEMBRANES; VIBRIO CHOLERAE;

EID: 79955865403     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi200332g     Document Type: Article
Times cited : (15)

References (36)
  • 3
  • 5
    • 33645978129 scopus 로고    scopus 로고
    • The mechanism of pore formation by bacterial toxins
    • Tilley, S. J. and Saibil, H. R. (2006) The mechanism of pore formation by bacterial toxins Curr. Opin. Struct. Biol. 16, 230-236
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 230-236
    • Tilley, S.J.1    Saibil, H.R.2
  • 6
    • 0035822706 scopus 로고    scopus 로고
    • β-Barrel pore-forming toxins: Intriguing dimorphic proteins
    • DOI 10.1021/bi0155394
    • Heuck, A. P., Tweten, R. K., and Johnson, A. E. (2001) β-Barrel pore-forming toxins: Intriguing dimorphic proteins Biochemistry 40, 9065-9073 (Pubitemid 32734170)
    • (2001) Biochemistry , vol.40 , Issue.31 , pp. 9065-9073
    • Heuck, A.P.1    Tweten, R.K.2    Johnson, A.E.3
  • 8
    • 21744447839 scopus 로고    scopus 로고
    • Crystal structure of the Vibrio cholerae cytolysin (VCC) pro-toxin and its assembly into a heptameric transmembrane pore
    • DOI 10.1016/j.jmb.2005.05.045, PII S0022283605006005
    • Olson, R. and Gouaux, E. (2005) Crystal structure of the Vibrio cholerae cytolysin (VCC) pro-toxin and its assembly into a heptameric transmembrane pore J. Mol. Biol. 350, 997-1016 (Pubitemid 40943458)
    • (2005) Journal of Molecular Biology , vol.350 , Issue.5 , pp. 997-1016
    • Olson, R.1    Gouaux, E.2
  • 10
    • 0018733831 scopus 로고
    • Purification and characterization of a hemolysin produced by Vibrio cholerae biotype El Tor: Another toxic substance produced by cholera vibrios
    • Honda, T. and Finkelstein, R. A. (1979) Purification and characterization of a hemolysin produced by Vibrio cholerae biotype El Tor: another toxic substance produced by cholera vibrios Infect. Immun. 26, 1020-1027 (Pubitemid 10212962)
    • (1979) Infection and Immunity , vol.26 , Issue.3 , pp. 1020-1027
    • Honda, T.1    Finkelstein, R.A.2
  • 11
    • 0021178642 scopus 로고
    • Molecular cloning of the hemolysin determinant from Vibrio cholerae El Tor
    • Goldberg, S. L. and Murphy, J. R. (1984) Molecular cloning of the hemolysin determinant from Vibrio cholerae El Tor J. Bacteriol. 160, 239-244 (Pubitemid 14022851)
    • (1984) Journal of Bacteriology , vol.160 , Issue.1 , pp. 239-244
    • Goldberg, S.L.1    Murphy, J.R.2
  • 12
    • 0021261377 scopus 로고
    • Non-O1 Vibrio cholerae hemolysin: Purification, partial characterization, and immunological relatedness to El Tor hemolysin
    • Yamamoto, K., Al-Omani, M., Honda, T., Takeda, Y., and Miwatani, T. (1984) Non-O1 Vibrio cholerae hemolysin: Purification, partial characterization, and immunological relatedness to El Tor hemolysin Infect. Immun. 45, 192-196 (Pubitemid 14084635)
    • (1984) Infection and Immunity , vol.45 , Issue.1 , pp. 192-196
    • Yamamoto, K.1    Al-Omani, M.2    Honda, T.3
  • 13
    • 0023274118 scopus 로고
    • Enterotoxicity of El Tor-like hemolysin of non-O1 Vibrio cholerae
    • Ichinose, Y., Yamamoto, K., Nakasone, N., Tanabe, M. J., Takeda, T., Miwatani, T., and Iwanaga, M. (1987) Enterotoxicity of El Tor-like hemolysin of non-O1 Vibrio cholerae Infect. Immun. 55, 1090-1093 (Pubitemid 17065656)
    • (1987) Infection and Immunity , vol.55 , Issue.5 , pp. 1090-1093
    • Ichinose, Y.1    Yamamoto, K.2    Nakasone, N.3
  • 14
    • 0026660362 scopus 로고
    • The mode of action of Vibrio cholerae cytolysin. The influences on both erythrocytes and planar lipid bilayers
    • Krasilnikov, O. V., Muratkhodjaev, J. N., and Zitzer, A. O. (1992) The mode of action of Vibrio cholerae cytolysin. The influences on both erythrocytes and planar lipid bilayers Biochim. Biophys. Acta 1111, 7-16
    • (1992) Biochim. Biophys. Acta , vol.1111 , pp. 7-16
    • Krasilnikov, O.V.1    Muratkhodjaev, J.N.2    Zitzer, A.O.3
  • 15
    • 0029004327 scopus 로고
    • Characterization of Vibrio cholerae El Tor cytolysin as an oligomerizing pore-forming toxin
    • Zitzer, A., Walev, I., Palmer, M., and Bhakdi, S. (1995) Characterization of Vibrio cholerae El Tor cytolysin as an oligomerizing pore-forming toxin Med. Microbiol. Immunol. 184, 37-44
    • (1995) Med. Microbiol. Immunol. , vol.184 , pp. 37-44
    • Zitzer, A.1    Walev, I.2    Palmer, M.3    Bhakdi, S.4
  • 16
    • 0030037293 scopus 로고    scopus 로고
    • Mechanism of membrane damage by El Tor hemolysin of Vibrio cholerae O1
    • Ikigai, H., Akatsuka, A., Tsujiyama, H., Nakae, T., and Shimamura, T. (1996) Mechanism of membrane damage by El Tor hemolysin of Vibrio cholerae O1 Infect. Immun. 64, 2968-2973 (Pubitemid 26256134)
    • (1996) Infection and Immunity , vol.64 , Issue.8 , pp. 2968-2973
    • Ikigai, H.1    Akatsuka, A.2    Tsujiyama, H.3    Nakae, T.4    Shimamura, T.5
  • 17
    • 0029741086 scopus 로고    scopus 로고
    • HlyA hemolysin of vibrio cholerae o1 biotype El Tor identification of the hemolytic complex and evidence for the formation of anion-selective ion-permeable channels
    • Menzl, K., Maier, E., Chakraborty, T., and Benz, R. (1996) HlyA hemolysin of Vibrio cholerae O1 biotype E1 Tor. Identification of the hemolytic complex and evidence for the formation of anion-selective ion-permeable channels Eur. J. Biochem. 240, 646-654 (Pubitemid 26321167)
    • (1996) European Journal of Biochemistry , vol.240 , Issue.3 , pp. 646-654
    • Menzl, K.1    Maier, E.2    Chakraborty, T.3    Benz, R.4
  • 19
    • 0025609753 scopus 로고
    • Two-step processing for activation of the cytolysin/hemolysin of Vibrio cholerae O1 biotype El Tor: Nucleotide sequence of the structural gene (hlyA) and characterization of the processed products
    • Yamamoto, K., Ichinose, Y., Shinagawa, H., Makino, K., Nakata, A., Iwanaga, M., Honda, T., and Miwatani, T. (1990) Two-step processing for activation of the cytolysin/hemolysin of Vibrio cholerae O1 biotype El Tor: Nucleotide sequence of the structural gene (hlyA) and characterization of the processed products Infect. Immun. 58, 4106-4116
    • (1990) Infect. Immun. , vol.58 , pp. 4106-4116
    • Yamamoto, K.1    Ichinose, Y.2    Shinagawa, H.3    Makino, K.4    Nakata, A.5    Iwanaga, M.6    Honda, T.7    Miwatani, T.8
  • 20
    • 72449138557 scopus 로고    scopus 로고
    • Three-dimensional structure of the detergent-solubilized Vibrio cholerae cytolysin (VCC) heptamer by electron cryomicroscopy
    • He, Y. and Olson, R. (2010) Three-dimensional structure of the detergent-solubilized Vibrio cholerae cytolysin (VCC) heptamer by electron cryomicroscopy J. Struct. Biol. 169, 6-13
    • (2010) J. Struct. Biol. , vol.169 , pp. 6-13
    • He, Y.1    Olson, R.2
  • 21
    • 0029858955 scopus 로고    scopus 로고
    • In vitro proteolytic processing and activation of the recombinant precursor of El Tor cytolysin/hemolysin (pro-HlyA) of Vibrio cholerae by soluble hemagglutinin/protease of V. cholerae, trypsin, and other proteases
    • Nagamune, K., Yamamoto, K., Naka, A., Matsuyama, J., Miwatani, T., and Honda, T. (1996) In vitro proteolytic processing and activation of the recombinant precursor of El Tor cytolysin/hemolysin (pro-HlyA) of Vibrio cholerae by soluble hemagglutinin/protease of V. cholerae, trypsin, and other proteases Infect. Immun. 64, 4655-4658 (Pubitemid 26357073)
    • (1996) Infection and Immunity , vol.64 , Issue.11 , pp. 4655-4658
    • Nagamune, K.1    Yamamoto, K.2    Naka, A.3    Matsuyama, J.4    Miwatani, T.5    Honda, T.6
  • 23
    • 0031024004 scopus 로고    scopus 로고
    • Intramolecular chaperone activity of the pro-region of Vibrio cholerae El Tor cytolysin
    • DOI 10.1074/jbc.272.2.1338
    • Nagamune, K., Yamamoto, K., and Honda, T. (1997) Intramolecular chaperone activity of the pro-region of Vibrio cholerae El Tor cytolysin J. Biol. Chem. 272, 1338-1343 (Pubitemid 27034637)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.2 , pp. 1338-1343
    • Nagamune, K.1    Yamamoto, K.2    Honda, T.3
  • 24
    • 0141866851 scopus 로고    scopus 로고
    • Unfolding of Vibrio cholerae hemolysin induces oligomerization of the toxin monomer
    • DOI 10.1074/jbc.M305965200
    • Chattopadhyay, K. and Banerjee, K. K. (2003) Unfolding of Vibrio cholerae hemolysin induces oligomerization of the toxin monomer J. Biol. Chem. 278, 38470-38475 (Pubitemid 37221741)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.40 , pp. 38470-38475
    • Chattopadhyay, K.1    Banerjee, K.K.2
  • 25
    • 0036047661 scopus 로고    scopus 로고
    • Vibrio cholerae hemolysin: Implication of amphiphilicity and lipid-induced conformational change for its pore-forming activity
    • DOI 10.1046/j.1432-1033.2002.03137.x
    • Chattopadhyay, K., Bhattacharyya, D., and Banerjee, K. K. (2002) Vibrio cholerae hemolysin. Implication of amphiphilicity and lipid-induced conformational change for its pore-forming activity Eur. J. Biochem. 269, 4351-4358 (Pubitemid 35026021)
    • (2002) European Journal of Biochemistry , vol.269 , Issue.17 , pp. 4351-4358
    • Chattopadhyay, K.1    Bhattacharyya, D.2    Banerjee, K.K.3
  • 26
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4 (1994) The CCP4 suite: Programs for protein crystallography Acta Crystallogr. D50, 760-763
    • (1994) Acta Crystallogr. , vol.50 , pp. 760-763
  • 27
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • Lee, B. and Richards, F. M. (1971) The interpretation of protein structures: Estimation of static accessibility J. Mol. Biol. 55, 379-400
    • (1971) J. Mol. Biol. , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 30
    • 0013800421 scopus 로고
    • The interaction of a naphthalene dye with apomyoglobin and apohemoglobin. A fluorescent probe of non-polar binding sites
    • Stryer, L. (1965) The interaction of a naphthalene dye with apomyoglobin and apohemoglobin. A fluorescent probe of non-polar binding sites J. Mol. Biol. 13, 482-495
    • (1965) J. Mol. Biol. , vol.13 , pp. 482-495
    • Stryer, L.1
  • 31
    • 0025292246 scopus 로고
    • In vitro folding and oligomerization of a membrane protein. Transition of bacterial porin from random coil to native conformation
    • Eisele, J. L. and Rosenbusch, J. P. (1990) In vitro folding and oligomerization of a membrane protein. Transition of bacterial porin from random coil to native conformation J. Biol. Chem. 265, 10217-10220
    • (1990) J. Biol. Chem. , vol.265 , pp. 10217-10220
    • Eisele, J.L.1    Rosenbusch, J.P.2
  • 33
    • 0028970780 scopus 로고
    • Vibrio spp. secrete proaerolysin as a folded dimer without the need for disulphide bond formation
    • Hardie, K. R., Schulze, A., Parker, M. W., and Buckley, J. T. (1995) Vibrio spp. secrete proaerolysin as a folded dimer without the need for disulphide bond formation Mol. Microbiol. 17, 1035-1044
    • (1995) Mol. Microbiol. , vol.17 , pp. 1035-1044
    • Hardie, K.R.1    Schulze, A.2    Parker, M.W.3    Buckley, J.T.4
  • 34
    • 0021801526 scopus 로고
    • Activation of the hole-forming toxin aerolysin by extracellular processing
    • Howard, S. P. and Buckley, J. T. (1985) Activation of the hole-forming toxin aerolysin by extracellular processing J. Bacteriol. 163, 336-340 (Pubitemid 15012757)
    • (1985) Journal of Bacteriology , vol.163 , Issue.1 , pp. 336-340
    • Howard, S.P.1    Buckley, J.T.2
  • 35
    • 0028878878 scopus 로고
    • The primary structure of Clostridium septicum α-toxin exhibits similarity with that of Aeromonas hydrophila aerolysin
    • Ballard, J., Crabtree, J., Roe, B. A., and Tweten, R. K. (1995) The primary structure of Clostridium septicum α-toxin exhibits similarity with that of Aeromonas hydrophila aerolysin Infect. Immun. 63, 340-344
    • (1995) Infect. Immun. , vol.63 , pp. 340-344
    • Ballard, J.1    Crabtree, J.2    Roe, B.A.3    Tweten, R.K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.