메뉴 건너뛰기




Volumn 156, Issue 2, 1997, Pages 157-172

Influence of Cys-130 S. aureus alpha-toxin on planar lipid bilayer and erythrocyte membranes

Author keywords

Erythrocyte; Ion channel; Planar lipid bilayer; Site directed mutagenesis; Staphylotoxin

Indexed keywords

AMINO ACID; ION CHANNEL; STAPHYLOCOCCUS TOXIN;

EID: 0030975688     PISSN: 00222631     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002329900198     Document Type: Article
Times cited : (24)

References (58)
  • 1
    • 0040224170 scopus 로고
    • The thermodynamic analysis of the observed osmotic pressures of protein salt in solutions of finite concentrations
    • Adair, G.S. 1929. The thermodynamic analysis of the observed osmotic pressures of protein salt in solutions of finite concentrations. Proc. Roy. Soc. London, Series A. 126:16-24
    • (1929) Proc. Roy. Soc. London, Series A. , vol.126 , pp. 16-24
    • Adair, G.S.1
  • 5
    • 0021720723 scopus 로고
    • Correlation between toxin binding and hemolytic activity in membrane damage by staphylococcal α-toxin
    • Bhakdi, S., Muhly, M., Fussle, R. 1984. Correlation between toxin binding and hemolytic activity in membrane damage by staphylococcal α-toxin. Infect. Immun. 46:318-323
    • (1984) Infect. Immun. , vol.46 , pp. 318-323
    • Bhakdi, S.1    Muhly, M.2    Fussle, R.3
  • 6
    • 0023901550 scopus 로고
    • Damage of cell membranes by pore-forming bacterial cytolysins
    • Bhakdi, S., Tranum-Jensen, J. 1988. Damage of cell membranes by pore-forming bacterial cytolysins. Prog. Allergy 40:1-43
    • (1988) Prog. Allergy , vol.40 , pp. 1-43
    • Bhakdi, S.1    Tranum-Jensen, J.2
  • 8
    • 0027183815 scopus 로고
    • A guide to use of pore-forming toxins for controlled permeabilization of cell membranes
    • Bhakdi, S., Weller, U., Walev, I., Martin, E., Jonas, D., Palmer, M. 1993. A guide to use of pore-forming toxins for controlled permeabilization of cell membranes. Med. Microbiol. Immunol. 182:167-175
    • (1993) Med. Microbiol. Immunol. , vol.182 , pp. 167-175
    • Bhakdi, S.1    Weller, U.2    Walev, I.3    Martin, E.4    Jonas, D.5    Palmer, M.6
  • 9
    • 0023665444 scopus 로고
    • Characterization of domain borders and of a naturally occurring major fragment of staphylococcal α-toxin
    • Blomqvist, L., Bergman, T., Thelestam, M., Jörnvall, H. 1987. Characterization of domain borders and of a naturally occurring major fragment of staphylococcal α-toxin. FEBS Lett. 211:127-132
    • (1987) FEBS Lett. , vol.211 , pp. 127-132
    • Blomqvist, L.1    Bergman, T.2    Thelestam, M.3    Jörnvall, H.4
  • 10
    • 0022549737 scopus 로고
    • A staphylococcal alpha-toxin fragment: Its characterization and use for mapping biologically active regions of alpha-toxin
    • Blomqvist, L., Thelestam, M. 1986. A staphylococcal alpha-toxin fragment: Its characterization and use for mapping biologically active regions of alpha-toxin. Acta Path. Microbiol. Immunol. Scand. Sect. B. 94:277-283
    • (1986) Acta Path. Microbiol. Immunol. Scand. Sect. B. , vol.94 , pp. 277-283
    • Blomqvist, L.1    Thelestam, M.2
  • 11
    • 8244234955 scopus 로고
    • Statistical method for approaching
    • Dubna
    • Eler, H. 1972. Statistical method for approaching. AINP Report, P11-6816, p. 27, Dubna
    • (1972) AINP Report, P11-6816 , pp. 27
    • Eler, H.1
  • 12
    • 0024399624 scopus 로고
    • Staphylococcal alpha-toxin increases the permeability of lipid vesicles by cholesterol and pH-dependent assembly of oligomeric channels
    • Forti, S., Menestrina, G. 1989. Staphylococcal alpha-toxin increases the permeability of lipid vesicles by cholesterol and pH-dependent assembly of oligomeric channels. Eur. J. Biochem. 181:767-773
    • (1989) Eur. J. Biochem. , vol.181 , pp. 767-773
    • Forti, S.1    Menestrina, G.2
  • 14
    • 0023186359 scopus 로고
    • Biophysical analysis of novel transport pathways indiced in red blood cell membranes
    • Ginsburg, H., Stein, W.D. 1987. Biophysical analysis of novel transport pathways indiced in red blood cell membranes. J. Membrane Biol. 96:1-10
    • (1987) J. Membrane Biol. , vol.96 , pp. 1-10
    • Ginsburg, H.1    Stein, W.D.2
  • 15
    • 0021747672 scopus 로고
    • Primary sequence of the alpha-toxin gene from Staphylococcus aureus Wood 46
    • Gray, G.S., Kehoe, M. 1984. Primary sequence of the alpha-toxin gene from Staphylococcus aureus Wood 46. Infect. Immun. 46:615-618
    • (1984) Infect. Immun. , vol.46 , pp. 615-618
    • Gray, G.S.1    Kehoe, M.2
  • 16
    • 0026927582 scopus 로고
    • Oligomer formation of staphylococcal alpha-toxin analyzed by electron microscopy and image processing
    • Hebert, H., Olofsson, A., Thelestam, M., Skriver, E. 1992. Oligomer formation of staphylococcal alpha-toxin analyzed by electron microscopy and image processing. FEMS Microbioi. Immunol. 105:5-12
    • (1992) FEMS Microbioi. Immunol. , vol.105 , pp. 5-12
    • Hebert, H.1    Olofsson, A.2    Thelestam, M.3    Skriver, E.4
  • 17
    • 0000215805 scopus 로고
    • Counting integral numbers of residues by chemical modification
    • T.E. Creighton, editor. Information Press LTD, Oxford
    • Hollecker, M. 1989. Counting integral numbers of residues by chemical modification. In: Protein Structure. A Practical Approach. T.E. Creighton, editor. p. 147, Information Press LTD, Oxford
    • (1989) Protein Structure. A Practical Approach , pp. 147
    • Hollecker, M.1
  • 18
    • 0022253233 scopus 로고
    • Conformational alteration in alpha-toxin from S. aureus concomitant with the transformation of the water-soluble monomer to the membrane oligomer
    • Ikigai, H., Nakae, T. 1985. Conformational alteration in alpha-toxin from S. aureus concomitant with the transformation of the water-soluble monomer to the membrane oligomer. Biochim. Biophys. Acta 30:175-181
    • (1985) Biochim. Biophys. Acta , vol.30 , pp. 175-181
    • Ikigai, H.1    Nakae, T.2
  • 19
    • 0028168029 scopus 로고
    • 2+ and guanosine 5′-[gamma-thio]triphosphate action on insulin secretion from alpha-toxin-permeabilized HIT-T15 cells
    • 2+ and guanosine 5′-[gamma-thio]triphosphate action on insulin secretion from alpha-toxin-permeabilized HIT-T15 cells. Biochem. J. 301:523-529
    • (1994) Biochem. J. , vol.301 , pp. 523-529
    • Jonas, J.C.1    Li, G.2    Palmer, M.3    Weller, U.4    Wollheim, C.B.5
  • 20
    • 0028324930 scopus 로고
    • Novel path to apoptosis: Small transmembrane pores created by Staphylococcal α-toxin in T-lymphocytes evoke internucleosomal DNA degradation
    • Jonas, D., Walev, I., Berger, T., Liebetrau, M., Palmer, M., Bhakdi, S. 1994b. Novel path to apoptosis: small transmembrane pores created by Staphylococcal α-toxin in T-lymphocytes evoke internucleosomal DNA degradation. Infect. Immun. 62:1304-1312
    • (1994) Infect. Immun. , vol.62 , pp. 1304-1312
    • Jonas, D.1    Walev, I.2    Berger, T.3    Liebetrau, M.4    Palmer, M.5    Bhakdi, S.6
  • 21
    • 0001506921 scopus 로고
    • Partial resolution of the enzymes catalyzing oxidative phosphorilation
    • Kagawa, Y., Racker, E. 1971. Partial resolution of the enzymes catalyzing oxidative phosphorilation. J. Biol.Chem. 246:5477-5487
    • (1971) J. Biol.Chem. , vol.246 , pp. 5477-5487
    • Kagawa, Y.1    Racker, E.2
  • 22
    • 0018942746 scopus 로고
    • Chemical studies on staphylococcal alpha-toxin and its fragments
    • Kato, I., Watanabe, M. 1980. Chemical studies on staphylococcal alpha-toxin and its fragments. Toxicon 18:361-365
    • (1980) Toxicon , vol.18 , pp. 361-365
    • Kato, I.1    Watanabe, M.2
  • 23
  • 24
    • 0026660362 scopus 로고
    • The mode of action of Vibrio cholerae cytolysin. The influence on both erythrocytes and planar lipid bilayers
    • Krasilnikov, O.V., Muratkhodjaev, J.N., Zitzer, A.O. 1992. The mode of action of Vibrio cholerae cytolysin. The influence 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
  • 25
    • 0024676138 scopus 로고
    • Ion transport through channels formed in lipid bilayers by S. aureus α-toxin
    • Krasilnikov, O.V., Sabirov, R.Z. 1989. Ion transport through channels formed in lipid bilayers by S. aureus α-toxin. Gen. Physiol. Biophys. 8:213-222
    • (1989) Gen. Physiol. Biophys. , vol.8 , pp. 213-222
    • Krasilnikov, O.V.1    Sabirov, R.Z.2
  • 30
    • 0027163275 scopus 로고
    • Effects of monoclonal antibodies on α-staphylotoxin action against erythrocytes and model phospholipid membranes
    • Krasilnikov, O.V., Ternovsky, V.I., Merzliak, P.G., Zachidova, L.T., Hungerer, K.-D. 1993. Effects of monoclonal antibodies on α-staphylotoxin action against erythrocytes and model phospholipid membranes. Biochim. Biophys. Acta 1182:94-100
    • (1993) Biochim. Biophys. Acta , vol.1182 , pp. 94-100
    • Krasilnikov, O.V.1    Ternovsky, V.I.2    Merzliak, P.G.3    Zachidova, L.T.4    Hungerer, K.-D.5
  • 31
    • 17744414381 scopus 로고
    • Properties of ion channels induced by α-staphylotoxin in bilayer lipid membranes
    • Krasilnikov, O.V., Ternovsky, V.I., Tashmukhamedov, B.A. 1981. Properties of ion channels induced by α-staphylotoxin in bilayer lipid membranes. Biofisica 26:271-275
    • (1981) Biofisica , vol.26 , pp. 271-275
    • Krasilnikov, O.V.1    Ternovsky, V.I.2    Tashmukhamedov, B.A.3
  • 35
    • 0022504362 scopus 로고
    • Ionic channel formed by S. aureus α-toxin: Voltage-dependent inhibition by divalent and trivalent cations
    • Menestrina, G. 1986. Ionic channel formed by S. aureus α-toxin: voltage-dependent inhibition by divalent and trivalent cations. J. Membrane Biol. 90:177-190
    • (1986) J. Membrane Biol. , vol.90 , pp. 177-190
    • Menestrina, G.1
  • 36
    • 0026758661 scopus 로고
    • Structural features of the pore formed by Staphylococcus aureus alpha-toxin inferred from chemical modification and primary structure analysis
    • Menestrina, G., Belmonte, G., Parisi, V., Morante, S. 1992. Structural features of the pore formed by Staphylococcus aureus alpha-toxin inferred from chemical modification and primary structure analysis. FEMS Microbiol. Immunol. 105:19-28
    • (1992) FEMS Microbiol. Immunol. , vol.105 , pp. 19-28
    • Menestrina, G.1    Belmonte, G.2    Parisi, V.3    Morante, S.4
  • 37
    • 0015459562 scopus 로고
    • Formation of bimolecular membranes from lipid monolayers and a study of their electrical properties
    • Montai, M., Mueller, P. 1972. Formation of bimolecular membranes from lipid monolayers and a study of their electrical properties. Proc. Natl. Acad. Sci. USA 69:3561-3566
    • (1972) Proc. Natl. Acad. Sci. USA , vol.69 , pp. 3561-3566
    • Montai, M.1    Mueller, P.2
  • 38
    • 33947480633 scopus 로고
    • Methods for the formation on single bimolecular lipid membranes in aqueous solution
    • Mueller, P., Rudin, D.O., Tien, H.T., Wescott, W.C. 1963. Methods for the formation on single bimolecular lipid membranes in aqueous solution. J. Phys. Chem. 67:534-535
    • (1963) J. Phys. Chem. , vol.67 , pp. 534-535
    • Mueller, P.1    Rudin, D.O.2    Tien, H.T.3    Wescott, W.C.4
  • 39
    • 0025335986 scopus 로고
    • Crystalline layers and three-dimensional structure of Staphylococcus aureus alpha-toxin
    • Olofsson, A., Kaveus, U., Hacksell, I., Thelestam, M., Hebert, H. 1990. Crystalline layers and three-dimensional structure of Staphylococcus aureus alpha-toxin. Mol. Biol. 214:299-306
    • (1990) Mol. Biol. , vol.214 , pp. 299-306
    • Olofsson, A.1    Kaveus, U.2    Hacksell, I.3    Thelestam, M.4    Hebert, H.5
  • 40
    • 0026692948 scopus 로고
    • The three-dimensional structure of trypsin-treated Staphylococcus aureus alpha-toxin
    • Olofsson, A., Kaveus, U., Thelestam, M., Hebert, H. 1992. The three-dimensional structure of trypsin-treated Staphylococcus aureus alpha-toxin. J. Struct. Biol. 108:238-244
    • (1992) J. Struct. Biol. , vol.108 , pp. 238-244
    • Olofsson, A.1    Kaveus, U.2    Thelestam, M.3    Hebert, H.4
  • 41
    • 0343509468 scopus 로고
    • S aureus alpha-toxin. Production of functionally intact, modifiable protein by introduction of cysteine residues
    • Palmer, M., Jursch, R., Weller, U., Valeva, A., Hilgert, K., Kehoe, M., Bhakdi, S. 1993a. S aureus alpha-toxin. Production of functionally intact, modifiable protein by introduction of cysteine residues. Med. Microbiol. Immunol. 182:207
    • (1993) Med. Microbiol. Immunol. , vol.182 , pp. 207
    • Palmer, M.1    Jursch, R.2    Weller, U.3    Valeva, A.4    Hilgert, K.5    Kehoe, M.6    Bhakdi, S.7
  • 42
    • 0027316337 scopus 로고
    • Staphylococcus aureus alpha-toxin. Production of functionally intact, site-specifically modifiable protein by introduction of cysteine in positions 69, 130, 186
    • Palmer, M., Jursch, R., Weller, U., Valeva, A., Hilgert, K., Kehoe, M., Bhakdi, S., 1993b. Staphylococcus aureus alpha-toxin. Production of functionally intact, site-specifically modifiable protein by introduction of cysteine in positions 69, 130, 186. J. Biol. Chem. 268:11959-11962
    • (1993) J. Biol. Chem. , vol.268 , pp. 11959-11962
    • Palmer, M.1    Jursch, R.2    Weller, U.3    Valeva, A.4    Hilgert, K.5    Kehoe, M.6    Bhakdi, S.7
  • 43
    • 0027241025 scopus 로고
    • Altered pore-forming properties of proteolytically nicked staphylococcal alpha-toxin
    • Palmer, M., Weller, U., Messner, M., Bhakdi, S. 1993c. Altered pore-forming properties of proteolytically nicked staphylococcal alpha-toxin. J. Biol. Chem. 268:11963-11967
    • (1993) J. Biol. Chem. , vol.268 , pp. 11963-11967
    • Palmer, M.1    Weller, U.2    Messner, M.3    Bhakdi, S.4
  • 44
    • 0000560829 scopus 로고
    • Filtration, diffusion and molecular sieving through porous cellulose membranes
    • Renkin, E.M. 1954. Filtration, diffusion and molecular sieving through porous cellulose membranes. J. Gen. Physiol. 38:225-243
    • (1954) J. Gen. Physiol. , vol.38 , pp. 225-243
    • Renkin, E.M.1
  • 45
    • 0027223744 scopus 로고
    • Relation between ionic channel conductance and conductivity of media containing different nonelectrolytes. A novel method of pore size determination
    • Sabirov, R.Z., Krasilnikov, O.V., Ternovsky, V.I., Merzliak, P.G. 1993. Relation between ionic channel conductance and conductivity of media containing different nonelectrolytes. A novel method of pore size determination. Gen. Physiol. Biophys. 12:95-111
    • (1993) Gen. Physiol. Biophys. , vol.12 , pp. 95-111
    • Sabirov, R.Z.1    Krasilnikov, O.V.2    Ternovsky, V.I.3    Merzliak, P.G.4
  • 46
    • 8244254206 scopus 로고
    • Three types of pores formed by S. aureus α-toxin in erythrocyte membranes
    • Sabirov, R.Z., Zakhidova, L.T., Krasilnikov, O.V. 1991. Three types of pores formed by S. aureus α-toxin in erythrocyte membranes. Biol. Membrany 8:749-754
    • (1991) Biol. Membrany , vol.8 , pp. 749-754
    • Sabirov, R.Z.1    Zakhidova, L.T.2    Krasilnikov, O.V.3
  • 47
    • 0015858867 scopus 로고
    • Physical and chemical studies on staphylococcal alpha-toxin a and B
    • Six, H., Harshman, S. 1973. Physical and chemical studies on staphylococcal alpha-toxin A and B. Biochemistry 12:2677-2683
    • (1973) Biochemistry , vol.12 , pp. 2677-2683
    • Six, H.1    Harshman, S.2
  • 48
    • 0023848842 scopus 로고
    • Staphylococcal alpha-toxin - Recent advances
    • Thelestam, M., Blomqvist, L. 1988. Staphylococcal alpha-toxin - Recent advances. Toxicon 26:51-65
    • (1988) Toxicon , vol.26 , pp. 51-65
    • Thelestam, M.1    Blomqvist, L.2
  • 49
    • 8244221475 scopus 로고
    • Comparative analyze of properties of ion channels induced by staphylococcal alpha-toxin and it's N-terminal fragment
    • Ternovsky, V.I., Zaripova, R.K., Krasilnikov, O.V., Korneev, A.S., 1991. Comparative analyze of properties of ion channels induced by staphylococcal alpha-toxin and it's N-terminal fragment. Biol. Membrany 8:271-279
    • (1991) Biol. Membrany , vol.8 , pp. 271-279
    • Ternovsky, V.I.1    Zaripova, R.K.2    Krasilnikov, O.V.3    Korneev, A.S.4
  • 50
    • 0021844629 scopus 로고
    • Secondary structure and assembly mechanism of an oligomeric channel protein
    • Tobkes, N., Wallace, B.A., Bayley, H. 1985. Secondary structure and assembly mechanism of an oligomeric channel protein. Biochemistry 24:1915-1920
    • (1985) Biochemistry , vol.24 , pp. 1915-1920
    • Tobkes, N.1    Wallace, B.A.2    Bayley, H.3
  • 51
    • 0342639204 scopus 로고    scopus 로고
    • Molecular architecture of toxin channel delineated by fluorometric analyses of cysteine-substituted mutants: Resistant cells prevent membrane insertion of pore-forming domain
    • Valeva, A., Walev, I., Pinkemell, M., Bayley, H., Palmer, M., Bhakdi, S. 1996. Molecular architecture of toxin channel delineated by fluorometric analyses of cysteine-substituted mutants: resistant cells prevent membrane insertion of pore-forming domain. Medical Microbiology and Immunology 185:119
    • (1996) Medical Microbiology and Immunology , vol.185 , pp. 119
    • Valeva, A.1    Walev, I.2    Pinkemell, M.3    Bayley, H.4    Palmer, M.5    Bhakdi, S.6
  • 52
    • 0028181019 scopus 로고
    • A pore-forming protein with a protease-activated trigger
    • Walker, B., Bayley, H. 1994. A pore-forming protein with a protease-activated trigger. Protein Eng. 7:91-97
    • (1994) Protein Eng. , vol.7 , pp. 91-97
    • Walker, B.1    Bayley, H.2
  • 53
    • 0027480752 scopus 로고
    • Functional complementation of staphylococcal α-hemolysin fragments. Overlaps, nicks, and gaps in the glycine-rich loop
    • Walker, B., Krishnasaslry, M., Bayley, H. 1993. Functional complementation of staphylococcal α-hemolysin fragments. Overlaps, nicks, and gaps in the glycine-rich loop. J. Biol. Chem. 268:5285-5292
    • (1993) J. Biol. Chem. , vol.268 , pp. 5285-5292
    • Walker, B.1    Krishnasaslry, M.2    Bayley, H.3
  • 54
    • 0026785678 scopus 로고
    • Assembly of the oligomeric membrane pore formed by Staphylococcal alpha-hemolysin examined by truncation mutagenesis
    • Walker, B., Krishnasastry, M., Zorn, L., Bayley, H. 1992. Assembly of the oligomeric membrane pore formed by Staphylococcal alpha-hemolysin examined by truncation mutagenesis. J. Biol. Chem. 267:21782-21786
    • (1992) J. Biol. Chem. , vol.267 , pp. 21782-21786
    • Walker, B.1    Krishnasastry, M.2    Zorn, L.3    Bayley, H.4
  • 55
    • 0026641089 scopus 로고
    • Functional expression of the α-hemolysin of S. aureus in intact E. coli and in cell lysates. Deletion of five C-terminal amino acids selectively impairs hemolytic activity
    • Walker, B., Krishnasastry, M., Zorn, L., Kasianowicz, J., Bayley, H. 1992. Functional expression of the α-hemolysin of S. aureus in intact E. coli and in cell lysates. Deletion of five C-terminal amino acids selectively impairs hemolytic activity. J. Biol. Chem. 267:10902-10909
    • (1992) J. Biol. Chem. , vol.267 , pp. 10902-10909
    • Walker, B.1    Krishnasastry, M.2    Zorn, L.3    Kasianowicz, J.4    Bayley, H.5
  • 56
    • 0026457115 scopus 로고
    • 2+ ions on its interaction with lipid bilayers
    • 2+ ions on its interaction with lipid bilayers. J. Struct. Biol. 109:129-141
    • (1992) J. Struct. Biol. , vol.109 , pp. 129-141
    • Ward, R.J.1    Leonard, K.2
  • 57
    • 0028341551 scopus 로고
    • Identification of a putative membrane-inserted segment in the a-toxin of Staphylococcus aureus
    • Ward, R.J., Palmer, M., Leonard, K., Bhakdi, S. 1994. Identification of a putative membrane-inserted segment in the a-toxin of Staphylococcus aureus. Biochemistry 33:7477-7484
    • (1994) Biochemistry , vol.33 , pp. 7477-7484
    • Ward, R.J.1    Palmer, M.2    Leonard, K.3    Bhakdi, S.4
  • 58
    • 0017815695 scopus 로고
    • Purification and some properties of a lethal toxic fragment of staphylococcal alpha-toxin by tryptic digestion
    • Watanabe, M., Kato, I. 1978. Purification and some properties of a lethal toxic fragment of staphylococcal alpha-toxin by tryptic digestion. Biochim. Biophys. Acta 535:388-400
    • (1978) Biochim. Biophys. Acta , vol.535 , pp. 388-400
    • Watanabe, M.1    Kato, I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.