메뉴 건너뛰기




Volumn 31, Issue 3, 1999, Pages 785-794

Expression and properties of an aerolysin - Clostridium sepficum alpha toxin hybrid protein

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA TOXIN; GLYCOPHORIN; GLYCOSYLPHOSPHATIDYLINOSITOL; HYBRID PROTEIN; MEMBRANE RECEPTOR;

EID: 0032908938     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.1999.01217.x     Document Type: Article
Times cited : (34)

References (37)
  • 2
    • 0028878878 scopus 로고
    • The primary structure of Clostridium septicum alpha 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 alpha 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
  • 3
    • 0016740031 scopus 로고
    • Interactions between aerolysin, erythrocytes and erythrocyte membranes
    • Bernheimer, A.W., Avigad, L.S., and Avigad, G. (1975) Interactions between aerolysin, erythrocytes and erythrocyte membranes. Infect Immun 11: 1312-1319.
    • (1975) Infect Immun , vol.11 , pp. 1312-1319
    • Bernheimer, A.W.1    Avigad, L.S.2    Avigad, G.3
  • 4
    • 0025004421 scopus 로고
    • Purification of cloned proaerolysin released by a low protease mutant of Aeromonas salmonicida
    • Buckley, J.T. (1990) Purification of cloned proaerolysin released by a low protease mutant of Aeromonas salmonicida. Biochem Cell Biol 68: 221-224.
    • (1990) Biochem Cell Biol , vol.68 , pp. 221-224
    • Buckley, J.T.1
  • 5
    • 0029561992 scopus 로고
    • Protonation of His-132 promotes oligomerization of the channel-forming toxin
    • Buckley, J.T., Wilmsen, U., Lesieur, C., Schulze, A., Pattus, F., Parker, M.W., et al. (1995) Protonation of His-132 promotes oligomerization of the channel-forming toxin. Biochemistry 34: 16450-16455.
    • (1995) Biochemistry , vol.34 , pp. 16450-16455
    • Buckley, J.T.1    Wilmsen, U.2    Lesieur, C.3    Schulze, A.4    Pattus, F.5    Parker, M.W.6
  • 6
    • 0029154039 scopus 로고
    • Rapid turnover and impaired cell-surface expression of the human folate receptor in mouse L(tk-) fibroblasts, a cell line defective in glycosylphosphatidylinositol tail synthesis
    • Chung, K.N., Roberts, S., Kim, C.H., Kirassova, M., Trepel, J., and Elwood, P.C. (1995) Rapid turnover and impaired cell-surface expression of the human folate receptor in mouse L(tk-) fibroblasts, a cell line defective in glycosylphosphatidylinositol tail synthesis. Arch Biochem Biophys 322: 228-234.
    • (1995) Arch Biochem Biophys , vol.322 , pp. 228-234
    • Chung, K.N.1    Roberts, S.2    Kim, C.H.3    Kirassova, M.4    Trepel, J.5    Elwood, P.C.6
  • 7
    • 0030789217 scopus 로고    scopus 로고
    • The erythrocyte receptor for the channel-forming toxin aerolysin is a novel glycosyl-phosphatidylinositol-anchored protein
    • Cowell, S., Wolfgang, A., Gruber, H.J., Nelson, K.L., and Buckley, J.T. (1997) The erythrocyte receptor for the channel-forming toxin aerolysin is a novel glycosyl-phosphatidylinositol-anchored protein. Mol Microbiol 25: 343-350.
    • (1997) Mol Microbiol , vol.25 , pp. 343-350
    • Cowell, S.1    Wolfgang, A.2    Gruber, H.J.3    Nelson, K.L.4    Buckley, J.T.5
  • 8
    • 0031936213 scopus 로고    scopus 로고
    • Glycosylphosphatidylinositol anchors of membrane glycoproteins are binding determinants for the channel-forming toxin aerolysin
    • Aerolysin-Clostridium septicum alpha toxin hybrid 793 Diep, D.B., Nelson, K.L, Raja, S.M., Pleshak, E.N., and Buckley, J.T. (1998a) Glycosylphosphatidylinositol anchors of membrane glycoproteins are binding determinants for the channel-forming toxin aerolysin. J Biol Chem 273: 2355-2360.
    • (1998) J Biol Chem , vol.273 , pp. 2355-2360
    • Diep, D.B.1    Nelson, K.L.2    Raja, S.M.3    Pleshak, E.N.4    Buckley, J.T.5
  • 9
    • 0031756554 scopus 로고    scopus 로고
    • Secretion and properties of the large and small lobes of the channel-forming toxin aerolysin
    • Diep, D.B., Lawrence, T.S., Ausio, J., Howard, S.P., and Buckley, J.T. (1998b) Secretion and properties of the large and small lobes of the channel-forming toxin aerolysin. Mol Microbiol 30: 341-352.
    • (1998) Mol Microbiol , vol.30 , pp. 341-352
    • Diep, D.B.1    Lawrence, T.S.2    Ausio, J.3    Howard, S.P.4    Buckley, J.T.5
  • 10
    • 0022870839 scopus 로고
    • Molecular cloning of the plasmid RP4 primase region in a multi-host-range tacP expression vector
    • Furste, J.P., Pansegrau, W., Frank, R., Blocker, H., Scholz, P., Bagdasarian, M., et al. (1986) Molecular cloning of the plasmid RP4 primase region in a multi-host-range tacP expression vector. Gene 48: 119-131.
    • (1986) Gene , vol.48 , pp. 119-131
    • Furste, J.P.1    Pansegrau, W.2    Frank, R.3    Blocker, H.4    Scholz, P.5    Bagdasarian, M.6
  • 11
    • 0023884322 scopus 로고
    • The cytolytic toxin aerolysin must aggregate to disrupt erythrocytes, and aggregation is stimulated by human glycophorin
    • Garland, W.J., and Buckley, J.T. (1988) The cytolytic toxin aerolysin must aggregate to disrupt erythrocytes, and aggregation is stimulated by human glycophorin. Infect Immun 56: 1249-1253.
    • (1988) Infect Immun , vol.56 , pp. 1249-1253
    • Garland, W.J.1    Buckley, J.T.2
  • 12
    • 0026745129 scopus 로고
    • Spectroscopic study of the activation and oligomerization of the channel-forming toxin aerolysin: Identification of the site of proteolytic activation
    • van der Goot, F.G., Lakey, J., Pattus, F., Kay, C.M., Sorokine, O., Van Dorsselaer, A., et al. (1992) Spectroscopic study of the activation and oligomerization of the channel-forming toxin aerolysin: identification of the site of proteolytic activation. Biochemistry 31: 8566-8570.
    • (1992) Biochemistry , vol.31 , pp. 8566-8570
    • Van Der Goot, F.G.1    Lakey, J.2    Pattus, F.3    Kay, C.M.4    Sorokine, O.5    Van Dorsselaer, A.6
  • 13
    • 0027275474 scopus 로고
    • Dimerization stabilizes the pore-forming toxin aerolysin in solution
    • van der Goot, F.G., Ausio, J., Wong, K.R., Pattus, F., and Buckley, J.T. (1993a) Dimerization stabilizes the pore-forming toxin aerolysin in solution. J Biol Chem 268: 18272-18279.
    • (1993) J Biol Chem , vol.268 , pp. 18272-18279
    • Van Der Goot, F.G.1    Ausio, J.2    Wong, K.R.3    Pattus, F.4    Buckley, J.T.5
  • 14
    • 0027480971 scopus 로고
    • Oligomerization of the channel-forming toxin aerolysin precedes insertion into lipid bilayers
    • van der Goot, F.G., Pattus, F., Wong, K.R., and Buckley, J.T. (1993b) Oligomerization of the channel-forming toxin aerolysin precedes insertion into lipid bilayers. Biochemistry 32: 2636-2642.
    • (1993) Biochemistry , vol.32 , pp. 2636-2642
    • Van Der Goot, F.G.1    Pattus, F.2    Wong, K.R.3    Buckley, J.T.4
  • 15
    • 0028044180 scopus 로고
    • Partial purification of the rat erythrocyte receptor for the channel-forming toxin aerolysin and reconstitution into planar lipid bilayers
    • Gruber, H.J., Wilmsen, H.U., Cowell, S., Schindler, H., and Buckley, J.T. (1994) Partial purification of the rat erythrocyte receptor for the channel-forming toxin aerolysin and reconstitution into planar lipid bilayers. Mol Microbiol 14: 1093-1101.
    • (1994) Mol Microbiol , vol.14 , pp. 1093-1101
    • Gruber, H.J.1    Wilmsen, H.U.2    Cowell, S.3    Schindler, H.4    Buckley, J.T.5
  • 16
    • 0019125857 scopus 로고
    • High frequency mobilization of the chromosome of Escherichia coli by a mutant of plasmid RF4 temperature-sensitive for maintenance
    • Harayama, S., Tsuda, M., and Lino, T. (1980) High frequency mobilization of the chromosome of Escherichia coli by a mutant of plasmid RF4 temperature-sensitive for maintenance. Mol Gen Genet 180: 47-56.
    • (1980) Mol Gen Genet , vol.180 , pp. 47-56
    • Harayama, S.1    Tsuda, M.2    Lino, T.3
  • 17
    • 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
  • 19
    • 0020071103 scopus 로고
    • Membrane glycoprotein receptor and hole-forming properties of a cytolytic protein toxin
    • Howard, S.P., and Buckley, J.T. (1982) Membrane glycoprotein receptor and hole-forming properties of a cytolytic protein toxin. Biochemistry 21: 1662-1667.
    • (1982) Biochemistry , vol.21 , pp. 1662-1667
    • Howard, S.P.1    Buckley, J.T.2
  • 20
    • 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.
    • (1985) J Bacteriol , vol.163 , pp. 336-340
    • Howard, S.P.1    Buckley, J.T.2
  • 21
    • 0027431108 scopus 로고
    • Isolation and analysis of eight exe genes and their involvement in extracellular protein secretion and outer membrane assembly in Aeromonas hydrophila
    • Howard, S.P., Critch, J., and Bedi, A. (1993) Isolation and analysis of eight exe genes and their involvement in extracellular protein secretion and outer membrane assembly in Aeromonas hydrophila. J Bacteriol 175: 6695-6703.
    • (1993) J Bacteriol , vol.175 , pp. 6695-6703
    • Howard, S.P.1    Critch, J.2    Bedi, A.3
  • 22
    • 0023238632 scopus 로고
    • Nucleotide sequence of the gene for the hole-forming toxin aerolysin from Aeromonas hydrophila
    • Howard, S.P., Garland, W.J., Green, M.J., and Buckley, J.T. (1987) Nucleotide sequence of the gene for the hole-forming toxin aerolysin from Aeromonas hydrophila. J Bacteriol 169:2896-2871.
    • (1987) J Bacteriol , vol.169 , pp. 2896-12871
    • Howard, S.P.1    Garland, W.J.2    Green, M.J.3    Buckley, J.T.4
  • 23
    • 0029828324 scopus 로고    scopus 로고
    • A TonB-like protein and a novel membrane protein containing an ATP-binding cassette function together in exotoxin secretion
    • Howard, S.P., Meiklejohn, H.G., Shivak, D., and Jahagirdar, R. (1996) A TonB-like protein and a novel membrane protein containing an ATP-binding cassette function together in exotoxin secretion. Mol Microbiol 22: 595-604.
    • (1996) Mol Microbiol , vol.22 , pp. 595-604
    • Howard, S.P.1    Meiklejohn, H.G.2    Shivak, D.3    Jahagirdar, R.4
  • 24
    • 0028151687 scopus 로고
    • Isolation and characterization of a second exe operon required for extracellular protein secretion in Aeromonas hydrophila
    • Jahagirdar, R., and Howard, S.P. (1994) Isolation and characterization of a second exe operon required for extracellular protein secretion in Aeromonas hydrophila. J Bacteriol 176: 6819-6826.
    • (1994) J Bacteriol , vol.176 , pp. 6819-6826
    • Jahagirdar, R.1    Howard, S.P.2
  • 25
    • 0025946698 scopus 로고
    • How thick is the glycocalyx of human erythrocytes?
    • Linss, W., Pilgrim, C., and Feuerstein, H. (1991) How thick is the glycocalyx of human erythrocytes? Acta Histochem 91: 101-104.
    • (1991) Acta Histochem , vol.91 , pp. 101-104
    • Linss, W.1    Pilgrim, C.2    Feuerstein, H.3
  • 26
    • 0003785155 scopus 로고
    • Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Miller, J.H. (1972) Experiments in Molecular Genetics. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press, p. 431.
    • (1972) Experiments in Molecular Genetics. , pp. 431
    • Miller, J.H.1
  • 27
    • 0026019764 scopus 로고
    • A series of wide-host-range low-copy-number vectors that allow direct screening for recombinants
    • Morales, V.M., Backman, A., and Bagdasarian, M. (1991) A series of wide-host-range low-copy-number vectors that allow direct screening for recombinants. Gene 97: 39-47.
    • (1991) Gene , vol.97 , pp. 39-47
    • Morales, V.M.1    Backman, A.2    Bagdasarian, M.3
  • 28
    • 0030978914 scopus 로고    scopus 로고
    • The glycosylphosphatidylinositol-anchored surface glycoprotein Thy-1 is a receptor for the channel-forming toxin aerolysin
    • Nelson, K.L., Raja, S.M., and Buckley, J.T. (1997) The glycosylphosphatidylinositol-anchored surface glycoprotein Thy-1 is a receptor for the channel-forming toxin aerolysin. J Biol Chem 272: 12170-12174.
    • (1997) J Biol Chem , vol.272 , pp. 12170-12174
    • Nelson, K.L.1    Raja, S.M.2    Buckley, J.T.3
  • 29
    • 0015240315 scopus 로고
    • Molecular weight determination of protein dodecyl sulphate complexes by gel electrophoresis in a discontinuous buffer system
    • Neville, D.M. (1971) Molecular weight determination of protein dodecyl sulphate complexes by gel electrophoresis in a discontinuous buffer system. J Biol Chem 246: 6328-6334.
    • (1971) J Biol Chem , vol.246 , pp. 6328-6334
    • Neville, D.M.1
  • 30
    • 0027976196 scopus 로고
    • Structure of the Aeromonas toxin proaerolysin in its water-soluble and membrane-channel states
    • Parker, M.W., Buckley, J.T., Postma, J.P., Tucker, A.D., Leonard, K., Pattus, F., et al. (1994) Structure of the Aeromonas toxin proaerolysin in its water-soluble and membrane-channel states. Nature 367: 292-295.
    • (1994) Nature , vol.367 , pp. 292-295
    • Parker, M.W.1    Buckley, J.T.2    Postma, J.P.3    Tucker, A.D.4    Leonard, K.5    Pattus, F.6
  • 31
    • 0030976146 scopus 로고    scopus 로고
    • Recent progress and future directions in studies of the main terminal branch of the general secretory pathway in Gram-negative bacteria
    • Pugsley, A.P., Francetic, O., Possot, O.M., Sauvonnet, N., and Hardie, K.R. (1997) Recent progress and future directions in studies of the main terminal branch of the general secretory pathway in Gram-negative bacteria. A review. Gene 192: 13-19.
    • (1997) A Review. Gene , vol.192 , pp. 13-19
    • Pugsley, A.P.1    Francetic, O.2    Possot, O.M.3    Sauvonnet, N.4    Hardie, K.R.5
  • 32
    • 0030957151 scopus 로고    scopus 로고
    • Aerolysin and pertussis toxin share a common receptor-binding domain
    • Rossjohn, J., Buckley, J.T., Hazes, B., Murzin, A.G., Read, R.J., and Parker, M.W. (1997) Aerolysin and pertussis toxin share a common receptor-binding domain. EMBO J 16: 3426-3434.
    • (1997) EMBO J , vol.16 , pp. 3426-3434
    • Rossjohn, J.1    Buckley, J.T.2    Hazes, B.3    Murzin, A.G.4    Read, R.J.5    Parker, M.W.6
  • 33
    • 0030881601 scopus 로고    scopus 로고
    • The propeptide of Clostridium septicum alpha toxin functions as an intracellular chaperone and is a potent inhibitor of alpha toxin-dependent cytolysis
    • Sellman, B.R., and Tweten, R.K. (1997) The propeptide of Clostridium septicum alpha toxin functions as an intracellular chaperone and is a potent inhibitor of alpha toxin-dependent cytolysis. Mol Microbiol 25: 429-440.
    • (1997) Mol Microbiol , vol.25 , pp. 429-440
    • Sellman, B.R.1    Tweten, R.K.2
  • 34
    • 0016360444 scopus 로고
    • Preparation of impermeable ghosts and inside-out vesicles from human erythrocyte membranes
    • Steck, T.L., and Kant, J.A. (1974) Preparation of impermeable ghosts and inside-out vesicles from human erythrocyte membranes. Methods Enzymol 31: 172-180.
    • (1974) Methods Enzymol , vol.31 , pp. 172-180
    • Steck, T.L.1    Kant, J.A.2
  • 36
    • 0026721371 scopus 로고
    • The aerolysin membrane channel is formed by heptamerization of the monomer
    • Wilmsen, H.U., Leonard, K.R., Tichelaar, W., Buckley, J.T., and Pattus, F. (1992) The aerolysin membrane channel is formed by heptamerization of the monomer. EMBO J 11: 2457-2463.
    • (1992) EMBO J , vol.11 , pp. 2457-2463
    • Wilmsen, H.U.1    Leonard, K.R.2    Tichelaar, W.3    Buckley, J.T.4    Pattus, F.5
  • 37
    • 0027240488 scopus 로고
    • Aeromonas spp. Can secrete Escherichia coli alkaline phosphatase into the culture supernatant, and its release requires a functional general secretion pathway
    • Wong, K.R., and Buckley, J.T. (1993) Aeromonas spp. can secrete Escherichia coli alkaline phosphatase into the culture supernatant, and its release requires a functional general secretion pathway. Mol Microbiol 9: 955-963.
    • (1993) Mol Microbiol , vol.9 , pp. 955-963
    • Wong, K.R.1    Buckley, J.T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.