메뉴 건너뛰기




Volumn 1762, Issue 1, 2006, Pages 110-114

Role of tyrosine-57 and -65 in membrane-damaging and sphingomyelinase activities of Clostridium perfringens alpha-toxin

Author keywords

Alpha toxin; Clostridium perfringens; Hemolytic activity; Liposome; Sphingomyelinase

Indexed keywords

ALANINE; ALPHA TOXIN; CALCIUM BINDING PROTEIN; CARBOXYFLUORESCEIN; CHOLESTEROL; DEOXYCHOLATE SODIUM; LEUCINE; PHENYLALANINE; SPHINGOMYELIN; SPHINGOMYELIN PHOSPHODIESTERASE; TYROSINE;

EID: 29644435330     PISSN: 09254439     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbadis.2005.10.002     Document Type: Article
Times cited : (17)

References (24)
  • 1
    • 0027231710 scopus 로고
    • Bacterial phospholipases C
    • R.W. Titball Bacterial phospholipases C Microbiol. Rev. 57 1993 347 366
    • (1993) Microbiol. Rev. , vol.57 , pp. 347-366
    • Titball, R.W.1
  • 2
    • 0028804183 scopus 로고
    • Toxins of Clostridium perfringens
    • J. Sakurai Toxins of Clostridium perfringens Rev. Med. Microbiol. 6 1995 175 185
    • (1995) Rev. Med. Microbiol. , vol.6 , pp. 175-185
    • Sakurai, J.1
  • 3
    • 14944352775 scopus 로고    scopus 로고
    • Clostridium perfringens alpha-toxin: Characterization and mode of action
    • J. Sakurai, M. Nagahama, and M. Oda Clostridium perfringens alpha-toxin: characterization and mode of action J. Biochem. (Tokyo) 136 2004 569 574
    • (2004) J. Biochem. (Tokyo) , vol.136 , pp. 569-574
    • Sakurai, J.1    Nagahama, M.2    Oda, M.3
  • 4
    • 0022542445 scopus 로고
    • Excitatory effect of Clostridium perfringens alpha toxin on the rat isolated aorta
    • Y. Fujii, S. Nomura, Y. Oshita, and J. Sakurai Excitatory effect of Clostridium perfringens alpha toxin on the rat isolated aorta Br. J. Pharmacol. 88 1986 531 539
    • (1986) Br. J. Pharmacol. , vol.88 , pp. 531-539
    • Fujii, Y.1    Nomura, S.2    Oshita, Y.3    Sakurai, J.4
  • 5
    • 0024524723 scopus 로고
    • Contraction of the rat isolated aorta caused by Clostridium perfringens alpha toxin (phospholipase C): Evidence for the involvement of arachidonic acid metabolism
    • Y. Fujii, and J. Sakurai Contraction of the rat isolated aorta caused by Clostridium perfringens alpha toxin (phospholipase C): evidence for the involvement of arachidonic acid metabolism Br. J. Pharmacol. 97 1989 119 124
    • (1989) Br. J. Pharmacol. , vol.97 , pp. 119-124
    • Fujii, Y.1    Sakurai, J.2
  • 6
    • 0025262045 scopus 로고
    • Contraction induced by Clostridium perfringens alpha toxin in the isolated rat ileum
    • J. Sakurai, Y. Fujii, and M. Shirotani Contraction induced by Clostridium perfringens alpha toxin in the isolated rat ileum Toxicon 28 1990 411 418
    • (1990) Toxicon , vol.28 , pp. 411-418
    • Sakurai, J.1    Fujii, Y.2    Shirotani, M.3
  • 7
    • 0027305710 scopus 로고
    • Evidence for coupling of Clostridium perfringens alpha-toxin-induced hemolysis to stimulated phosphatidic acid formation in rabbit erythrocytes
    • J. Sakurai, S. Ohci, and H. Tanaka Evidence for coupling of Clostridium perfringens alpha-toxin-induced hemolysis to stimulated phosphatidic acid formation in rabbit erythrocytes Infect. Immun. 61 1993 3711 3718
    • (1993) Infect. Immun. , vol.61 , pp. 3711-3718
    • Sakurai, J.1    Ohci, S.2    Tanaka, H.3
  • 8
    • 0028008791 scopus 로고
    • Regulation of Clostridium perfringens alpha-toxin-activated phospholipase C in rabbit erythrocyte membranes
    • J. Sakurai, S. Ohci, and H. Tanaka Regulation of Clostridium perfringens alpha-toxin-activated phospholipase C in rabbit erythrocyte membranes Infect. Immun. 62 1994 717 721
    • (1994) Infect. Immun. , vol.62 , pp. 717-721
    • Sakurai, J.1    Ohci, S.2    Tanaka, H.3
  • 9
    • 1842425716 scopus 로고    scopus 로고
    • Clostridium perfringens alpha-toxin activates the sphingomyelin metabolism system in sheep erythrocytes
    • S. Ochi, M. Oda, H. Matsuda, S. Ikari, and J. Sakurai Clostridium perfringens alpha-toxin activates the sphingomyelin metabolism system in sheep erythrocytes J. Biol. Chem. 279 2004 12181 12189
    • (2004) J. Biol. Chem. , vol.279 , pp. 12181-12189
    • Ochi, S.1    Oda, M.2    Matsuda, H.3    Ikari, S.4    Sakurai, J.5
  • 10
    • 0024578787 scopus 로고
    • Dissociation of various biological activities of Clostridium perfringens alpha toxin by chemical modification
    • J. Sakurai, Y. Fujii, K. Torii, and K. Kobayashi Dissociation of various biological activities of Clostridium perfringens alpha toxin by chemical modification Toxicon 27 1989 317 323
    • (1989) Toxicon , vol.27 , pp. 317-323
    • Sakurai, J.1    Fujii, Y.2    Torii, K.3    Kobayashi, K.4
  • 14
    • 0028916854 scopus 로고
    • Site-directed mutagenesis of histidine residues in Clostridium perfringens alpha toxin
    • M. Nagahama, Y. Okagawa, T. Nakayama, E. Nishioka, and J. Sakurai Site-directed mutagenesis of histidine residues in Clostridium perfringens alpha toxin J. Bacteriol. 177 1995 1179 1185
    • (1995) J. Bacteriol. , vol.177 , pp. 1179-1185
    • Nagahama, M.1    Okagawa, Y.2    Nakayama, T.3    Nishioka, E.4    Sakurai, J.5
  • 15
    • 0030859334 scopus 로고    scopus 로고
    • Site-specific mutagenesis of Clostridium perfringens alpha-toxin: Replacement of Asp-56, Asp-130, or Glu-152 causes loss of enzymatic and hemolytic activities
    • M. Nagahama, T. Nakayama, K. Michiue, and J. Sakurai Site-specific mutagenesis of Clostridium perfringens alpha-toxin: replacement of Asp-56, Asp-130, or Glu-152 causes loss of enzymatic and hemolytic activities Infect. Immun. 65 1997 3489 3492
    • (1997) Infect. Immun. , vol.65 , pp. 3489-3492
    • Nagahama, M.1    Nakayama, T.2    Michiue, K.3    Sakurai, J.4
  • 16
    • 0027303379 scopus 로고
    • New perspective on zinc biochemistry: Cocatalytic sites in multi-zinc enzymes
    • B.L. Vallee, and D.S. Auld New perspective on zinc biochemistry: cocatalytic sites in multi-zinc enzymes Biochemistry 32 1993 6493 6500
    • (1993) Biochemistry , vol.32 , pp. 6493-6500
    • Vallee, B.L.1    Auld, D.S.2
  • 17
    • 0029909653 scopus 로고    scopus 로고
    • Membrane-penetrating domain of streptolysin O identified by cysteine scanning mutagenesis
    • M. Palmer, P. Saweljew, I. Vulicevic, A. Valeva, M. Kehoe, and S. Bhakdi Membrane-penetrating domain of streptolysin O identified by cysteine scanning mutagenesis J. Biol. Chem. 271 1996 26664 26667
    • (1996) J. Biol. Chem. , vol.271 , pp. 26664-26667
    • Palmer, M.1    Saweljew, P.2    Vulicevic, I.3    Valeva, A.4    Kehoe, M.5    Bhakdi, S.6
  • 18
    • 0032514655 scopus 로고    scopus 로고
    • Identification of a membrane-spanning domain of the thiol-activated pore-forming toxin Clostridium perfringens perfringolysin O: An alpha-helical to beta-sheet transition identified by fluorescence spectroscopy
    • L.A. Shepard, A.P. Heuck, B.D. Hamman, J. Rossjohn, M.W. Parker, K.R. Ryan, A.E. Johnson, and R.K. Tweten Identification of a membrane-spanning domain of the thiol-activated pore-forming toxin Clostridium perfringens perfringolysin O: an alpha-helical to beta-sheet transition identified by fluorescence spectroscopy Biochemistry 37 1998 14563 14574
    • (1998) Biochemistry , vol.37 , pp. 14563-14574
    • Shepard, L.A.1    Heuck, A.P.2    Hamman, B.D.3    Rossjohn, J.4    Parker, M.W.5    Ryan, K.R.6    Johnson, A.E.7    Tweten, R.K.8
  • 19
    • 0036034828 scopus 로고    scopus 로고
    • Role of the C-domain in the biological activities of Clostridium perfringens alpha-toxin
    • M. Nagahama, M. Mukai, S. Morimitsu, S. Ochi, and J. Sakurai Role of the C-domain in the biological activities of Clostridium perfringens alpha-toxin Microbiol. Immunol. 46 2002 647 655
    • (2002) Microbiol. Immunol. , vol.46 , pp. 647-655
    • Nagahama, M.1    Mukai, M.2    Morimitsu, S.3    Ochi, S.4    Sakurai, J.5
  • 20
    • 0032963482 scopus 로고    scopus 로고
    • Clostridium perfringens beta-toxin is sensitive to thiol-group modification but does not require a thiol group for lethal activity
    • M. Nagahama, A. Kihara, T. Miyawaki, M. Mukai, Y. Sakaguchi, S. Ochi, and J. Sakurai Clostridium perfringens beta-toxin is sensitive to thiol-group modification but does not require a thiol group for lethal activity Biochim. Biophys. Acta 1454 1999 97 105
    • (1999) Biochim. Biophys. Acta , vol.1454 , pp. 97-105
    • Nagahama, M.1    Kihara, A.2    Miyawaki, T.3    Mukai, M.4    Sakaguchi, Y.5    Ochi, S.6    Sakurai, J.7
  • 21
    • 0029986712 scopus 로고    scopus 로고
    • Membrane-damaging action of Clostridium perfringens alpha-toxin on phospholipid liposomes
    • M. Nagahama, K. Michiue, and J. Sakurai Membrane-damaging action of Clostridium perfringens alpha-toxin on phospholipid liposomes Biochim. Biophys. Acta 1280 1996 120 126
    • (1996) Biochim. Biophys. Acta , vol.1280 , pp. 120-126
    • Nagahama, M.1    Michiue, K.2    Sakurai, J.3
  • 22
    • 0029924449 scopus 로고    scopus 로고
    • Molecular architecture of a toxin pore: A 15-residue sequence lines the transmembrane channel of staphylococcal alpha-toxin
    • A. Valeva, A. Weisser, B. Walker, M. Kehoe, H. Bayley, S. Bhakdi, and M. Palmer Molecular architecture of a toxin pore: a 15-residue sequence lines the transmembrane channel of staphylococcal alpha-toxin EMBO J. 15 1996 1857 1864
    • (1996) EMBO J. , vol.15 , pp. 1857-1864
    • Valeva, A.1    Weisser, A.2    Walker, B.3    Kehoe, M.4    Bayley, H.5    Bhakdi, S.6    Palmer, M.7
  • 23
    • 0027379581 scopus 로고
    • Crystal structure of phospholipase C from Bacillus cereus complexed with a substrate analog
    • S. Hansen, E. Hough, L.A. Svensson, Y.L. Wong, and S.F. Martin Crystal structure of phospholipase C from Bacillus cereus complexed with a substrate analog J. Mol. Biol. 234 1993 179 187
    • (1993) J. Mol. Biol. , vol.234 , pp. 179-187
    • Hansen, S.1    Hough, E.2    Svensson, L.A.3    Wong, Y.L.4    Martin, S.F.5
  • 24
    • 0037452525 scopus 로고    scopus 로고
    • Altering substrate specificity of phosphatidylcholine-preferring phospholipase C of Bacillus cereus by random mutagenesis of the headgroup binding site
    • N.M. Antikainen, P.J. Hergenrother, M.M. Harris, W. Corbett, and S.F. Martin Altering substrate specificity of phosphatidylcholine-preferring phospholipase C of Bacillus cereus by random mutagenesis of the headgroup binding site Biochemistry 42 2003 1603 1610
    • (2003) Biochemistry , vol.42 , pp. 1603-1610
    • Antikainen, N.M.1    Hergenrother, P.J.2    Harris, M.M.3    Corbett, W.4    Martin, S.F.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.