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Volumn 16, Issue 2, 2010, Pages 85-90

Temperature-dependent hemolytic activity of membrane pore-forming peptide toxin, tolaasin

Author keywords

Hemolysis; Peptide toxin; Pore formation; Pseudomonas tolaasii; Tolaasin

Indexed keywords

HEMOGLOBIN; PORE FORMING CYTOTOXIC PROTEIN; TOLAASIN; UNCLASSIFIED DRUG;

EID: 74749106588     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.1199     Document Type: Article
Times cited : (9)

References (29)
  • 3
    • 0000516886 scopus 로고
    • Isolation and biological activity of toxins produced by a Japanese strain of Pseudomonas tolaasii, the pathogen of bacterial rot of cultivated oyster mushroom
    • Shirata A, Sugaya K, Takasugi M, Monde K. Isolation and biological activity of toxins produced by a Japanese strain of Pseudomonas tolaasii, the pathogen of bacterial rot of cultivated oyster mushroom. Ann. Phytopathol. Soc. Jpn. 1995; 61: 493-502.
    • (1995) Ann. Phytopathol. Soc. Jpn , vol.61 , pp. 493-502
    • Shirata, A.1    Sugaya, K.2    Takasugi, M.3    Monde, K.4
  • 5
    • 0002259680 scopus 로고
    • Biological properties and spectrum of activity of tolaasin, a lipodepsipeptide toxin produced by themushroom pathogen Pseudomonastolaasii
    • Rainey PB, Brodey CL, Johnstone K. Biological properties and spectrum of activity of tolaasin, a lipodepsipeptide toxin produced by themushroom pathogen Pseudomonastolaasii. Physiol.Mol. Plant Pathol. 1991; 39: 57-70.
    • (1991) Physiol.Mol. Plant Pathol , vol.39 , pp. 57-70
    • Rainey, P.B.1    Brodey, C.L.2    Johnstone, K.3
  • 6
    • 0001452163 scopus 로고
    • Evidence for the involvement of the surface active properties of the extracellular toxin tolaasin in the manifestation of brown blotch disease symptoms by Pseudomonas tolaasii on Agaricus bisporus
    • Hutchison MI, Johnstone K. Evidence for the involvement of the surface active properties of the extracellular toxin tolaasin in the manifestation of brown blotch disease symptoms by Pseudomonas tolaasii on Agaricus bisporus. Physiol. Mol. Plant Pathol. 1993; 42: 373-384.
    • (1993) Physiol. Mol. Plant Pathol , vol.42 , pp. 373-384
    • Hutchison, M.I.1    Johnstone, K.2
  • 7
    • 0001765867 scopus 로고
    • Bacterial blotch disease of the cultivated mushroom is caused by an ion channel forming lipodepsipeptide toxin
    • Brodey CL, Rainey PB, Tester M, Johnstone K. Bacterial blotch disease of the cultivated mushroom is caused by an ion channel forming lipodepsipeptide toxin.Mol. Plant-Microb. Interact. 1991; 4: 407-411.
    • (1991) Mol. Plant-Microb. Interact , vol.4 , pp. 407-411
    • Brodey, C.L.1    Rainey, P.B.2    Tester, M.3    Johnstone, K.4
  • 8
    • 0142125681 scopus 로고    scopus 로고
    • Two types of ion channel formation of tolaasin, a Pseudomonas peptide toxin
    • Cho KH, Kim YK. Two types of ion channel formation of tolaasin, a Pseudomonas peptide toxin. FEMS Microbiol. Lett. 2003; 221: 221-226.
    • (2003) FEMS Microbiol. Lett , vol.221 , pp. 221-226
    • Cho, K.H.1    Kim, Y.K.2
  • 9
    • 33846647081 scopus 로고    scopus 로고
    • Purification of a pore-forming peptide toxin, tolaasin, produced by Psedomonastolaasii 6264
    • Cho KH, Kim ST, Kim YK. Purification of a pore-forming peptide toxin, tolaasin, produced by Psedomonastolaasii 6264. J. Biochem.Mol. Biol. 2007; 40: 113-118.
    • (2007) J. Biochem.Mol. Biol , vol.40 , pp. 113-118
    • Cho, K.H.1    Kim, S.T.2    Kim, Y.K.3
  • 10
    • 33645183428 scopus 로고    scopus 로고
    • Hemolytic properties of tolaasin causing the brown blotch disease on oyster mushroom
    • Cho KH, Park KS, Kim YK. Hemolytic properties of tolaasin causing the brown blotch disease on oyster mushroom. J. Kor. Soc. Agric. Chem. Biotechnol. 2000; 43: 190-195.
    • (2000) J. Kor. Soc. Agric. Chem. Biotechnol , vol.43 , pp. 190-195
    • Cho, K.H.1    Park, K.S.2    Kim, Y.K.3
  • 12
    • 0032717886 scopus 로고    scopus 로고
    • Mechanism of the binding, insertion and destabilization of phospholipid bilayer membrane by α-helix antimicrobial and cell non-selective membrane-lytic peptides
    • Shai Y. Mechanism of the binding, insertion and destabilization of phospholipid bilayer membrane by α-helix antimicrobial and cell non-selective membrane-lytic peptides. Biochim. Biophys. Acta 1999; 1462: 55-70.
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 55-70
    • Shai, Y.1
  • 13
    • 0030599455 scopus 로고    scopus 로고
    • Mechanism of action of hemolysin III from Bacillus cereus
    • Baida GE, Kuzmin NP. Mechanism of action of hemolysin III from Bacillus cereus. Biochim. Biophys. Acta 1996; 1284: 122-124.
    • (1996) Biochim. Biophys. Acta , vol.1284 , pp. 122-124
    • Baida, G.E.1    Kuzmin, N.P.2
  • 14
  • 15
    • 0015195762 scopus 로고
    • Characteristics of streptolysin O action
    • Oberley TD, Duncan JL. Characteristics of streptolysin O action. Infect. Immun. 1971; 4: 683-687.
    • (1971) Infect. Immun , vol.4 , pp. 683-687
    • Oberley, T.D.1    Duncan, J.L.2
  • 16
    • 0029004327 scopus 로고
    • Characterization of Vibrio cholerae El Tor cytolysin as an oligomerizing pore-forming toxin
    • Zitzer A, Walev I, Palmer M, Bhakdi S. Characterization of Vibrio cholerae El Tor cytolysin as an oligomerizing pore-forming toxin. Med. Microbiol. Immunol. 1995; 184: 37-44.
    • (1995) Med. Microbiol. Immunol , vol.184 , pp. 37-44
    • Zitzer, A.1    Walev, I.2    Palmer, M.3    Bhakdi, S.4
  • 17
    • 0024538224 scopus 로고
    • Effects of divalent cations and saccharides on Vibrio metschnikovii cytolysin-induced hemolysis of rabbit erythrocytes
    • Miyake M, Honda T, Miwatani T. Effects of divalent cations and saccharides on Vibrio metschnikovii cytolysin-induced hemolysis of rabbit erythrocytes. Infect. Immun. 1989; 57: 158-163.
    • (1989) Infect. Immun , vol.57 , pp. 158-163
    • Miyake, M.1    Honda, T.2    Miwatani, T.3
  • 19
    • 0027398335 scopus 로고
    • Pore formation by the sea anemone cytolysin equinatoxin II in red blood cells and model lipid membranes
    • Belmonte G, Pederzolli C, Macek P, Menestrina G. Pore formation by the sea anemone cytolysin equinatoxin II in red blood cells and model lipid membranes. J.Membr. Biol. 1993; 131: 11-22.
    • (1993) J.Membr. Biol , vol.131 , pp. 11-22
    • Belmonte, G.1    Pederzolli, C.2    Macek, P.3    Menestrina, G.4
  • 20
    • 0017289510 scopus 로고
    • Evidence for a one-hit theory in the immune bactericidal reaction and demonstration of a multi-hit response for hemolysis by streptolysin O and Clostridium perfringens theta-toxin
    • Inoue K, Akiyama Y, Kinoshita T, Higasho Y, Amano T. Evidence for a one-hit theory in the immune bactericidal reaction and demonstration of a multi-hit response for hemolysis by streptolysin O and Clostridium perfringens theta-toxin. Infect. Immun. 1976; 13: 337-344.
    • (1976) Infect. Immun , vol.13 , pp. 337-344
    • Inoue, K.1    Akiyama, Y.2    Kinoshita, T.3    Higasho, Y.4    Amano, T.5
  • 21
    • 0021844372 scopus 로고
    • Purification and characterization of an extracellular cytolysin produced by Vibrio damsela
    • Kothary MH, Kreger AS. Purification and characterization of an extracellular cytolysin produced by Vibrio damsela. Infect. Immun. 1985; 49: 25-31.
    • (1985) Infect. Immun , vol.49 , pp. 25-31
    • Kothary, M.H.1    Kreger, A.S.2
  • 23
    • 0019772493 scopus 로고
    • Effect of streptolysin S on liposomes; influence of membrane lipid composition on toxin action
    • Duncan JL, Buckingham L. Effect of streptolysin S on liposomes; influence of membrane lipid composition on toxin action. Biochim. Biophys. Acta 1981; 648: 6-12.
    • (1981) Biochim. Biophys. Acta , vol.648 , pp. 6-12
    • Duncan, J.L.1    Buckingham, L.2
  • 24
    • 0023429534 scopus 로고
    • Mechanism of hemolysis by Vibrio vulnificus haemolysin
    • Yamanaka H, Satoh T, Katsu T, Shinoda S. Mechanism of hemolysis by Vibrio vulnificus haemolysin. J. Gen.Microbiol. 1987; 133: 2859-2864.
    • (1987) J. Gen.Microbiol , vol.133 , pp. 2859-2864
    • Yamanaka, H.1    Satoh, T.2    Katsu, T.3    Shinoda, S.4
  • 25
    • 0026631525 scopus 로고
    • Influence of membrane fluidity on the assembly of Staphylococcus aureus alpha-toxin, a channel-forming protein, in liposome membrane
    • Tomita T, Watanabe M, Yasuda T. Influence of membrane fluidity on the assembly of Staphylococcus aureus alpha-toxin, a channel-forming protein, in liposome membrane. J. Biol. Chem. 1992; 267: 13391-13397.
    • (1992) J. Biol. Chem , vol.267 , pp. 13391-13397
    • Tomita, T.1    Watanabe, M.2    Yasuda, T.3
  • 27
    • 0024463403 scopus 로고
    • Propranolol-induced alterations in rat erythrocyte membrane fluidity and apparent phase-transition temperatures. a depth-dependent process
    • Weitman SD, Phelan AM, Lech JJ, Lange DG. Propranolol-induced alterations in rat erythrocyte membrane fluidity and apparent phase-transition temperatures. a depth-dependent process. Biochem. Pharmacol. 1989; 38: 2949-2955.
    • (1989) Biochem. Pharmacol , vol.38 , pp. 2949-2955
    • Weitman, S.D.1    Phelan, A.M.2    Lech, J.J.3    Lange, D.G.4
  • 28
    • 0021928232 scopus 로고
    • Purification and characterization of an extracellular cytolysin produced by Vibrio vulnificus
    • Gray LD, Kreger AS. Purification and characterization of an extracellular cytolysin produced by Vibrio vulnificus. Infect. Immun. 1985; 48: 62-72.
    • (1985) Infect. Immun , vol.48 , pp. 62-72
    • Gray, L.D.1    Kreger, A.S.2
  • 29
    • 33750500720 scopus 로고    scopus 로고
    • WLIP and tolaasin I, lipodepsipeptides from Pseudomonas reactans and Pseudomonas tolaasii, permeabilise model membranes
    • Coraiola M, Cantore PL, Lazzaroni S, Evidente A, Iacobellis NS, Serra MD.WLIP and tolaasin I, lipodepsipeptides from Pseudomonas reactans and Pseudomonas tolaasii, permeabilise model membranes. Biochim. Biophys. Acta 2006; 1758: 1713-1722.
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1713-1722
    • Coraiola, M.1    Cantore, P.L.2    Lazzaroni, S.3    Evidente, A.4    Iacobellis, N.S.5    Serra, M.D.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.