메뉴 건너뛰기




Volumn 6, Issue 10, 2011, Pages

Relationship between localization on cellular membranes and cytotoxicity of vibrio vulnificus hemolysin

Author keywords

[No Author keywords available]

Indexed keywords

AEROLYSIN; BACTERIAL TOXIN; CELL MARKER; CHOLESTEROL; HEMOLYSIN; METHYL BETA CYCLODEXTRIN; THERMOSTABLE DIRECT HEMOLYSIN; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; BETA CYCLODEXTRIN DERIVATIVE; CYTOTOXIN; METHYL-BETA-CYCLODEXTRIN;

EID: 80054782050     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0026018     Document Type: Article
Times cited : (12)

References (29)
  • 1
    • 0025937669 scopus 로고
    • Vibrio vulnificus. Hazard on the half shell
    • Koenig KL, Mueller J, Rose T, (1991) Vibrio vulnificus. Hazard on the half shell. West J Med 155: 400-403.
    • (1991) West J Med , vol.155 , pp. 400-403
    • Koenig, K.L.1    Mueller, J.2    Rose, T.3
  • 3
    • 0034100450 scopus 로고    scopus 로고
    • Epidemiology and pathogenesis of Vibrio vulnificus
    • Strom MS, Paranjpye RN, (2000) Epidemiology and pathogenesis of Vibrio vulnificus. Microbes Infect 2: 177-188.
    • (2000) Microbes Infect , vol.2 , pp. 177-188
    • Strom, M.S.1    Paranjpye, R.N.2
  • 4
    • 0021928232 scopus 로고
    • Purification and characterization of an extracellular cytolysin produced by Vibrio vulnificus
    • Gray LD, Kreger AS, (1985) Purification and characterization of an extracellular cytolysin produced by Vibrio vulnificus. Infect Immun 48: 62-72.
    • (1985) Infect Immun , vol.48 , pp. 62-72
    • Gray, L.D.1    Kreger, A.S.2
  • 6
    • 0027320947 scopus 로고
    • Hemolytic mechanism of cytolysin produced from V. vulnificus
    • Kim HR, Rho HW, Jeong MH, Park JW, Kim JS, et al. (1993) Hemolytic mechanism of cytolysin produced from V. vulnificus. Life Sci 53: 571-577.
    • (1993) Life Sci , vol.53 , pp. 571-577
    • Kim, H.R.1    Rho, H.W.2    Jeong, M.H.3    Park, J.W.4    Kim, J.S.5
  • 7
    • 0023429534 scopus 로고
    • Mechanism of haemolysis by Vibrio vulnificus haemolysin
    • Yamanaka H, Satoh T, Katsu T, Shinoda S, (1987) Mechanism of haemolysis by Vibrio vulnificus haemolysin. J Gen Microbiol 133: 2859-2864.
    • (1987) J Gen Microbiol , vol.133 , pp. 2859-2864
    • Yamanaka, H.1    Satoh, T.2    Katsu, T.3    Shinoda, S.4
  • 8
    • 0037205960 scopus 로고    scopus 로고
    • Cholesterol induce oligomerization of Vibrio vulnificus cytolysin specifically
    • Kim BS, Kim JS, (2002) Cholesterol induce oligomerization of Vibrio vulnificus cytolysin specifically. Exp Mol Med 34: 239-242.
    • (2002) Exp Mol Med , vol.34 , pp. 239-242
    • Kim, B.S.1    Kim, J.S.2
  • 9
    • 0032438178 scopus 로고    scopus 로고
    • Engagement of GPI-linked CD48 contributes to TCR signals and cytoskeletal reorganization: a role for lipid rafts in T cell activation
    • Moran M, Miceli MC, (1998) Engagement of GPI-linked CD48 contributes to TCR signals and cytoskeletal reorganization: a role for lipid rafts in T cell activation. Immunity 9: 787-796.
    • (1998) Immunity , vol.9 , pp. 787-796
    • Moran, M.1    Miceli, M.C.2
  • 10
    • 0035851918 scopus 로고    scopus 로고
    • Vav1/Rac-dependent actin cytoskeleton reorganization is required for lipid raft clustering in T cells
    • Villalba M, Bi K, Rodriguez F, Tanaka Y, Schoenberger S, et al. (2001) Vav1/Rac-dependent actin cytoskeleton reorganization is required for lipid raft clustering in T cells. J Cell Biol 155: 331-338.
    • (2001) J Cell Biol , vol.155 , pp. 331-338
    • Villalba, M.1    Bi, K.2    Rodriguez, F.3    Tanaka, Y.4    Schoenberger, S.5
  • 11
    • 2442487900 scopus 로고    scopus 로고
    • Bacterial penetration of bladder epithelium through lipid rafts
    • Duncan MJ, Li G, Shin JS, Carson JL, Abraham SN, (2004) Bacterial penetration of bladder epithelium through lipid rafts. J Biol Chem 279: 18944-18951.
    • (2004) J Biol Chem , vol.279 , pp. 18944-18951
    • Duncan, M.J.1    Li, G.2    Shin, J.S.3    Carson, J.L.4    Abraham, S.N.5
  • 12
    • 17844381899 scopus 로고    scopus 로고
    • Bacterial invasion via lipid rafts
    • Lafont F, van der Goot FG, (2005) Bacterial invasion via lipid rafts. Cell Microbiol 7: 613-620.
    • (2005) Cell Microbiol , vol.7 , pp. 613-620
    • Lafont, F.1    van der Goot, F.G.2
  • 13
    • 0038757868 scopus 로고    scopus 로고
    • Membrane raft microdomains mediate lateral assemblies required for HIV-1 infection
    • Mañes S, del Real G, Lacalle RA, Lucas P, Gómez-Moutón C, et al. (2000) Membrane raft microdomains mediate lateral assemblies required for HIV-1 infection. EMBO Rep 1: 190-196.
    • (2000) EMBO Rep , vol.1 , pp. 190-196
    • Mañes, S.1    del Real, G.2    Lacalle, R.A.3    Lucas, P.4    Gómez-Moutón, C.5
  • 14
    • 0033055564 scopus 로고    scopus 로고
    • Detergent-insoluble glycosphingolipid/cholesterol-rich membrane domains, lipid rafts and caveolae (review)
    • Hooper NM, (1999) Detergent-insoluble glycosphingolipid/cholesterol-rich membrane domains, lipid rafts and caveolae (review). Mol Membr Biol 16: 145-156.
    • (1999) Mol Membr Biol , vol.16 , pp. 145-156
    • Hooper, N.M.1
  • 15
    • 0034707082 scopus 로고    scopus 로고
    • Insolubility of lipids in triton X-100: physical origin and relationship to sphingolipid/cholesterol membrane domains (rafts)
    • London E, Brown DA, (2000) Insolubility of lipids in triton X-100: physical origin and relationship to sphingolipid/cholesterol membrane domains (rafts). Biochim Biophys Acta 1508: 182-195.
    • (2000) Biochim Biophys Acta , vol.1508 , pp. 182-195
    • London, E.1    Brown, D.A.2
  • 16
    • 0036841874 scopus 로고    scopus 로고
    • Triton promotes domain formation in lipid raft mixtures
    • Heerklotz H, (2002) Triton promotes domain formation in lipid raft mixtures. Biophys J 83: 2693-2701.
    • (2002) Biophys J , vol.83 , pp. 2693-2701
    • Heerklotz, H.1
  • 17
    • 22744437388 scopus 로고    scopus 로고
    • Detergent-resistant membranes should not be identified with membrane rafts
    • Lichtenberg D, Goni FM, Heerklotz H, (2005) Detergent-resistant membranes should not be identified with membrane rafts. Trends Biochem Sci 30: 430-436.
    • (2005) Trends Biochem Sci , vol.30 , pp. 430-436
    • Lichtenberg, D.1    Goni, F.M.2    Heerklotz, H.3
  • 18
    • 40749123910 scopus 로고    scopus 로고
    • Lysenin: a sphingomyelin specific pore-forming toxin
    • Shogomori H, Kobayashi T, (2008) Lysenin: a sphingomyelin specific pore-forming toxin. Biochim Biophys Acta 1780: 612-618.
    • (2008) Biochim Biophys Acta , vol.1780 , pp. 612-618
    • Shogomori, H.1    Kobayashi, T.2
  • 19
    • 34250368055 scopus 로고    scopus 로고
    • Gangliosides GM1 and GM3 in the living cell membrane form clusters susceptible to cholesterol depletion and chilling
    • Fujita A, Cheng J, Hirakawa M, Furukawa K, Kusunoki S, et al. (2007) Gangliosides GM1 and GM3 in the living cell membrane form clusters susceptible to cholesterol depletion and chilling. Mol Biol Cell 18: 2112-2122.
    • (2007) Mol Biol Cell , vol.18 , pp. 2112-2122
    • Fujita, A.1    Cheng, J.2    Hirakawa, M.3    Furukawa, K.4    Kusunoki, S.5
  • 20
    • 76749161447 scopus 로고    scopus 로고
    • Association of Vibrio parahaemolyticus thermostable direct hemolysin with lipid rafts is essential for cytotoxicity but not hemolytic activity
    • Matsuda S, Kodama T, Okada N, Okayama K, Honda T, et al. (2010) Association of Vibrio parahaemolyticus thermostable direct hemolysin with lipid rafts is essential for cytotoxicity but not hemolytic activity. Infect Immun 78: 603-610.
    • (2010) Infect Immun , vol.78 , pp. 603-610
    • Matsuda, S.1    Kodama, T.2    Okada, N.3    Okayama, K.4    Honda, T.5
  • 21
    • 0032498627 scopus 로고    scopus 로고
    • A pore-forming toxin interacts with a GPI-anchored protein and causes vacuolation of the endoplasmic reticulum
    • Abrami L, Fivaz M, Glauser PE, Parton RG, van der Goot FG, (1998) A pore-forming toxin interacts with a GPI-anchored protein and causes vacuolation of the endoplasmic reticulum. J Cell Biol 140: 525-540.
    • (1998) J Cell Biol , vol.140 , pp. 525-540
    • Abrami, L.1    Fivaz, M.2    Glauser, P.E.3    Parton, R.G.4    van der Goot, F.G.5
  • 22
    • 0034733561 scopus 로고    scopus 로고
    • Channel formation by the glycosylphosphatidylinositol-anchored protein binding toxin aerolysin is not promoted by lipid rafts
    • Nelson KL, Buckley JT, (2000) Channel formation by the glycosylphosphatidylinositol-anchored protein binding toxin aerolysin is not promoted by lipid rafts. J Biol Chem 275: 19839-19843.
    • (2000) J Biol Chem , vol.275 , pp. 19839-19843
    • Nelson, K.L.1    Buckley, J.T.2
  • 23
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K, Ikonen E, (1997) Functional rafts in cell membranes. Nature 387: 569-572.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 24
    • 77956267156 scopus 로고    scopus 로고
    • Outer membrane vesicles of Vibrio vulnificus deliver cytolysin-hemolysin VvhA into epithelial cells to induce cytotoxicity
    • Kim YR, Kim BU, Kim SY, Kim CM, Na HS, et al. (2010) Outer membrane vesicles of Vibrio vulnificus deliver cytolysin-hemolysin VvhA into epithelial cells to induce cytotoxicity. Biochem Biophys Res Commun 399: 607-612.
    • (2010) Biochem Biophys Res Commun , vol.399 , pp. 607-612
    • Kim, Y.R.1    Kim, B.U.2    Kim, S.Y.3    Kim, C.M.4    Na, H.S.5
  • 25
    • 34249025819 scopus 로고    scopus 로고
    • Membrane cholesterol is required for activity of Vibrio vulnificus cytolysin
    • Yu HN, Lee YR, Park KH, Rah SY, Noh EM, et al. (2007) Membrane cholesterol is required for activity of Vibrio vulnificus cytolysin. Arch Microbiol 187: 467-473.
    • (2007) Arch Microbiol , vol.187 , pp. 467-473
    • Yu, H.N.1    Lee, Y.R.2    Park, K.H.3    Rah, S.Y.4    Noh, E.M.5
  • 26
    • 0019256456 scopus 로고
    • Streptococcal toxins (streptolysin O, streptolysin S, erythrogenic toxin)
    • Alouf JE, (1980) Streptococcal toxins (streptolysin O, streptolysin S, erythrogenic toxin). Pharmacol Ther 11: 661-717.
    • (1980) Pharmacol Ther , vol.11 , pp. 661-717
    • Alouf, J.E.1
  • 27
    • 0020029082 scopus 로고
    • Interaction of alveolysin A sulfhydryl-activated bacterial cytolytic toxin with thiol group reagents and cholesterol
    • Geoffroy C, Alouf JE, (1982) Interaction of alveolysin A sulfhydryl-activated bacterial cytolytic toxin with thiol group reagents and cholesterol. Toxicon 20: 239-241.
    • (1982) Toxicon , vol.20 , pp. 239-241
    • Geoffroy, C.1    Alouf, J.E.2
  • 28
    • 0030978914 scopus 로고    scopus 로고
    • The glycosylphosphatidylinositol-anchored surface glycoprotein Thy-1 is a receptor for the channel-forming toxin aerolysin
    • Nelson KL, Raja SM, Buckley JT, (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
    • 0027764576 scopus 로고
    • Simple purification method for a Vibrio vulnificus hemolysin by a hydrophobic column chromatography in the presence of a detergent
    • Oh EG, Tamanoi Y, Toyoda A, Usui K, Miyoshi S, et al. (1993) Simple purification method for a Vibrio vulnificus hemolysin by a hydrophobic column chromatography in the presence of a detergent. Microbiol Immunol 37: 975-978.
    • (1993) Microbiol Immunol , vol.37 , pp. 975-978
    • Oh, E.G.1    Tamanoi, Y.2    Toyoda, A.3    Usui, K.4    Miyoshi, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.