메뉴 건너뛰기




Volumn 108, Issue 18, 2011, Pages 7385-7390

Crystal structure of the Vibrio cholerae cytolysin heptamer reveals common features among disparate pore-forming toxins

Author keywords

Hemolysin; Membrane protein; Virulence factor; X ray crystallography

Indexed keywords

CYTOLYSIN; PHENYLALANINE; PORE FORMING CYTOTOXIC PROTEIN; TRYPTOPHAN DERIVATIVE;

EID: 79956294243     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1017442108     Document Type: Article
Times cited : (107)

References (56)
  • 1
    • 0030900285 scopus 로고    scopus 로고
    • Potent membrane-permeabilizing and cytocidal action of Vibrio cholerae cytolysin on human intestinal cells
    • Zitzer A, Wassenaar TM, Walev I, Bhakdi S (1997) Potent membrane-permeabilizing and cytocidal action of Vibrio cholerae cytolysin on human intestinal cells. Infect Immun 65:1293-1298. (Pubitemid 27146615)
    • (1997) Infection and Immunity , vol.65 , Issue.4 , pp. 1293-1298
    • Zitzer, A.1    Wassenaar, T.M.2    Walev, I.3    Bhakdi, S.4
  • 2
    • 44449114233 scopus 로고    scopus 로고
    • Pro-inflammatory feedback activation cycle evoked by attack of Vibrio cholerae cytolysin on human neutrophil granulocytes
    • DOI 10.1007/s00430-007-0061-2
    • Valeva A, et al. (2008) Pro-inflammatory feedback activation cycle evoked by attack of Vibrio cholerae cytolysin on human neutrophil granulocytes. Med Microbiol Immunol 197:285-293. (Pubitemid 351754684)
    • (2008) Medical Microbiology and Immunology , vol.197 , Issue.3 , pp. 285-293
    • Valeva, A.1    Walev, I.2    Weis, S.3    Boukhallouk, F.4    Wassenaar, T.M.5    Bhakdi, S.6
  • 3
    • 63749099761 scopus 로고    scopus 로고
    • The Vibrio cholerae cytolysin promotes chloride secretion from intact human intestinal mucosa
    • Debellis L, et al. (2009) The Vibrio cholerae cytolysin promotes chloride secretion from intact human intestinal mucosa. PLoS One 4:e5074.
    • (2009) PLoS One , vol.4
    • Debellis, L.1
  • 4
    • 70350220388 scopus 로고    scopus 로고
    • Successful small intestine colonization of adult mice by Vibrio cholerae requires ketamine anesthesia and accessory toxins
    • Olivier V, Queen J, Satchell KJ (2009) Successful small intestine colonization of adult mice by Vibrio cholerae requires ketamine anesthesia and accessory toxins. PLoS One 4:e7352.
    • (2009) PLoS One , vol.4
    • Olivier, V.1    Queen, J.2    Satchell, K.J.3
  • 6
    • 0037302443 scopus 로고    scopus 로고
    • Vibrio cholerae cytolysin is composed of an alpha-hemolysin-like core
    • DOI 10.1110/ps.0231703
    • Olson R, Gouaux E (2003) Vibrio cholerae cytolysin is composed of an alpha-hemolysinlike core. Protein Sci 12:379-383. (Pubitemid 36120351)
    • (2003) Protein Science , vol.12 , Issue.2 , pp. 379-383
    • Olson, R.1    Gouaux, E.2
  • 7
    • 0032932083 scopus 로고    scopus 로고
    • Crystal structure of staphylococcal lukF delineates conformational changes accompanying formation of a transmembrane channel
    • DOI 10.1038/5821
    • Olson R, Nariya H, Yokota K, Kamio Y, Gouaux E (1999) Crystal structure of staphylococcal LukF delineates conformational changes accompanying formation of a transmembrane channel. Nat Struct Biol 6:134-140. (Pubitemid 29069775)
    • (1999) Nature Structural Biology , vol.6 , Issue.2 , pp. 134-140
    • Olson, R.1    Nariya, H.2    Yokota, K.3    Kamio, Y.4    Gouaux, E.5
  • 8
    • 0033103175 scopus 로고    scopus 로고
    • The structure of a Staphylococcus aureus leucocidin component (LukF-PV) reveals the fold of the water-soluble species of a family of transmembrane pore-forming toxins
    • Pedelacq JD, et al. (1999) The structure of a Staphylococcus aureus leucocidin component (LukF-PV) reveals the fold of the water-soluble species of a family of transmembrane pore-forming toxins. Structure 7:277-287.
    • (1999) Structure , vol.7 , pp. 277-287
    • Pedelacq, J.D.1
  • 10
    • 0030447720 scopus 로고    scopus 로고
    • Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore
    • DOI 10.1126/science.274.5294.1859
    • Song L, et al. (1996) Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore. Science 274:1859-1866. (Pubitemid 26424757)
    • (1996) Science , vol.274 , Issue.5294 , pp. 1859-1866
    • Song, L.1    Hobaugh, M.R.2    Shustak, C.3    Cheley, S.4    Bayley, H.5    Gouaux, J.E.6
  • 11
    • 0034861304 scopus 로고    scopus 로고
    • Not as simple as just punching a hole
    • DOI 10.1016/S0041-0101(01)00151-9, PII S0041010101001519
    • Fivaz M, Abrami L, Tsitrin Y, van der Goot FG (2001) Not as simple as just punching a hole. Toxicon 39:1637-1645. (Pubitemid 32786997)
    • (2001) Toxicon , vol.39 , Issue.11 , pp. 1637-1645
    • Fivaz, M.1    Abrami, L.2    Tsitrin, Y.3    Van Der, G.F.G.4
  • 12
    • 34447291354 scopus 로고    scopus 로고
    • Anthrax toxin: Receptor binding, internalization, pore formation, and translocation
    • Young JA, Collier RJ (2007) Anthrax toxin: Receptor binding, internalization, pore formation, and translocation. Annu Rev Biochem 76:243-265.
    • (2007) Annu Rev Biochem , vol.76 , pp. 243-265
    • Young, J.A.1    Collier, R.J.2
  • 13
    • 25444452398 scopus 로고    scopus 로고
    • Cholesterol-dependent cytolysins, a family of versatile pore-forming toxins
    • Tweten RK (2005) Cholesterol-dependent cytolysins, a family of versatile pore-forming toxins. Infect Immun 73:6199-6209.
    • (2005) Infect Immun , vol.73 , pp. 6199-6209
    • Tweten, R.K.1
  • 14
    • 0033615736 scopus 로고    scopus 로고
    • The mechanism of membrane insertion for a cholesterol-dependent cytolysin: A novel paradigm for pore-forming toxins
    • DOI 10.1016/S0092-8674(00)81660-8
    • Shatursky O, et al. (1999) The mechanism of membrane insertion for a cholesterol-dependent cytolysin: A novel paradigm for pore-forming toxins. Cell 99:293-299. (Pubitemid 29519908)
    • (1999) Cell , vol.99 , Issue.3 , pp. 293-299
    • Shatursky, O.1    Heuck, A.P.2    Shepard, L.A.3    Rossjohn, J.4    Parker, M.W.5    Johnson, A.E.6    Tweten, R.K.7
  • 15
    • 0030037293 scopus 로고    scopus 로고
    • Mechanism of membrane damage by El Tor hemolysin of Vibrio cholerae O1
    • Ikigai H, Akatsuka A, Tsujiyama H, Nakae T, Shimamura T (1996) Mechanism of membrane damage by El Tor hemolysin of Vibrio cholerae O1. Infect Immun 64:2968-2973.
    • (1996) Infect Immun , vol.64 , pp. 2968-2973
    • Ikigai, H.1    Akatsuka, A.2    Tsujiyama, H.3    Nakae, T.4    Shimamura, T.5
  • 16
    • 0033556418 scopus 로고    scopus 로고
    • Oligomerization of Vibrio cholerae cytolysin yields a pentameric pore and has a dual specificity for cholesterol and sphingolipids in the target membrane
    • Zitzer A, Zitzer O, Bhakdi S, Palmer M (1999) Oligomerization of Vibrio cholerae cytolysin yields a pentameric pore and has a dual specificity for cholesterol and sphingolipids in the target membrane. J Biol Chem 274:1375-1380.
    • (1999) J Biol Chem , vol.274 , pp. 1375-1380
    • Zitzer, A.1    Zitzer, O.2    Bhakdi, S.3    Palmer, M.4
  • 17
    • 21744447839 scopus 로고    scopus 로고
    • Crystal structure of the Vibrio cholerae cytolysin (VCC) pro-toxin and its assembly into a heptameric transmembrane pore
    • DOI 10.1016/j.jmb.2005.05.045, PII S0022283605006005
    • Olson R, Gouaux E (2005) Crystal structure of the Vibrio cholerae cytolysin (VCC) pro-toxin and its assembly into a heptameric transmembrane pore. J Mol Biol 350:997-1016. (Pubitemid 40943458)
    • (2005) Journal of Molecular Biology , vol.350 , Issue.5 , pp. 997-1016
    • Olson, R.1    Gouaux, E.2
  • 18
    • 0031017025 scopus 로고    scopus 로고
    • Carbohydrate-mediated regulation of interaction of Vibrio cholerae hemolysin with erythrocyte and phospholipid vesicle
    • DOI 10.1074/jbc.272.1.162
    • Saha N, Banerjee KK (1997) Carbohydrate-mediated regulation of interaction of Vibrio cholerae hemolysin with erythrocyte and phospholipid vesicle. J Biol Chem 272:162-167. (Pubitemid 27021139)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.1 , pp. 162-167
    • Saha, N.1    Banerjee, K.K.2
  • 19
    • 0029858955 scopus 로고    scopus 로고
    • In vitro proteolytic processing and activation of the recombinant precursor of El Tor cytolysin/hemolysin (pro-HlyA) of Vibrio cholerae by soluble hemagglutinin/protease of V. cholerae, trypsin, and other proteases
    • Nagamune K, et al. (1996) In vitro proteolytic processing and activation of the recombinant precursor of El Tor cytolysin/hemolysin (pro-HlyA) of Vibrio cholerae by soluble hemagglutinin/protease of V. cholerae, trypsin, and other proteases. Infect Immun 64:4655-4658.
    • (1996) Infect Immun , vol.64 , pp. 4655-4658
    • Nagamune, K.1
  • 20
    • 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
  • 21
    • 0029240394 scopus 로고
    • An intermediate in the assembly of a pore-forming protein trapped with a genetically-engineered switch
    • Walker B, Braha O, Cheley S, Bayley H (1995) An intermediate in the assembly of a pore-forming protein trapped with a genetically-engineered switch. Chem Biol 2:99-105.
    • (1995) Chem Biol , vol.2 , pp. 99-105
    • Walker, B.1    Braha, O.2    Cheley, S.3    Bayley, H.4
  • 22
    • 0030735356 scopus 로고    scopus 로고
    • Staphylococcal alpha-toxin: Formation of the heptameric pore is partially cooperative and proceeds through multiple intermediate stages
    • DOI 10.1021/bi971075r
    • Valeva A, Palmer M, Bhakdi S (1997) Staphylococcal alpha-toxin: Formation of the heptameric pore is partially cooperative and proceeds through multiple intermediate stages. Biochemistry 36:13298-13304. (Pubitemid 27473377)
    • (1997) Biochemistry , vol.36 , Issue.43 , pp. 13298-13304
    • Valeva, A.1    Palmer, M.2    Bhakdi, S.3
  • 24
    • 72449138557 scopus 로고    scopus 로고
    • Three-dimensional structure of the detergent-solubilized Vibrio cholerae cytolysin (VCC) heptamer by electron cryomicroscopy
    • He Y, Olson R (2010) Three-dimensional structure of the detergent-solubilized Vibrio cholerae cytolysin (VCC) heptamer by electron cryomicroscopy. J Struct Biol 169:6-13.
    • (2010) J Struct Biol , vol.169 , pp. 6-13
    • He, Y.1    Olson, R.2
  • 25
    • 0036432233 scopus 로고    scopus 로고
    • Interaction of the Vibrio cholerae cytolysin (VCC) with cholesterol, some cholesterol esters, and cholesterol derivatives: A TEM study
    • DOI 10.1016/S1047-8477(02)00563-4, PII S1047847702005634
    • Harris JR, et al. (2002) Interaction of the Vibrio cholerae cytolysin (VCC) with cholesterol, some cholesterol esters, and cholesterol derivatives: A TEM study. J Struct Biol 139:122-135. (Pubitemid 35333802)
    • (2002) Journal of Structural Biology , vol.139 , Issue.2 , pp. 122-135
    • Harris, J.R.1    Bhakdi, S.2    Meissner, U.3    Scheffler, D.4    Bittman, R.5    Li, G.6    Zitzer, A.7    Palmer, M.8
  • 26
    • 0025262173 scopus 로고
    • Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): A vehicle for direct determination of three-dimensional structure
    • Hendrickson WA, Horton JR, LeMaster DM (1990) Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): A vehicle for direct determination of three-dimensional structure. EMBO J 9:1665-1672.
    • (1990) EMBO J , vol.9 , pp. 1665-1672
    • Hendrickson, W.A.1    Horton, J.R.2    LeMaster, D.M.3
  • 27
    • 0031734465 scopus 로고    scopus 로고
    • Roll out the barrel
    • Gouaux E (1998) Roll out the barrel. Nat Struct Biol 5:931-932.
    • (1998) Nat Struct Biol , vol.5 , pp. 931-932
    • Gouaux, E.1
  • 30
    • 0029741086 scopus 로고    scopus 로고
    • HlyA hemolysin of Vibrio cholerae O1 biotype E1 Tor. Identification of the hemolytic complex and evidence for the formation of anion-selective ion-permeable channels
    • Menzl K, Maier E, Chakraborty T, Benz R (1996) HlyA hemolysin of Vibrio cholerae O1 biotype E1 Tor. Identification of the hemolytic complex and evidence for the formation of anion-selective ion-permeable channels. Eur J Biochem 240:646-654.
    • (1996) Eur J Biochem , vol.240 , pp. 646-654
    • Menzl, K.1    Maier, E.2    Chakraborty, T.3    Benz, R.4
  • 31
    • 29944444756 scopus 로고    scopus 로고
    • A molecular model of the Vibrio cholerae cytolysin transmembrane pore
    • DOI 10.1016/j.toxicon.2005.09.007, PII S0041010105003375
    • Pantano S, Montecucco C (2006) A molecular model of the Vibrio cholerae cytolysin transmembrane pore. Toxicon 47:35-40. (Pubitemid 43042393)
    • (2006) Toxicon , vol.47 , Issue.1 , pp. 35-40
    • Pantano, S.1    Montecucco, C.2
  • 32
    • 0033453691 scopus 로고    scopus 로고
    • Ion channels of biological membranes: Prediction of single channel conductance
    • Ranatunga KM, Adcock C, Kerr ID, Smith GR, Sansom MS (1999) Ion channels of biological membranes: Prediction of single channel conductance. Theor Chem Acc 101:97-102.
    • (1999) Theor Chem Acc , vol.101 , pp. 97-102
    • Ranatunga, K.M.1    Adcock, C.2    Kerr, I.D.3    Smith, G.R.4    Sansom, M.S.5
  • 33
    • 73649123850 scopus 로고    scopus 로고
    • The aromatic ring of phenylalanine 334 is essential for oligomerization of Vibrio vulnificus hemolysin
    • Kashimoto T, et al. (2009) The aromatic ring of phenylalanine 334 is essential for oligomerization of Vibrio vulnificus hemolysin. J Bacteriol 192:568-574.
    • (2009) J Bacteriol , vol.192 , pp. 568-574
    • Kashimoto, T.1
  • 34
    • 33947223487 scopus 로고    scopus 로고
    • Pore formation by Vibrio cholerae cytolysin requires cholesterol in both monolayers of the target membrane
    • DOI 10.1016/j.biochi.2006.12.003, PII S0300908406003191
    • Krasilnikov OV, et al. (2007) Pore formation by Vibrio cholerae cytolysin requires cholesterol in both monolayers of the target membrane. Biochimie 89:271-277. (Pubitemid 46436266)
    • (2007) Biochimie , vol.89 , Issue.3 , pp. 271-277
    • Krasilnikov, O.V.1    Merzlyak, P.G.2    Lima, V.L.M.3    Zitzer, A.O.4    Valeva, A.5    Yuldasheva, L.N.6
  • 35
    • 33644859965 scopus 로고    scopus 로고
    • Role of the amino latch of staphylococcal alpha-hemolysin in pore formation: A co-operative interaction between the N terminus and position 217
    • DOI 10.1074/jbc.M510841200
    • Jayasinghe L, Miles G, Bayley H (2006) Role of the amino latch of staphylococcal alpha-hemolysin in pore formation: A co-operative interaction between the N terminus and position 217. J Biol Chem 281:2195-2204. (Pubitemid 43845810)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.4 , pp. 2195-2204
    • Jayasinghe, L.1    Miles, G.2    Bayley, H.3
  • 36
    • 0029126941 scopus 로고
    • Interactions between residues in staphylococcal alpha-hemolysin revealed by reversion mutagenesis
    • Panchal RG, Bayley H (1995) Interactions between residues in staphylococcal alpha-hemolysin revealed by reversion mutagenesis. J Biol Chem 270:23072-23076.
    • (1995) J Biol Chem , vol.270 , pp. 23072-23076
    • Panchal, R.G.1    Bayley, H.2
  • 37
    • 0033523767 scopus 로고    scopus 로고
    • Plasma membrane microdomains act as concentration platforms to facilitate intoxication by aerolysin
    • DOI 10.1083/jcb.147.1.175
    • Abrami L, van Der Goot FG (1999) Plasma membrane microdomains act as concentration platforms to facilitate intoxication by aerolysin. J Cell Biol 147:175-184. (Pubitemid 30211805)
    • (1999) Journal of Cell Biology , vol.147 , Issue.1 , pp. 175-184
    • Abrami, L.1    Van Der, G.F.G.2
  • 38
    • 0037415611 scopus 로고    scopus 로고
    • Anthrax toxin triggers endocytosis of its receptor via a lipid raft-mediated clathrin-dependent process
    • DOI 10.1083/jcb.200211018
    • Abrami L, Liu S, Cosson P, Leppla SH, van der Goot FG (2003) Anthrax toxin triggers endocytosis of its receptor via a lipid raft-mediated clathrin-dependent process. J Cell Biol 160:321-328. (Pubitemid 36182723)
    • (2003) Journal of Cell Biology , vol.160 , Issue.3 , pp. 321-328
    • Abrami, L.1    Liu, S.2    Cosson, P.3    Leppla, S.H.4    Van Der, G.F.G.5
  • 39
    • 77749292162 scopus 로고    scopus 로고
    • Only two amino acids are essential for cytolytic toxin recognition of cholesterol at the membrane surface
    • Farrand AJ, LaChapelle S, Hotze EM, Johnson AE, Tweten RK (2010) Only two amino acids are essential for cytolytic toxin recognition of cholesterol at the membrane surface. Proc Natl Acad Sci USA 107:4341-4346.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 4341-4346
    • Farrand, A.J.1    LaChapelle, S.2    Hotze, E.M.3    Johnson, A.E.4    Tweten, R.K.5
  • 40
    • 2442650172 scopus 로고    scopus 로고
    • High resolution crystallographic studies of alpha-hemolysin-phospholipid complexes define heptamer-lipid head group interactions: Implication for understanding protein-lipid interactions
    • DOI 10.1110/ps.03561104
    • Galdiero S, Gouaux E (2004) High resolution crystallographic studies of alpha-hemolysin-phospholipid complexes define heptamer-lipid head group interactions: Implication for understanding protein-lipid interactions. Protein Sci 13:1503-1511. (Pubitemid 38669238)
    • (2004) Protein Science , vol.13 , Issue.6 , pp. 1503-1511
    • Galdiero, S.1    Gouaux, E.2
  • 41
    • 74849118341 scopus 로고    scopus 로고
    • Lipid rafts as a membrane-organizing principle
    • Lingwood D, Simons K (2010) Lipid rafts as a membrane-organizing principle. Science 327:46-50.
    • (2010) Science , vol.327 , pp. 46-50
    • Lingwood, D.1    Simons, K.2
  • 43
    • 77649244670 scopus 로고    scopus 로고
    • Three-dimensional structure of the anthrax toxin pore inserted into lipid nanodiscs and lipid vesicles
    • Katayama H, et al. (2010) Three-dimensional structure of the anthrax toxin pore inserted into lipid nanodiscs and lipid vesicles. Proc Natl Acad Sci USA 107:3453-3457.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 3453-3457
    • Katayama, H.1
  • 47
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Otwinowski Z, Minor W (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276:307-326. (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 48
    • 37549039510 scopus 로고    scopus 로고
    • A short history of SHELX
    • Sheldrick GM (2008) A short history of SHELX. Acta Crystallogr A 64:112-122.
    • (2008) Acta Crystallogr A , vol.64 , pp. 112-122
    • Sheldrick, G.M.1
  • 49
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4 (1994) The CCP4 suite: Programs for protein crystallography. Acta Crystallogr D 50:760-763.
    • (1994) Acta Crystallogr D , vol.50 , Issue.4 , pp. 760-763
    • Project, C.C.1
  • 53
    • 34547592557 scopus 로고    scopus 로고
    • MolProbity: All-atom contacts and structure validation for proteins and nucleic acids
    • Davis IW, et al. (2007) MolProbity: All-atom contacts and structure validation for proteins and nucleic acids. Nucleic Acids Res 35:W375-383.
    • (2007) Nucleic Acids Res , vol.35
    • Davis, I.W.1
  • 54
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brünger AT, et al. (1998) Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr D 54:905-921.
    • (1998) Acta Crystallogr D , vol.54 , pp. 905-921
    • Brünger, A.T.1
  • 56
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera - A visualization system for exploratory research and analysis
    • Pettersen EF, et al. (2004) UCSF Chimera - A visualization system for exploratory research and analysis. J Comput Chem 25:1605-1612.
    • (2004) J Comput Chem , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.