메뉴 건너뛰기




Volumn 4, Issue 1, 2013, Pages

Structural and functional analysis of the pore-forming toxin NetB from clostridium perfringens

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA HEMOLYSIN; BACTERIAL TOXIN; MEMBRANE RECEPTOR; MONOMER; NETB TOXIN; UNCLASSIFIED DRUG; CATION; ENTEROTOXIN; MUTANT PROTEIN; NETB PROTEIN, CLOSTRIDIUM PERFRINGENS;

EID: 84874618304     PISSN: 21612129     EISSN: 21507511     Source Type: Journal    
DOI: 10.1128/mBio.00019-13     Document Type: Article
Times cited : (58)

References (54)
  • 5
    • 33645978129 scopus 로고    scopus 로고
    • The mechanism of pore formation by bacterial toxins
    • Tilley SJ, Saibil HR. 2006. The mechanism of pore formation by bacterial toxins. Curr. Opin. Struct. Biol. 16:230-236.
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 230-236
    • Tilley, S.J.1    Saibil, H.R.2
  • 7
    • 3542993232 scopus 로고    scopus 로고
    • Clostridium perfringens epsilon-toxin shows structural similarity to the pore-forming toxin aerolysin
    • Cole AR, Gibert M, Popoff M, Moss DS, Titball RW, Basak AK. 2004. Clostridium perfringens epsilon-toxin shows structural similarity to the pore-forming toxin aerolysin. Nat. Struct. Mol. Biol. 11:797-798.
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 797-798
    • Cole, A.R.1    Gibert, M.2    Popoff, M.3    Moss, D.S.4    Titball, R.W.5    Basak, A.K.6
  • 8
    • 81555195262 scopus 로고    scopus 로고
    • Epsilon toxin: A fascinating pore-forming toxin
    • Popoff MR. 2011. Epsilon toxin: a fascinating pore-forming toxin. FEBS J. 278:4602-4615.
    • (2011) FEBS J. , vol.278 , pp. 4602-4615
    • Popoff, M.R.1
  • 10
    • 0030447720 scopus 로고    scopus 로고
    • Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore
    • Song L, Hobaugh MR, Shustak C, Cheley S, Bayley H, Gouaux JE. 1996. Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore. Science 274:1859-1866.
    • (1996) Science , vol.274 , pp. 1859-1866
    • Song, L.1    Hobaugh, M.R.2    Shustak, C.3    Cheley, S.4    Bayley, H.5    Gouaux, J.E.6
  • 11
    • 4544341370 scopus 로고    scopus 로고
    • Bacterial two-component and heteroheptameric pore-forming cytolytic toxins: Structures, pore-forming mechanism, and organization of the genes
    • Kaneko J, Kamio Y. 2004. Bacterial two-component and heteroheptameric pore-forming cytolytic toxins: structures, pore-forming mechanism, and organization of the genes. Biosci. Biotechnol. Biochem. 68:981-1003.
    • (2004) Biosci. Biotechnol. Biochem. , vol.68 , pp. 981-1003
    • Kaneko, J.1    Kamio, Y.2
  • 13
    • 0035313528 scopus 로고    scopus 로고
    • CytK toxin of Bacillus cereus forms pores in planar lipid bilayers and is cytotoxic to intestinal epithelia
    • Hardy SP, Lund T, Granum PE. 2001. CytK toxin of Bacillus cereus forms pores in planar lipid bilayers and is cytotoxic to intestinal epithelia. FEMS Microbiol. Lett. 197:47-51.
    • (2001) FEMS Microbiol. Lett. , vol.197 , pp. 47-51
    • Hardy, S.P.1    Lund, T.2    Granum, P.E.3
  • 14
    • 0141703462 scopus 로고    scopus 로고
    • Biological activities and pore formation of Clostridium perfringens beta toxin in HL 60 cells
    • Nagahama M, Hayashi S, Morimitsu S, Sakurai J. 2003. Biological activities and pore formation of Clostridium perfringens beta toxin in HL 60 cells. J. Biol. Chem. 278:36934-36941.
    • (2003) J. Biol. Chem. , vol.278 , pp. 36934-36941
    • Nagahama, M.1    Hayashi, S.2    Morimitsu, S.3    Sakurai, J.4
  • 16
    • 79952082941 scopus 로고    scopus 로고
    • NetB, a poreforming toxin from necrotic enteritis strains of Clostridium perfringens
    • Keyburn AL, Bannam TL, Moore RJ, Rood JI. 2010. NetB, a poreforming toxin from necrotic enteritis strains of Clostridium perfringens. Toxins (Basel) 2:1913-1927.
    • (2010) Toxins (Basel) , vol.2 , pp. 1913-1927
    • Keyburn, A.L.1    Bannam, T.L.2    Moore, R.J.3    Rood, J.I.4
  • 17
    • 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
    • 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.
    • (2006) J. Biol. Chem. , vol.281 , pp. 2195-2204
    • Jayasinghe, L.1    Miles, G.2    Bayley, H.3
  • 18
    • 0032932083 scopus 로고    scopus 로고
    • Crystal structure of staphylococcal LukF delineates conformational changes accompanying formation of a transmembrane channel
    • 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.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 134-140
    • Olson, R.1    Nariya, H.2    Yokota, K.3    Kamio, Y.4    Gouaux, E.5
  • 19
  • 20
    • 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
    • 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.
    • (2004) Protein Sci. , vol.13 , pp. 1503-1511
    • Galdiero, S.1    Gouaux, E.2
  • 21
    • 0029125825 scopus 로고
    • Key residues for membrane binding, oligomerization, and pore forming activity of staphylococcal alphahemolysin identified by cysteine scanning mutagenesis and targeted chemical modification
    • Walker B, Bayley H. 1995. Key residues for membrane binding, oligomerization, and pore forming activity of staphylococcal alphahemolysin identified by cysteine scanning mutagenesis and targeted chemical modification. J. Biol. Chem. 270:23065-23071.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23065-23071
    • Walker, B.1    Bayley, H.2
  • 22
    • 0031887515 scopus 로고    scopus 로고
    • Site-directed mutagenesis of Clostridium perfringens beta-toxin: Expression of wild-type and mutant toxins in Bacillus subtilis
    • Steinthorsdottir V, Fridriksdottir V, Gunnarsson E, Andrésson OS. 1998. Site-directed mutagenesis of Clostridium perfringens beta-toxin: expression of wild-type and mutant toxins in Bacillus subtilis. FEMS Microbiol. Lett. 158:17-23.
    • (1998) FEMS Microbiol. Lett. , vol.158 , pp. 17-23
    • Steinthorsdottir, V.1    Fridriksdottir, V.2    Gunnarsson, E.3    Andrésson, O.S.4
  • 23
    • 0343775797 scopus 로고    scopus 로고
    • Clostridium perfringens beta-toxin forms multimeric transmembrane pores in human endothelial cells
    • Steinthorsdottir V, Halldórsson H, Andrésson OS. 2000. Clostridium perfringens beta-toxin forms multimeric transmembrane pores in human endothelial cells. Microb. Pathog. 28:45-50.
    • (2000) Microb. Pathog. , vol.28 , pp. 45-50
    • Steinthorsdottir, V.1    Halldórsson, H.2    Andrésson, O.S.3
  • 24
    • 0035179919 scopus 로고    scopus 로고
    • Synergistic effects of alpha-toxin and perfringolysin O in Clostridium perfringens-mediated gas gangrene
    • Awad MM, Ellemor DM, Boyd RL, Emmins JJ, Rood JI. 2001. Synergistic effects of alpha-toxin and perfringolysin O in Clostridium perfringens-mediated gas gangrene. Infect. Immun. 69:7904-7910.
    • (2001) Infect. Immun. , vol.69 , pp. 7904-7910
    • Awad, M.M.1    Ellemor, D.M.2    Boyd, R.L.3    Emmins, J.J.4    Rood, J.I.5
  • 25
    • 77249116209 scopus 로고    scopus 로고
    • Association between avian necrotic enteritis and Clostridium perfringens strains expressing NetB toxin
    • Keyburn AL, Yan XX, Bannam TL, Van Immerseel F, Rood JI, Moore RJ. 2010. Association between avian necrotic enteritis and Clostridium perfringens strains expressing NetB toxin. Vet. Res. 41:21. http://dx.doi.org/10.1051/vetres/2009069.
    • (2010) Vet. Res. , vol.41 , pp. 21
    • Keyburn, A.L.1    Yan, X.X.2    Bannam, T.L.3    van Immerseel, F.4    Rood, J.I.5    Moore, R.J.6
  • 26
    • 58149316218 scopus 로고    scopus 로고
    • Rethinking our understanding of the pathogenesis of necrotic enteritis in chickens
    • Van Immerseel F, Rood JI, Moore RJ, Titball RW. 2009. Rethinking our understanding of the pathogenesis of necrotic enteritis in chickens. Trends Microbiol. 17:32-36.
    • (2009) Trends Microbiol. , vol.17 , pp. 32-36
    • van Immerseel, F.1    Rood, J.I.2    Moore, R.J.3    Titball, R.W.4
  • 27
    • 0022504362 scopus 로고
    • Ionic channels formed by Staphylococcus aureus alpha-toxin: Voltage-dependent inhibition by divalent and trivalent cations
    • Menestrina G. 1986. Ionic channels formed by Staphylococcus aureus alpha-toxin: voltage-dependent inhibition by divalent and trivalent cations. J. Membr. Biol. 90:177-190.
    • (1986) J. Membr. Biol. , vol.90 , pp. 177-190
    • Menestrina, G.1
  • 28
    • 61549096565 scopus 로고    scopus 로고
    • Necrotic enteritis in chickens: A paradigm of enteric infection by Clostridium perfringens type A
    • Cooper KK, Songer JG. 2009. Necrotic enteritis in chickens: a paradigm of enteric infection by Clostridium perfringens type A. Anaerobe 15:55-60.
    • (2009) Anaerobe , vol.15 , pp. 55-60
    • Cooper, K.K.1    Songer, J.G.2
  • 32
    • 0033779406 scopus 로고    scopus 로고
    • Electrophysiological evidence for heptameric stoichiometry of ion channels formed by Staphylococcus aureus alpha-toxin in planar lipid bilayers
    • Krasilnikov OV, Merzlyak PG, Yuldasheva LN, Rodrigues CG, Bhakdi S, Valeva A. 2000. Electrophysiological evidence for heptameric stoichiometry of ion channels formed by Staphylococcus aureus alpha-toxin in planar lipid bilayers. Mol. Microbiol. 37:1372-1378.
    • (2000) Mol. Microbiol. , vol.37 , pp. 1372-1378
    • Krasilnikov, O.V.1    Merzlyak, P.G.2    Yuldasheva, L.N.3    Rodrigues, C.G.4    Bhakdi, S.5    Valeva, A.6
  • 33
    • 0033801218 scopus 로고    scopus 로고
    • Clostridium perfringens beta-toxin forms potential-dependent, cation-selective channels in lipid bilayers
    • Shatursky O, Bayles R, Rogers M, Jost BH, Songer JG, Tweten RK. 2000. Clostridium perfringens beta-toxin forms potential-dependent, cation-selective channels in lipid bilayers. Infect. Immun. 68:5546-5551.
    • (2000) Infect. Immun. , vol.68 , pp. 5546-5551
    • Shatursky, O.1    Bayles, R.2    Rogers, M.3    Jost, B.H.4    Songer, J.G.5    Tweten, R.K.6
  • 34
    • 59149098535 scopus 로고    scopus 로고
    • Clostridium perfringens delta toxin is sequence related to beta toxin, NetB, and Staphylococcus pore-forming toxins, but shows functional differences
    • Manich M, Knapp O, Gibert M, Maier E, Jolivet-Reynaud C, Geny B, Benz R, Popoff MR. 2008. Clostridium perfringens delta toxin is sequence related to beta toxin, NetB, and Staphylococcus pore-forming toxins, but shows functional differences. PLoS One 3:e3764. http://dx.doi.org /10.1371/journal.pone.0003764.
    • (2008) PLoS One , vol.3
    • Manich, M.1    Knapp, O.2    Gibert, M.3    Maier, E.4    Jolivet-Reynaud, C.5    Geny, B.6    Benz, R.7    Popoff, M.R.8
  • 36
    • 0014104040 scopus 로고
    • Composition of neutral lipids from erythrocytes of common mammals
    • Nelson GJ. 1967. Composition of neutral lipids from erythrocytes of common mammals. J. Lipid Res. 8:374-379.
    • (1967) J. Lipid Res. , vol.8 , pp. 374-379
    • Nelson, G.J.1
  • 37
    • 0017333166 scopus 로고
    • Lipids of Plasmodium lophurae, and of erythrocytes and plasma of normal and P. lophuraeinfected Pekin ducklings
    • Beach DH, Sherman IW, Holz GG, Jr. 1977. Lipids of Plasmodium lophurae, and of erythrocytes and plasma of normal and P. lophuraeinfected Pekin ducklings. J. Parasitol. 63:62-75.
    • (1977) J. Parasitol. , vol.63 , pp. 62-75
    • Beach, D.H.1    Sherman, I.W.2    Holz Jr., G.G.3
  • 38
    • 34948900954 scopus 로고    scopus 로고
    • Immunization of broiler chickens against Clostridium perfringens-induced necrotic enteritis
    • Kulkarni RR, Parreira VR, Sharif S, Prescott JF. 2007. Immunization of broiler chickens against Clostridium perfringens-induced necrotic enteritis. Clin. Vaccine Immunol. 14:1070-1077.
    • (2007) Clin. Vaccine Immunol. , vol.14 , pp. 1070-1077
    • Kulkarni, R.R.1    Parreira, V.R.2    Sharif, S.3    Prescott, J.F.4
  • 39
    • 46249090420 scopus 로고    scopus 로고
    • Recombinant attenuated Salmonella enterica serovar Typhimurium expressing the carboxy-terminal domain of alpha toxin from Clostridium perfringens induces protective responses against necrotic enteritis in chickens
    • Zekarias B, Mo H, Curtiss R, III. 2008. Recombinant attenuated Salmonella enterica serovar Typhimurium expressing the carboxy-terminal domain of alpha toxin from Clostridium perfringens induces protective responses against necrotic enteritis in chickens. Clin. Vaccine Immunol. 15:805-816.
    • (2008) Clin. Vaccine Immunol. , vol.15 , pp. 805-816
    • Zekarias, B.1    Mo, H.2    Curtiss III, R.3
  • 40
    • 84864025012 scopus 로고    scopus 로고
    • Vaccination with Clostridium perfringens recombinant proteins in combination with Montanide TM ISA 71 VG adjuvant increases protection against experimental necrotic enteritis in commercial broiler chickens
    • Jang SI, Lillehoj HS, Lee SH, Lee KW, Lillehoj EP, Hong YH, An DJ, Jeong W, Chun JE, Bertrand F, Dupuis L, Deville S, Arous JB. 2012. Vaccination with Clostridium perfringens recombinant proteins in combination with Montanide TM ISA 71 VG adjuvant increases protection against experimental necrotic enteritis in commercial broiler chickens. Vaccine 30:5401-5406.
    • (2012) Vaccine , vol.30 , pp. 5401-5406
    • Jang, S.I.1    Lillehoj, H.S.2    Lee, S.H.3    Lee, K.W.4    Lillehoj, E.P.5    Hong, Y.H.6    An, D.J.7    Jeong, W.8    Chun, J.E.9    Bertrand, F.10    Dupuis, L.11    Deville, S.12    Arous, J.B.13
  • 41
    • 0031894178 scopus 로고    scopus 로고
    • Conjugative transfer of RP4-oriT shuttle vectors from Escherichia coli to Clostridium perfringens
    • Lyras D, Rood JI. 1998. Conjugative transfer of RP4-oriT shuttle vectors from Escherichia coli to Clostridium perfringens. Plasmid 39:160-164.
    • (1998) Plasmid , vol.39 , pp. 160-164
    • Lyras, D.1    Rood, J.I.2
  • 42
    • 0024436683 scopus 로고
    • Electroporation-mediated transformation of lysostaphin-treated Clostridium perfringens
    • Scott PT, Rood JI. 1989. Electroporation-mediated transformation of lysostaphin-treated Clostridium perfringens. Gene 82:327-333.
    • (1989) Gene , vol.82 , pp. 327-333
    • Scott, P.T.1    Rood, J.I.2
  • 43
    • 0032850188 scopus 로고    scopus 로고
    • Identification of structural and functional domains of the tetracycline efflux protein TetA(P) from Clostridium perfringens
    • Bannam TL, Rood JI. 1999. Identification of structural and functional domains of the tetracycline efflux protein TetA(P) from Clostridium perfringens. Microbiology 145:2947-2955.
    • (1999) Microbiology , vol.145 , pp. 2947-2955
    • Bannam, T.L.1    Rood, J.I.2
  • 44
    • 33645471986 scopus 로고    scopus 로고
    • A family of E. coli expression vectors for laboratory scale and high throughput soluble protein production
    • Cabrita LD, Dai W, Bottomley SP. 2006. A family of E. coli expression vectors for laboratory scale and high throughput soluble protein production. BMC Biotechnol. 6:12. http://dx.doi.org/10.1186/1472-6750-6-12.
    • (2006) BMC Biotechnol. , vol.6 , pp. 12
    • Cabrita, L.D.1    Dai, W.2    Bottomley, S.P.3
  • 48
    • 0003076963 scopus 로고
    • Recent changes to the MOSFLM package for processing film and image plate data
    • Leslie AGW. 1992. Recent changes to the MOSFLM package for processing film and image plate data. Joint CCP4+ESF-EAMCB. Newsl. Proteins Crystallogr. 26:27-33.
    • (1992) Joint CCP4+ESF-EAMCB. Newsl. Proteins Crystallogr. , vol.26 , pp. 27-33
    • Leslie, A.G.W.1
  • 52
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4. 1994. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50:760-763.
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 53
    • 50249136103 scopus 로고    scopus 로고
    • Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7
    • Langer G, Cohen SX, Lamzin VS, Perrakis A. 2008. Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7. Nat. Protoc. 3:1171-1179.
    • (2008) Nat. Protoc. , vol.3 , pp. 1171-1179
    • Langer, G.1    Cohen, S.X.2    Lamzin, V.S.3    Perrakis, A.4
  • 54


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.