메뉴 건너뛰기




Volumn 8, Issue 10, 2013, Pages

The Bacillus cereus Hbl and Nhe Tripartite Enterotoxin Components Assemble Sequentially on the Surface of Target Cells and Are Not Interchangeable

Author keywords

[No Author keywords available]

Indexed keywords

ENTEROTOXIN; ENTEROTOXIN HBL; ENTEROTOXIN NHE; UNCLASSIFIED DRUG;

EID: 84885733644     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0076955     Document Type: Article
Times cited : (81)

References (51)
  • 2
    • 0017803024 scopus 로고
    • Prevalence of Bacillus cereus in the faeces of healthy adults
    • Ghosh AC, (1978) Prevalence of Bacillus cereus in the faeces of healthy adults. J Hyg (Lond) 80: 233-236.
    • (1978) J Hyg (Lond) , vol.80 , pp. 233-236
    • Ghosh, A.C.1
  • 3
    • 0036128355 scopus 로고    scopus 로고
    • Genome structure and evolution of the Bacillus cereus group
    • Kolsto AB, Lereclus D, Mock M, (2002) Genome structure and evolution of the Bacillus cereus group. Curr Top Microbiol Immunol 264: 95-108.
    • (2002) Curr Top Microbiol Immunol , vol.264 , pp. 95-108
    • Kolsto, A.B.1    Lereclus, D.2    Mock, M.3
  • 4
    • 70349481688 scopus 로고    scopus 로고
    • Literature review on the safety of Toyocerin, a non-toxigenic and non-pathogenic Bacillus cereus var. toyoi preparation
    • Williams LD, Burdock GA, Jimenez G, Castillo M, (2009) Literature review on the safety of Toyocerin, a non-toxigenic and non-pathogenic Bacillus cereus var. toyoi preparation. Regul Toxicol Pharmacol 55: 236-246.
    • (2009) Regul Toxicol Pharmacol , vol.55 , pp. 236-246
    • Williams, L.D.1    Burdock, G.A.2    Jimenez, G.3    Castillo, M.4
  • 6
    • 10444239437 scopus 로고    scopus 로고
    • Bacillus cereus, the causative agent of an emetic type of food-borne illness
    • Ehling-Schulz M, Fricker M, Scherer S, (2004) Bacillus cereus, the causative agent of an emetic type of food-borne illness. Mol Nutr Food Res 48: 479-487.
    • (2004) Mol Nutr Food Res , vol.48 , pp. 479-487
    • Ehling-Schulz, M.1    Fricker, M.2    Scherer, S.3
  • 7
    • 77950658604 scopus 로고    scopus 로고
    • Bacillus cereus, a volatile human pathogen
    • Bottone EJ, (2010) Bacillus cereus, a volatile human pathogen. Clin Microbiol Rev 23: 382-398.
    • (2010) Clin Microbiol Rev , vol.23 , pp. 382-398
    • Bottone, E.J.1
  • 8
    • 0027517868 scopus 로고
    • Bacillus cereus and related species
    • Drobniewski FA, (1993) Bacillus cereus and related species. Clin Microbiol Rev 6: 324-338.
    • (1993) Clin Microbiol Rev , vol.6 , pp. 324-338
    • Drobniewski, F.A.1
  • 10
    • 0037009447 scopus 로고    scopus 로고
    • A cell-cell signaling peptide activates the PlcR virulence regulon in bacteria of the Bacillus cereus group
    • Slamti L, Lereclus D, (2002) A cell-cell signaling peptide activates the PlcR virulence regulon in bacteria of the Bacillus cereus group. EMBO J 21: 4550-4559.
    • (2002) EMBO J , vol.21 , pp. 4550-4559
    • Slamti, L.1    Lereclus, D.2
  • 12
    • 0033745098 scopus 로고    scopus 로고
    • A new cytotoxin from Bacillus cereus that may cause necrotic enteritis
    • Lund T, De Buyser ML, Granum PE, (2000) A new cytotoxin from Bacillus cereus that may cause necrotic enteritis. Mol Microbiol 38: 254-261.
    • (2000) Mol Microbiol , vol.38 , pp. 254-261
    • Lund, T.1    De Buyser, M.L.2    Granum, P.E.3
  • 13
    • 0030221647 scopus 로고    scopus 로고
    • Characterisation of a non-haemolytic enterotoxin complex from Bacillus cereus isolated after a foodborne outbreak
    • Lund T, Granum PE, (1996) Characterisation of a non-haemolytic enterotoxin complex from Bacillus cereus isolated after a foodborne outbreak. FEMS Microbiol Lett 141: 151-156.
    • (1996) FEMS Microbiol Lett , vol.141 , pp. 151-156
    • Lund, T.1    Granum, P.E.2
  • 14
    • 0021331647 scopus 로고
    • Isolation and some properties of an enterotoxin produced by Bacillus cereus
    • Thompson NE, Ketterhagen MJ, Bergdoll MS, Schantz EJ, (1984) Isolation and some properties of an enterotoxin produced by Bacillus cereus. Infect Immun 43: 887-894.
    • (1984) Infect Immun , vol.43 , pp. 887-894
    • Thompson, N.E.1    Ketterhagen, M.J.2    Bergdoll, M.S.3    Schantz, E.J.4
  • 15
    • 0028929005 scopus 로고
    • Extracellular virulence factors in Bacillus cereus endophthalmitis: methods and implication of involvement of hemolysin BL
    • Beecher DJ, Pulido JS, Barney NP, Wong AC, (1995) Extracellular virulence factors in Bacillus cereus endophthalmitis: methods and implication of involvement of hemolysin BL. Infect Immun 63: 632-639.
    • (1995) Infect Immun , vol.63 , pp. 632-639
    • Beecher, D.J.1    Pulido, J.S.2    Barney, N.P.3    Wong, A.C.4
  • 16
    • 42949110817 scopus 로고    scopus 로고
    • Bacillus cereus Nhe is a pore-forming toxin with structural and functional properties similar to the ClyA (HlyE, SheA) family of haemolysins, able to induce osmotic lysis in epithelia
    • Fagerlund A, Lindback T, Storset AK, Granum PE, Hardy SP, (2008) Bacillus cereus Nhe is a pore-forming toxin with structural and functional properties similar to the ClyA (HlyE, SheA) family of haemolysins, able to induce osmotic lysis in epithelia. Microbiology 154: 693-704.
    • (2008) Microbiology , vol.154 , pp. 693-704
    • Fagerlund, A.1    Lindback, T.2    Storset, A.K.3    Granum, P.E.4    Hardy, S.P.5
  • 17
    • 0036702151 scopus 로고    scopus 로고
    • Enterotoxigenic profiles of food-poisoning and food-borne Bacillus cereus strains
    • Guinebretiere MH, Broussolle V, Nguyen-The C, (2002) Enterotoxigenic profiles of food-poisoning and food-borne Bacillus cereus strains. J Clin Microbiol 40: 3053-3056.
    • (2002) J Clin Microbiol , vol.40 , pp. 3053-3056
    • Guinebretiere, M.H.1    Broussolle, V.2    Nguyen-The, C.3
  • 18
    • 33645240293 scopus 로고    scopus 로고
    • Determination of the toxic potential of Bacillus cereus isolates by quantitative enterotoxin analyses
    • Moravek M, Dietrich R, Buerk C, Broussolle V, Guinebretiere MH, et al. (2006) Determination of the toxic potential of Bacillus cereus isolates by quantitative enterotoxin analyses. FEMS Microbiol Lett 257: 293-298.
    • (2006) FEMS Microbiol Lett , vol.257 , pp. 293-298
    • Moravek, M.1    Dietrich, R.2    Buerk, C.3    Broussolle, V.4    Guinebretiere, M.H.5
  • 19
    • 0025727024 scopus 로고
    • Characterization of the components of hemolysin BL from Bacillus cereus
    • Beecher DJ, Macmillan JD, (1991) Characterization of the components of hemolysin BL from Bacillus cereus. Infect Immun 59: 1778-1784.
    • (1991) Infect Immun , vol.59 , pp. 1778-1784
    • Beecher, D.J.1    Macmillan, J.D.2
  • 20
    • 0031033049 scopus 로고    scopus 로고
    • Tripartite hemolysin BL from Bacillus cereus. Hemolytic analysis of component interactions and a model for its characteristic paradoxical zone phenomenon
    • Beecher DJ, Wong AC, (1997) Tripartite hemolysin BL from Bacillus cereus. Hemolytic analysis of component interactions and a model for its characteristic paradoxical zone phenomenon. J Biol Chem 272: 233-239.
    • (1997) J Biol Chem , vol.272 , pp. 233-239
    • Beecher, D.J.1    Wong, A.C.2
  • 22
    • 77956644756 scopus 로고    scopus 로고
    • Cytotoxicity of the Bacillus cereus Nhe enterotoxin requires specific binding order of its three exoprotein components
    • Lindback T, Hardy SP, Dietrich R, Sodring M, Didier A, et al. (2010) Cytotoxicity of the Bacillus cereus Nhe enterotoxin requires specific binding order of its three exoprotein components. Infect Immun 78: 3813-3821.
    • (2010) Infect Immun , vol.78 , pp. 3813-3821
    • Lindback, T.1    Hardy, S.P.2    Dietrich, R.3    Sodring, M.4    Didier, A.5
  • 23
    • 84876975134 scopus 로고    scopus 로고
    • Complex formation between NheB and NheC is necessary to induce cytotoxic activity by the three-component Bacillus cereus Nhe enterotoxin
    • Heilkenbrinker U, Dietrich R, Didier A, Zhu K, Lindback T, et al. (2013) Complex formation between NheB and NheC is necessary to induce cytotoxic activity by the three-component Bacillus cereus Nhe enterotoxin. PLoS One 8: e63104.
    • (2013) PLoS One , vol.8
    • Heilkenbrinker, U.1    Dietrich, R.2    Didier, A.3    Zhu, K.4    Lindback, T.5
  • 24
    • 41149147722 scopus 로고    scopus 로고
    • X-ray crystal structure of the B component of Hemolysin BL from Bacillus cereus
    • Madegowda M, Eswaramoorthy S, Burley SK, Swaminathan S, (2008) X-ray crystal structure of the B component of Hemolysin BL from Bacillus cereus. Proteins 71: 534-540.
    • (2008) Proteins , vol.71 , pp. 534-540
    • Madegowda, M.1    Eswaramoorthy, S.2    Burley, S.K.3    Swaminathan, S.4
  • 25
    • 0034695613 scopus 로고    scopus 로고
    • E. coli hemolysin E (HlyE, ClyA, SheA): X-ray crystal structure of the toxin and observation of membrane pores by electron microscopy
    • Wallace AJ, Stillman TJ, Atkins A, Jamieson SJ, Bullough PA, et al. (2000) E. coli hemolysin E (HlyE, ClyA, SheA): X-ray crystal structure of the toxin and observation of membrane pores by electron microscopy. Cell 100: 265-276.
    • (2000) Cell , vol.100 , pp. 265-276
    • Wallace, A.J.1    Stillman, T.J.2    Atkins, A.3    Jamieson, S.J.4    Bullough, P.A.5
  • 26
    • 77955901062 scopus 로고    scopus 로고
    • Hemolysin E (HlyE, ClyA, SheA) and related toxins
    • Hunt S, Green J, Artymiuk PJ, (2010) Hemolysin E (HlyE, ClyA, SheA) and related toxins. Adv Exp Med Biol 677: 116-126.
    • (2010) Adv Exp Med Biol , vol.677 , pp. 116-126
    • Hunt, S.1    Green, J.2    Artymiuk, P.J.3
  • 27
    • 66649132042 scopus 로고    scopus 로고
    • The structure of a cytolytic alpha-helical toxin pore reveals its assembly mechanism
    • Mueller M, Grauschopf U, Maier T, Glockshuber R, Ban N, (2009) The structure of a cytolytic alpha-helical toxin pore reveals its assembly mechanism. Nature 459: 726-730.
    • (2009) Nature , vol.459 , pp. 726-730
    • Mueller, M.1    Grauschopf, U.2    Maier, T.3    Glockshuber, R.4    Ban, N.5
  • 28
    • 77955284761 scopus 로고    scopus 로고
    • Mutations affecting export and activity of cytolysin A from Escherichia coli
    • Ludwig A, Volkerink G, von Rhein C, Bauer S, Maier E, et al. (2010) Mutations affecting export and activity of cytolysin A from Escherichia coli. J Bacteriol 192: 4001-4011.
    • (2010) J Bacteriol , vol.192 , pp. 4001-4011
    • Ludwig, A.1    Volkerink, G.2    von Rhein, C.3    Bauer, S.4    Maier, E.5
  • 29
    • 0242318248 scopus 로고    scopus 로고
    • Phosphatidylcholine-specific phospholipase C and sphingomyelinase activities in bacteria of the Bacillus cereus group
    • Pomerantsev AP, Kalnin KV, Osorio M, Leppla SH, (2003) Phosphatidylcholine-specific phospholipase C and sphingomyelinase activities in bacteria of the Bacillus cereus group. Infect Immun 71: 6591-6606.
    • (2003) Infect Immun , vol.71 , pp. 6591-6606
    • Pomerantsev, A.P.1    Kalnin, K.V.2    Osorio, M.3    Leppla, S.H.4
  • 31
    • 67749120325 scopus 로고    scopus 로고
    • A new minimal replicon of Bacillus anthracis plasmid pXO1
    • Pomerantsev AP, Camp A, Leppla SH, (2009) A new minimal replicon of Bacillus anthracis plasmid pXO1. J Bacteriol 191: 5134-5146.
    • (2009) J Bacteriol , vol.191 , pp. 5134-5146
    • Pomerantsev, A.P.1    Camp, A.2    Leppla, S.H.3
  • 32
    • 0141527346 scopus 로고    scopus 로고
    • Retroviral insertional mutagenesis identifies a small protein required for synthesis of diphthamide, the target of bacterial ADP-ribosylating toxins
    • Liu S, Leppla SH, (2003) Retroviral insertional mutagenesis identifies a small protein required for synthesis of diphthamide, the target of bacterial ADP-ribosylating toxins. Mol Cell 12: 603-613.
    • (2003) Mol Cell , vol.12 , pp. 603-613
    • Liu, S.1    Leppla, S.H.2
  • 33
    • 63849136060 scopus 로고    scopus 로고
    • Codon-optimized fluorescent proteins designed for expression in low-GC gram-positive bacteria
    • Sastalla I, Chim K, Cheung GY, Pomerantsev AP, Leppla SH, (2009) Codon-optimized fluorescent proteins designed for expression in low-GC gram-positive bacteria. Appl Environ Microbiol 75: 2099-2110.
    • (2009) Appl Environ Microbiol , vol.75 , pp. 2099-2110
    • Sastalla, I.1    Chim, K.2    Cheung, G.Y.3    Pomerantsev, A.P.4    Leppla, S.H.5
  • 34
    • 80053319529 scopus 로고    scopus 로고
    • A Bacillus anthracis strain deleted for six proteases serves as an effective host for production of recombinant proteins
    • Pomerantsev AP, Pomerantseva OM, Moayeri M, Fattah R, Tallant C, et al. (2011) A Bacillus anthracis strain deleted for six proteases serves as an effective host for production of recombinant proteins. Protein Expr Purif 80: 80-90.
    • (2011) Protein Expr Purif , vol.80 , pp. 80-90
    • Pomerantsev, A.P.1    Pomerantseva, O.M.2    Moayeri, M.3    Fattah, R.4    Tallant, C.5
  • 35
    • 0034049623 scopus 로고    scopus 로고
    • Optimized production and purification of Bacillus anthracis lethal factor
    • Park S, Leppla SH, (2000) Optimized production and purification of Bacillus anthracis lethal factor. Protein Expr Purif 18: 293-302.
    • (2000) Protein Expr Purif , vol.18 , pp. 293-302
    • Park, S.1    Leppla, S.H.2
  • 37
    • 0032695865 scopus 로고    scopus 로고
    • Sequence analysis of three Bacillus cereus loci carrying PIcR-regulated genes encoding degradative enzymes and enterotoxin
    • Okstad OA, Gominet M, Purnelle B, Rose M, Lereclus D, et al. (1999) Sequence analysis of three Bacillus cereus loci carrying PIcR-regulated genes encoding degradative enzymes and enterotoxin. Microbiology 145 (Pt 11): 3129-3138.
    • (1999) Microbiology 145 (Pt , vol.11 , pp. 3129-3138
    • Okstad, O.A.1    Gominet, M.2    Purnelle, B.3    Rose, M.4    Lereclus, D.5
  • 38
    • 0042736000 scopus 로고    scopus 로고
    • Insertional inactivation of hblC encoding the L2 component of Bacillus cereus ATCC 14579 haemolysin BL strongly reduces enterotoxigenic activity, but not the haemolytic activity against human erythrocytes
    • Lindback T, Okstad OA, Rishovd AL, Kolsto AB, (1999) Insertional inactivation of hblC encoding the L2 component of Bacillus cereus ATCC 14579 haemolysin BL strongly reduces enterotoxigenic activity, but not the haemolytic activity against human erythrocytes. Microbiology 145 (Pt 11): 3139-3146.
    • (1999) Microbiology 145 (Pt , vol.11 , pp. 3139-3146
    • Lindback, T.1    Okstad, O.A.2    Rishovd, A.L.3    Kolsto, A.B.4
  • 40
    • 0033860741 scopus 로고    scopus 로고
    • Evidence for contribution of tripartite hemolysin BL, phosphatidylcholine-preferring phospholipase C, and collagenase to virulence of Bacillus cereus endophthalmitis
    • Beecher DJ, Olsen TW, Somers EB, Wong AC, (2000) Evidence for contribution of tripartite hemolysin BL, phosphatidylcholine-preferring phospholipase C, and collagenase to virulence of Bacillus cereus endophthalmitis. Infect Immun 68: 5269-5276.
    • (2000) Infect Immun , vol.68 , pp. 5269-5276
    • Beecher, D.J.1    Olsen, T.W.2    Somers, E.B.3    Wong, A.C.4
  • 41
    • 0038781942 scopus 로고    scopus 로고
    • Relationship of plcR-regulated factors to Bacillus endophthalmitis virulence
    • Callegan MC, Kane ST, Cochran DC, Gilmore MS, Gominet M, et al. (2003) Relationship of plcR-regulated factors to Bacillus endophthalmitis virulence. Infect Immun 71: 3116-3124.
    • (2003) Infect Immun , vol.71 , pp. 3116-3124
    • Callegan, M.C.1    Kane, S.T.2    Cochran, D.C.3    Gilmore, M.S.4    Gominet, M.5
  • 43
    • 0029963619 scopus 로고    scopus 로고
    • Identification of a Bacillus thuringiensis gene that positively regulates transcription of the phosphatidylinositol-specific phospholipase C gene at the onset of the stationary phase
    • Lereclus D, Agaisse H, Gominet M, Salamitou S, Sanchis V, (1996) Identification of a Bacillus thuringiensis gene that positively regulates transcription of the phosphatidylinositol-specific phospholipase C gene at the onset of the stationary phase. J Bacteriol 178: 2749-2756.
    • (1996) J Bacteriol , vol.178 , pp. 2749-2756
    • Lereclus, D.1    Agaisse, H.2    Gominet, M.3    Salamitou, S.4    Sanchis, V.5
  • 44
    • 0023448638 scopus 로고
    • Identification of self-transmissible plasmids in four Bacillus thuringiensis subspecies
    • Reddy A, Battisti L, Thorne CB, (1987) Identification of self-transmissible plasmids in four Bacillus thuringiensis subspecies. J Bacteriol 169: 5263-5270.
    • (1987) J Bacteriol , vol.169 , pp. 5263-5270
    • Reddy, A.1    Battisti, L.2    Thorne, C.B.3
  • 45
    • 4544264417 scopus 로고    scopus 로고
    • Binary bacterial toxins: biochemistry, biology, and applications of common Clostridium and Bacillus proteins
    • table of contents
    • Barth H, Aktories K, Popoff MR, Stiles BG (2004) Binary bacterial toxins: biochemistry, biology, and applications of common Clostridium and Bacillus proteins. Microbiol Mol Biol Rev 68: 373-402, table of contents.
    • (2004) Microbiol Mol Biol Rev , vol.68 , pp. 373-402
    • Barth, H.1    Aktories, K.2    Popoff, M.R.3    Stiles, B.G.4
  • 47
    • 84875804760 scopus 로고    scopus 로고
    • The effects of Staphylococcus aureus leukotoxins on the host: cell lysis and beyond
    • Yoong P, Torres VJ, (2013) The effects of Staphylococcus aureus leukotoxins on the host: cell lysis and beyond. Curr Opin Microbiol 16: 63-69.
    • (2013) Curr Opin Microbiol , vol.16 , pp. 63-69
    • Yoong, P.1    Torres, V.J.2
  • 48
    • 84859444351 scopus 로고    scopus 로고
    • Inhibition of cytotoxicity by the Nhe cytotoxin of Bacillus cereus through the interaction of dodecyl maltoside with the NheB component
    • Phung D, Granum PE, Dietrich R, Martlbauer E, Hardy SP, (2012) Inhibition of cytotoxicity by the Nhe cytotoxin of Bacillus cereus through the interaction of dodecyl maltoside with the NheB component. FEMS Microbiol Lett 330: 98-104.
    • (2012) FEMS Microbiol Lett , vol.330 , pp. 98-104
    • Phung, D.1    Granum, P.E.2    Dietrich, R.3    Martlbauer, E.4    Hardy, S.P.5
  • 49
    • 0042879872 scopus 로고    scopus 로고
    • Molecular features of the cytolytic pore-forming bacterial protein toxins
    • Alouf JE, (2003) Molecular features of the cytolytic pore-forming bacterial protein toxins. Folia Microbiol (Praha) 48: 5-16.
    • (2003) Folia Microbiol (Praha) , vol.48 , pp. 5-16
    • Alouf, J.E.1
  • 50
    • 84863115878 scopus 로고    scopus 로고
    • Monoclonal antibodies neutralize Bacillus cereus Nhe enterotoxin by inhibiting ordered binding of its three exoprotein components
    • Didier A, Dietrich R, Gruber S, Bock S, Moravek M, et al. (2012) Monoclonal antibodies neutralize Bacillus cereus Nhe enterotoxin by inhibiting ordered binding of its three exoprotein components. Infect Immun 80: 832-838.
    • (2012) Infect Immun , vol.80 , pp. 832-838
    • Didier, A.1    Dietrich, R.2    Gruber, S.3    Bock, S.4    Moravek, M.5
  • 51
    • 0028331322 scopus 로고
    • The membrane attack complex of complement. Assembly, structure and cytotoxic activity
    • Esser AF, (1994) The membrane attack complex of complement. Assembly, structure and cytotoxic activity. Toxicology 87: 229-247.
    • (1994) Toxicology , vol.87 , pp. 229-247
    • Esser, A.F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.