膜孔形成毒素
(Pore-forming toxin から転送)
出典: フリー百科事典『ウィキペディア（Wikipedia）』 (2021/10/04 04:35 UTC 版)
膜孔形成毒素（まくこうけいせいどくそ、英: Pore-Forming Toxin、略称: PFT）とは、生物によって生合成されて外分泌される毒素の中で、細胞膜を貫通する細孔を形成することで、標的細胞を障害、あるいは、死に追いやるタンパク質である。細菌の他に、ミミズなどによっても産生されており、様々な種類の膜孔形成毒素が知られている。
- ^ a b Marcus Mueller, Ulla Grauschopf, Timm Maier, Rudi Glockshuber & Nenad Ban (2009). “The structure of a cytolytic alpha-helical toxin pore reveals its assembly mechanism”. Nature 459 (7247): 726–730. doi:10.1038/nature08026. PMID 19421192.
- ^ Langzhou Song, Michael R. Hobaugh, Christopher Shustak, Stephen Cheley, Hagan Bayley, J. Eric Gouaux (1996). “Structure of staphylococcal α-hemolysin, a heptameric transmembrane pore”. Science 274 (5294): 1859–1866. doi:10.1126/science.274.5294.1859. PMID 8943190.
- ^ Valérie Guillet, Pierre Roblin, Sandra Werner, Manuela Coraiola, Gianfranco Menestrina, Henri Monteil, Gilles Prévost & Lionel Mourey (2004). “Crystal structure of leucotoxin S component: new insight into the Staphylococcal beta-barrel pore-forming toxin”. J. Biol. Chem. 279 (39): 41028–41037. doi:10.1074/jbc.M406904200. PMID 15262988.
- ^ Parker MW, Buckley JT, Postma JP, Tucker AD, Leonard K, Pattus F, Tsernoglou D (1994). “Structure of the Aeromonas toxin proaerolysin in its water-soluble and membrane-channel states”. Nature 367 (6460): 292–295. doi:10.1038/367292a0. PMID 7510043.
- ^ Cole, A. R., Gibert, M., Popoff, M., Moss, D. S., Titball, R. W., & Basak, A. K. (2004). “Clostridium perfringens ε-toxin shows structural similarity to the pore-forming toxin aerolysin”. Nat. Struct. Mol. Biol. 11 (8): 797–798. doi:10.1038/nsmb804.
- ^ Thanabalu T, Porter AG (1996). “A Bacillus sphaericus gene encoding a novel type of mosquitocidal toxin of 31.8 kDa”. Gene 170 (1): 85–89. doi:10.1016/0378-1119(95)00836-5. PMID 8621095.
- ^ Liu JW, Porter AG, Wee BY, Thanabalu T (1996). “New gene from nine Bacillus sphaericus strains encoding highly conserved 35.8-kilodalton mosquitocidal toxins”. Applied and Environmental Microbiology 62 (6): 2174–2176. PMC PMC167996. PMID 8787415.
- ^ Berry C, Crickmore N (2017). “Structural classification of insecticidal proteins - Towards an in silico characterisation of novel toxins”. J. Invertebr. Pathol. 142: 16–22. doi:10.1016/j.jip.2016.07.015. PMID 27480403.
- ^ US 7078592B2 "Nucleic acids encoding coleopteran-toxic polypeptides and insect-resistant transgenic plants comprising them."
- ^ Berry C, Crickmore N (2017). “Structural classification of insecticidal proteins - Towards an in silico characterisation of novel toxins”. J. Invertebr. Pathol. 142: 16–22. doi:10.1016/j.jip.2016.07.015. PMID 27480403.
- ^ Oei C, Hindley J, Berry C (1990). “An analysis of the genes encoding the 51.4- and 41.9-kDa toxins of Bacillus sphaericus 2297 by deletion mutagenesis: the construction of fusion proteins”. FEMS Microbiol. Lett. 60 (3): 265–273. doi:10.1111/j.1574-6968.1990.tb03900.x. PMID 2083839.
- ^ Jones GW, Nielsen-Leroux C, Yang Y, Yuan Z, Dumas VF, Monnerat RG, Berry C (2007). “A new Cry toxin with a unique two-component dependency from Bacillus sphaericus”. FASEB J. 21 (14): 4112–4120. doi:10.1096/fj.07-8913com. PMID 17646596.
- ^ Ellis RT, Stockhoff BA, Stamp L, Schnepf HE, Schwab GE, Knuth M, Russell J, Cardineau GA, Narva KE (2002). “Novel Bacillus thuringiensis binary insecticidal crystal proteins active on western corn rootworm, Diabrotica virgifera virgifera LeConte”. Appl. Environ. Microbiol. 68 (3): 1137–45. doi:10.1128/AEM.68.3.1137-1145.2002. PMC PMC123759. PMID 11872461.
- ^ PDB 3o44
- ^ De S, Olson R (2011). “Crystal structure of the Vibrio cholerae cytolysin heptamer reveals common features among disparate pore-forming toxins”. Proc. Natl. Acad. Sci. USA 108 (18): 7385–7390. doi:10.1073/pnas.1017442108. PMC PMC3088620. PMID 21502531.
- ^ PDB 3b07
- ^ Yamashita K, Kawai Y, Tanaka Y, Hirano N, Kaneko J, Tomita N, Ohta M, Kamio Y, Yao M, Tanaka I (2011). “Crystal structure of the octameric pore of staphylococcal γ-hemolysin reveals the β-barrel pore formation mechanism by two components”. Proc. Natl. Acad. Sci. USA 108 (42): 17314–17319. doi:10.1073/pnas.1110402108. PMC PMC3198349. PMID 21969538.
- ^ PDB 1T5R
- ^ Guillet V, Roblin P, Werner S, Coraiola M, Menestrina G, Monteil H, Prévost G, Mourey L (2004). “Crystal structure of leucotoxin S component: new insight into the Staphylococcal beta-barrel pore-forming toxins”. J. Biol. Chem. 279 (39): 41028–41037. doi:10.1074/jbc.M406904200. PMID 15262988.
- ^ Schwartz JL, Potvin L, Coux F, Charles JF, Berry C, Humphreys MJ, Jones AF, Bernhart I, Dalla Serra M, Menestrina (2001). “Permeabilization of model lipid membranes by Bacillus sphaericus mosquitocidal binary toxin and its individual components”. J. Membr. Biol. 184 (2): 171–183. doi:10.1007/s00232-001-0086-1. PMID 11719853.
- ^ Cokmus C, Davidson EW, Cooper K (1997). “Electrophysiological effects of Bacillus sphaericus binary toxin on cultured mosquito cells”. J. Invertebr. Pathol. 69 (3): 197–204. doi:10.1006/jipa.1997.4660. PMID 9170345.
- ^ Opota O, Gauthier NC, Doye A, Berry C, Gounon P, Lemichez E, Pauron D (2011). “Bacillus sphaericus binary toxin elicits host cell autophagy as a response to intoxication”. PLoS ONE 6 (2): e14682. doi:10.1371/journal.pone.0014682. PMC PMC3038859. PMID 21339824.
- ^ Tangsongcharoen C, Chomanee N, Promdonkoy B, Boonserm P (2015). “Lysinibacillus sphaericus binary toxin induces apoptosis in susceptible Culex quinquefasciatus larvae”. J. Invertebr. Pathol. 128: 57–63. doi:10.1016/j.jip.2015.04.008. PMID 25958262.
- ^ de Melo JV, Jones GW, Berry C, Vasconcelos RH, de Oliveira CM, Furtado AF, Peixoto CA, Silva-Filha MH (2009). “Cytopathological effects of Bacillus sphaericus Cry48Aa/Cry49Aa toxin on binary toxin-susceptible and -resistant Culex quinquefasciatus larvae”. Appl. Environ. Microbiol. 75 (14): 4782–4789. doi:10.1128/AEM.00811-09. PMC PMC2708442. PMID 19502449.
- ^ Narva KE, Wang NX, Herman R (2017). “Safety considerations derived from Cry34Ab1/Cry35Ab1 structure and function”. J. Invertebr. Pathol. 142: 27–33. doi:10.1016/j.jip.2016.07.019. PMID 27480405.
- ^ Fujita K, Katahira J, Horiguchi Y, Sonoda N, Furuse M, Tsukita S (2000). “Clostridium perfringens enterotoxin binds to the second extracellular loop of claudin-3, a tight junction integral membrane protein”. FEBS Lett. 476 (3): 258–261. doi:10.1016/S0014-5793(00)01744-0. PMID 10913624.
- ^ a b Silva-Filha MH, Nielsen-LeRoux C, Charles JF (1999). “Identification of the receptor for Bacillus sphaericus crystal toxin in the brush border membrane of the mosquito Culex pipiens (Diptera: Culicidae)”. Insect Biochem. Mol. Biol. 29 (8): 711–721. doi:10.1016/S0965-1748(99)00047-8. PMID 10451923.
- ^ Ferreira LM, Romão TP, de-Melo-Neto OP, Silva-Filha MH (2010). “The orthologue to the Cpm1/Cqm1 receptor in Aedes aegypti is expressed as a midgut GPI-anchored α-glucosidase, which does not bind to the insecticidal binary toxin”. Insect Biochem. Mol. Biol. 40 (8): 604–610. doi:10.1016/j.ibmb.2010.05.007. PMID 20685335.
- ^ US 6248536B1 "Bacillus thuringiensis CryET33 and CryET34 compositions and uses thereof."
- ^ Thanabalu, T. (2000). Cloning and characterisation of a gene encoding a 100 kDa toxin from Bacillus sphaericus SSII-1 and expresson of insecticidal toxins in Caulobacter crescentus (Ph.D. thesis). National University of Singapore.
- ^ Treiber N, Reinert DJ, Carpusca I, Aktories K, Schulz GE (2008). “Structure and mode of action of a mosquitocidal holotoxin”. J. Mol. Biol. 381 (1): 150–159. doi:10.1016/j.jmb.2008.05.067. PMID 18586267.
- ^ Rossjohn J, Feil SC, McKinstry WJ, Tweten RK, Parker MW (1997). “Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form”. Cell 89 (5): 685–692. doi:10.1016/S0092-8674(00)80251-2. PMID 9182756.
- ^ Tilley SJ, Orlova EV, Gilbert RJ, Andrew PW, Saibil HR (2005). “Structural basis of pore formation by the bacterial toxin pneumolysin”. Cell 121 (2): 247–256. doi:10.1016/j.cell.2005.02.033. PMID 15851031.
- ^ Rosado CJ, Buckle AM, Law RH, Butcher RE, Kan WT, Bird CH, Ung K, Browne KA, Baran K, Bashtannyk-Puhalovich TA, Faux NG, Wong W, Porter CJ, Pike RN, Ellisdon AM, Pearce MC, Bottomley SP, Emsley J, Smith AI, Rossjohn J, Hartland EL, Voskoboinik I, Trapani JA, Bird PI, Dunstone MA, Whisstock JC (2007). “A common fold mediates vertebrate defense and bacterial attack”. Science 317 (5844): 1548–51. doi:10.1126/science.1144706. PMID 17717151.
- ^ Tschopp J, Masson D, Stanley KK (1986). “Structural/functional similarity between proteins involved in complement- and cytotoxic T-lymphocyte-mediated cytolysis”. Nature 322 (6082): 831–4. doi:10.1038/322831a0. PMID 2427956.
- ^ Nishiwaki H, Nakashima K, Ishida C, Kawamura T, Matsuda K (2007). “Cloning, functional characterization, and mode of action of a novel insecticidal pore-forming toxin, sphaericolysin, produced by Bacillus sphaericus”. Appl. Environ. Microbiol. 73 (10): 3404–3411. doi:10.1128/AEM.00021-07. PMC PMC1907092. PMID 17400778.
- ^ Bruce Alberts; Alexander Johnson; Julian Lewis; Martin Raff; Keith Roberts; Peter Walter (2002). Molecular Biology of the Cell (4th ed.). Routledge. ISBN 0-8153-3218-1.
[続きの解説]
「膜孔形成毒素」の続きの解説一覧
- 1 膜孔形成毒素とは
- 2 膜孔形成毒素の概要
- 3 コレストロール依存性細胞溶解素
- 4 外部リンク
- 膜孔形成毒素のページへのリンク
