메뉴 건너뛰기




Volumn 8, Issue 1, 2018, Pages

Engineering Bacillus thuringiensis Cyt1Aa toxin specificity from dipteran to lepidopteran toxicity

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; ENDOTOXIN; HEMOLYSIN; INSECT PROTEIN; INSECTICIDAL CRYSTAL PROTEIN, BACILLUS THURINGIENSIS; INSECTICIDE; PROTEIN BINDING; RECOMBINANT PROTEIN;

EID: 85044418520     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/s41598-018-22740-9     Document Type: Article
Times cited : (27)

References (40)
  • 1
    • 84870955143 scopus 로고    scopus 로고
    • Bacillus thuringiensis insecticidal toxins: Mode of action, insect resistance and consequences for crop protection
    • Pardo-López, L., Soberón, M. & Bravo, A. Bacillus thuringiensis insecticidal toxins: Mode of action, insect resistance and consequences for crop protection. FEMS Microbiol. Rev. 37, 3-22 (2013).
    • (2013) FEMS Microbiol. Rev. , vol.37 , pp. 3-22
    • Pardo-López, L.1    Soberón, M.2    Bravo, A.3
  • 3
    • 84877581296 scopus 로고    scopus 로고
    • Cyt toxins produced by Bacillus thuringiensis: A protein fold conserved in several pathogenic microorganisms
    • Soberón, M., López-Díaz, J. A. & Bravo, A. Cyt toxins produced by Bacillus thuringiensis: A protein fold conserved in several pathogenic microorganisms. Peptides. 41, 87-93 (2013).
    • (2013) Peptides. , vol.41 , pp. 87-93
    • Soberón, M.1    López-Díaz, J.A.2    Bravo, A.3
  • 4
    • 67650485570 scopus 로고    scopus 로고
    • Effects of Bacillus thuringiensis ?-endotoxins on the pea aphid (Acyrthosiphon pisum)
    • Porcar, M., Grenier, A.-M., Federici, B. & Rahbe, Y. Effects of Bacillus thuringiensis ?-endotoxins on the pea aphid (Acyrthosiphon pisum). Appl. Environ. Microbiol. 78, 4897-4900 (2009).
    • (2009) Appl. Environ. Microbiol. , vol.78 , pp. 4897-4900
    • Porcar, M.1    Grenier, A.-M.2    Federici, B.3    Rahbe, Y.4
  • 5
    • 84878180392 scopus 로고    scopus 로고
    • Aphicidal efficacy of scorpion and spider derived neurotoxins
    • Pal, N., Yamamoto, T., King, G. F., Waine, C. & Bonning, B. Aphicidal efficacy of scorpion and spider derived neurotoxins. Toxicon. 70, 114-122 (2013).
    • (2013) Toxicon. , vol.70 , pp. 114-122
    • Pal, N.1    Yamamoto, T.2    King, G.F.3    Waine, C.4    Bonning, B.5
  • 6
    • 0031763335 scopus 로고    scopus 로고
    • Cyt1Aa protein of Bacillus thuringiensis is toxic to the cottonwood leaf beetle, Chrysomela scripta, and suppresses high levels of resistance to Cry3Aa
    • Federici, B. A. & Bauer, L. S. Cyt1Aa protein of Bacillus thuringiensis is toxic to the cottonwood leaf beetle, Chrysomela scripta, and suppresses high levels of resistance to Cry3Aa. Appl. Environ. Microbiol. 64, 4368-4371 (1998).
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 4368-4371
    • Federici, B.A.1    Bauer, L.S.2
  • 8
    • 27544481364 scopus 로고    scopus 로고
    • 2005 Development of Bacillus thuringiensis-based assay on Lygus hesperus
    • Wellman-Desbiens, E. & Cote, J.-C. 2005 Development of Bacillus thuringiensis-based assay on Lygus hesperus. J. Econ. Entomol. 98, 1469-1479 (2013).
    • (2013) J. Econ Entomol. , vol.98 , pp. 1469-1479
    • Wellman-Desbiens, E.1    Cote, J.-C.2
  • 9
    • 84879474169 scopus 로고    scopus 로고
    • Cross-order and cross-phylum activity of Bacillus thuringiensis pesticidal proteins
    • van Frankenhuyzen, K. Cross-order and cross-phylum activity of Bacillus thuringiensis pesticidal proteins. J. Invertebr. Pathol. 114, 76-85 (2013).
    • (2013) J. Invertebr. Pathol. , vol.114 , pp. 76-85
    • Van Frankenhuyzen, K.1
  • 10
    • 84875918897 scopus 로고    scopus 로고
    • Activity of Bacillus thuringiensis Cyt1Ba crystal protein against hymenopteran forest pests
    • van Frankenhuyzen, K. & Tonon, A. Activity of Bacillus thuringiensis Cyt1Ba crystal protein against hymenopteran forest pests. J. Invertebr Pathol. 113, 160-162 (2013).
    • (2013) J. Invertebr Pathol. , vol.113 , pp. 160-162
    • Van Frankenhuyzen, K.1    Tonon, A.2
  • 11
    • 29444435452 scopus 로고    scopus 로고
    • Bti Cry11Aa and Cyt1Aa toxins interactions support the synergism-model that Cyt1Aa functions as membranebound receptor
    • Pérez, C. et al. Bti Cry11Aa and Cyt1Aa toxins interactions support the synergism-model that Cyt1Aa functions as membranebound receptor. Proc. Natl. Acad. Sci. USA 102, 18303-18308 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 18303-18308
    • Pérez, C.1
  • 12
    • 79951509059 scopus 로고    scopus 로고
    • Binding of Bacillus thuringiensis subsp israelensis Cry4Ba to Cyt1Aa has an important role in synergism
    • Cantón, P. E., Reyes, E. Z., RuízdeEscudero, I., Bravo, A. & Soberon, M. Binding of Bacillus thuringiensis subsp. israelensis Cry4Ba to Cyt1Aa has an important role in synergism. Peptides. 32, 595-600 (2011).
    • (2011) Peptides. , vol.32 , pp. 595-600
    • Cantón, P.E.1    Reyes, E.Z.2    Ruízdeescudero, I.3    Bravo, A.4    Soberon, M.5
  • 13
    • 0030883387 scopus 로고    scopus 로고
    • CytA enables CryIV endotoxins of Bacillus thuringiensis to overcome high levels of CryIV resistance in the mosquito Culex quinquefasciatus
    • Wirth, M., Georghiou, G. P. & Federici, B. A. CytA enables CryIV endotoxins of Bacillus thuringiensis to overcome high levels of CryIV resistance in the mosquito Culex quinquefasciatus. Proc. Natl. Acad. Sci. USA 9, 10536-10540 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.9 , pp. 10536-10540
    • Wirth, M.1    Georghiou, G.P.2    Federici, B.A.3
  • 14
    • 0029669956 scopus 로고    scopus 로고
    • Structure of the mosquitocidal deltaendotoxin CytB from Bacillus thuringiensis ssp kyushuensis and implications for membrane pore formation
    • Li, J., Koni, P. A. & Ellar, D. J. Structure of the mosquitocidal deltaendotoxin CytB from Bacillus thuringiensis ssp. kyushuensis and implications for membrane pore formation. J. Mol. Biol. 257, 129-52 (1996).
    • (1996) J. Mol. Biol. , vol.257 , pp. 129-152
    • Li, J.1    Koni, P.A.2    Ellar, D.J.3
  • 15
    • 0024595787 scopus 로고
    • Israelensis forms cation-selective channels in planar lipid bilayers
    • A cytolytic delta-endotoxin from Bacillus thuringiensis var.
    • Knowles, B. H. et al. A cytolytic delta-endotoxin from Bacillus thuringiensis var. israelensis forms cation-selective channels in planar lipid bilayers. FEBS Lett. 244, 259-262 (1989).
    • (1989) FEBS Lett. , vol.244 , pp. 259-262
    • Knowles, B.H.1
  • 16
    • 0037883692 scopus 로고    scopus 로고
    • Cytolytic toxin Cyt1Aa and its mechanism of membrane damage: Data and hypothesis
    • Butko, P. Cytolytic toxin Cyt1Aa and its mechanism of membrane damage: data and hypothesis. Appl. Environ. Microbiol. 69, 2415-2422 (2003).
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 2415-2422
    • Butko, P.1
  • 17
    • 70450265465 scopus 로고    scopus 로고
    • Domain II loop 3 of Bacillus thuringiensis Cry1Ab toxin is involved in a "ping-pong" binding mechanism with Manduca sexta aminopeptidase-N and cadherin receptors
    • Pacheco, S. et al. Domain II loop 3 of Bacillus thuringiensis Cry1Ab toxin is involved in a "ping-pong" binding mechanism with Manduca sexta aminopeptidase-N and cadherin receptors. J. Biol. Chem. 284, 32750-32757 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 32750-32757
    • Pacheco, S.1
  • 18
    • 0041817553 scopus 로고    scopus 로고
    • Molecular basis for Bacillus thuringiensis Cry1Ab toxin specificity: Two structural determinants in the Manduca sexta Bt-R1 receptor interact with loops ?-8 and 2 in domain II of Cy1Ab toxin
    • Gomez, I., Dean, D. H., Bravo, A. & Soberon, M. Molecular basis for Bacillus thuringiensis Cry1Ab toxin specificity: Two structural determinants in the Manduca sexta Bt-R1 receptor interact with loops ?-8 and 2 in domain II of Cy1Ab toxin. Biochemistry. 42, 10482-10489 (2003).
    • (2003) Biochemistry. , vol.42 , pp. 10482-10489
    • Gomez, I.1    Dean, D.H.2    Bravo, A.3    Soberon, M.4
  • 19
    • 0029908854 scopus 로고    scopus 로고
    • Protein engineering of Bacillus thuringiensis delta-endotoxin: Mutations at domain II of CryIAb enhance receptor affinity and toxicity toward gypsy moth larvae
    • Rajamohan, F., Alzate, O., Cotrill, J. A., Curtiss, A. & Dean, D. H. Protein engineering of Bacillus thuringiensis delta-endotoxin: mutations at domain II of CryIAb enhance receptor affinity and toxicity toward gypsy moth larvae. Proc. Natl. Acad. Sci. USA 93, 14338-14343 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 14338-14343
    • Rajamohan, F.1    Alzate, O.2    Cotrill, J.A.3    Curtiss, A.4    Dean, D.H.5
  • 20
    • 33644982091 scopus 로고    scopus 로고
    • Redesigning Bacillus thuringiensis Cry1Aa toxin into a mosquito toxin
    • Liu, X. S. & Dean, D. H. Redesigning Bacillus thuringiensis Cry1Aa toxin into a mosquito toxin. Prot. Eng. Design. Selec. 19, 107-111 (2006).
    • (2006) Prot. Eng. Design. Selec. , vol.19 , pp. 107-111
    • Liu, X.S.1    Dean, D.H.2
  • 21
    • 84957585285 scopus 로고    scopus 로고
    • Loop replacements with gut-binding peptides in Cry1Ab domain II enhanced toxicity against the brown planthopper, Nilaparvata lugens (Stal)
    • Shao, E. et al. Loop replacements with gut-binding peptides in Cry1Ab domain II enhanced toxicity against the brown planthopper, Nilaparvata lugens (Stal). Scientific Rep. 6, 20106 (2016).
    • (2016) Scientific Rep. , vol.6 , pp. 20106
    • Shao, E.1
  • 22
    • 84878156378 scopus 로고    scopus 로고
    • Retargeting of the Bacillus thuringiensis toxin Cyt2Aa against hemipteran insect pest
    • Chougule, N. P. et al. Retargeting of the Bacillus thuringiensis toxin Cyt2Aa against hemipteran insect pest. Procs. Natl. Acad. Sci. USA 110, 8465-8470 (2013).
    • (2013) Procs. Natl. Acad. Sci. USA , vol.110 , pp. 8465-8470
    • Chougule, N.P.1
  • 23
    • 84885943293 scopus 로고    scopus 로고
    • Manduca sexta aminopeptidase-N and alkaline phosphatase have a differential role in the mode of action of Cry1Aa, Cry1Ab and Cry1Ac toxins from Bacillus thuringiensis
    • Flores-Escobar, B., Rodríguez-Magadan, H., Bravo, A., Soberon, M. & Gomez, I. Manduca sexta aminopeptidase-N and alkaline phosphatase have a differential role in the mode of action of Cry1Aa, Cry1Ab and Cry1Ac toxins from Bacillus thuringiensis. Appl. Environ. Microbiol. 79, 4543-4550 (2013).
    • (2013) Appl. Environ. Microbiol. , vol.79 , pp. 4543-4550
    • Flores-Escobar, B.1    Rodríguez-Magadan, H.2    Bravo, A.3    Soberon, M.4    Gomez, I.5
  • 24
    • 65849141019 scopus 로고    scopus 로고
    • Dominant negative mutants of Bacillus thuringiensis Cry1Ab toxin function as anti-toxins: Demonstration of the role of oligomerization in toxicity
    • Rodríguez-Almazán, C. et al. Dominant negative mutants of Bacillus thuringiensis Cry1Ab toxin function as anti-toxins: Demonstration of the role of oligomerization in toxicity. PloS ONE. 4, e5545 (2009).
    • (2009) PloS ONE. , vol.4 , pp. e5545
    • Rodríguez-Almazán, C.1
  • 25
    • 80054847383 scopus 로고    scopus 로고
    • Cyt1Aa toxin: Crystal structure reveals implications for its membrane-perforating function
    • Cohen, S. et al. Cyt1Aa toxin: crystal structure reveals implications for its membrane-perforating function. J. Mol. Biol. 413, 804-814 (2011).
    • (2011) J. Mol. Biol. , vol.413 , pp. 804-814
    • Cohen, S.1
  • 26
    • 77954860412 scopus 로고    scopus 로고
    • Single-concentration tests show synergism among Bacillus thuringiensis subsp israelensis toxins against the malaria vector mosquito Anopheles albimanus
    • Fernández-Luna, M. T. et al. Single-concentration tests show synergism among Bacillus thuringiensis subsp. israelensis toxins against the malaria vector mosquito Anopheles albimanus. J. Invertebr. Pathol. 10, 231-233 (2010).
    • (2010) J. Invertebr. Pathol. , vol.10 , pp. 231-233
    • Fernández-Luna, M.T.1
  • 27
    • 84899447848 scopus 로고    scopus 로고
    • Membrane binding and oligomer membrane insertion are necessary but insufficient for Bacillus thuringiensis Cyt1Aa toxicity
    • Canton, P. E., López-Días, J. A., Gill, S. S., Bravo, A. & Soberon, M. Membrane binding and oligomer membrane insertion are necessary but insufficient for Bacillus thuringiensis Cyt1Aa toxicity. Peptides. 53, 286-291 (2014).
    • (2014) Peptides. , vol.53 , pp. 286-291
    • Canton, P.E.1    López-Días, J.A.2    Gill, S.S.3    Bravo, A.4    Soberon, M.5
  • 28
    • 84886398064 scopus 로고    scopus 로고
    • Oligomerization is a key step in Cyt1Aa membrane insertion and toxicity but not necessary to synergize Cry11Aa toxicity in Aedes aegypti larvae
    • López-Diaz, J. A., Cantón, P. E., Gill, S. S., Soberón, M. & Bravo, A. Oligomerization is a key step in Cyt1Aa membrane insertion and toxicity but not necessary to synergize Cry11Aa toxicity in Aedes aegypti larvae. Environ. Microbiol. 155, 3030-3039 (2013).
    • (2013) Environ. Microbiol. , vol.155 , pp. 3030-3039
    • López-Diaz, J.A.1    Cantón, P.E.2    Gill, S.S.3    Soberón, M.4    Bravo, A.5
  • 29
    • 0020631287 scopus 로고
    • Mechanism of action of Bacillus thuringiensis var israelensis insecticidal ?-endotoxin
    • Thomas, W. E. & Ellar, D. J. Mechanism of action of Bacillus thuringiensis var israelensis insecticidal ?-endotoxin. FEBS Lett. 154, 362-368 (1983).
    • (1983) FEBS Lett. , vol.154 , pp. 362-368
    • Thomas, W.E.1    Ellar, D.J.2
  • 30
    • 0034663667 scopus 로고    scopus 로고
    • Membrane pore architecture of a cytolytic toxin from Bacillus thuringiensis
    • Promdonkoy, B. & Ellar, D. J. Membrane pore architecture of a cytolytic toxin from. Bacillus thuringiensis. Biochem. J. 350, 275-282 (2000).
    • (2000) Biochem. J. , vol.350 , pp. 275-282
    • Promdonkoy, B.1    Ellar, D.J.2
  • 31
    • 2542457488 scopus 로고    scopus 로고
    • Effect of pH and ionic strength on the cytolytic toxin Cyt1A a florescence spectroscopy study
    • Manceva, S. D., Pustay-Carey, M. & Butko, P. Effect of pH and ionic strength on the cytolytic toxin Cyt1A a florescence spectroscopy study. Biochim. Biophys Acta. 1699, 123-130 (2004).
    • (2004) Biochim. Biophys Acta. , vol.1699 , pp. 123-130
    • Manceva, S.D.1    Pustay-Carey, M.2    Butko, P.3
  • 32
    • 85029360621 scopus 로고    scopus 로고
    • Highly effective broad spectrum chimeric larvicide that targets vector mosquitoes using a lipophilic protein
    • Bideshi, D. K., Park, H.-W., Hice, R. H., Wirth, M. C. & Federeci, B. A. Highly effective broad spectrum chimeric larvicide that targets vector mosquitoes using a lipophilic protein. Sci. Rep. 7(1), 11282 (2017).
    • (2017) Sci. Rep. , vol.7 , Issue.1 , pp. 11282
    • Bideshi, D.K.1    Park, H.-W.2    Hice, R.H.3    Wirth, M.C.4    Federeci, B.A.5
  • 33
    • 0028148010 scopus 로고
    • Synergism of mosquitocidal toxicity between CytA and CryIV proteins using inclusions produced from cloned genes of Bacillus thuringiensis subsp
    • Wu, D., Johnson, J. J. & Federici, B. A. Synergism of mosquitocidal toxicity between CytA and CryIV proteins using inclusions produced from cloned genes of Bacillus thuringiensis subsp. israelensis. Mol. Microbiol. 13, 965-972 (1994).
    • (1994) Israelensis. Mol. Microbiol. , vol.13 , pp. 965-972
    • Wu, D.1    Johnson, J.J.2    Federici, B.A.3
  • 34
    • 0025786601 scopus 로고
    • Construction of cloning vectors for Bacillus thuringiensis
    • Arantes, O. & Lereclus, D. Construction of cloning vectors for Bacillus thuringiensis. Gene. 108, 115-119 (1991).
    • (1991) Gene. , vol.108 , pp. 115-119
    • Arantes, O.1    Lereclus, D.2
  • 35
    • 0027418862 scopus 로고
    • High-level cryIVD and cytA gene expression in Bacillus thuringiensis does not require the 20-kilodalton protein, and the coexpressed gene products are synergistic in their toxicity to mosquitoes
    • Chang, C., Yu, Y. M., Dai, S. M., Law, S. K. & Gill, S. S. High-level cryIVD and cytA gene expression in Bacillus thuringiensis does not require the 20-kilodalton protein, and the coexpressed gene products are synergistic in their toxicity to mosquitoes. Appl. Environ. Microbiol. 59, 815-821 (1993).
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 815-821
    • Chang, C.1    Yu, Y.M.2    Dai, S.M.3    Law, S.K.4    Gill, S.S.5
  • 37
    • 0020645619 scopus 로고
    • Bacillus thuringiensis var israelensis crystal deltaendotoxin: Effects on insect and mammalian cells in vitro and in vivo
    • Thomas, W. E. & Ellar, D. J. Bacillus thuringiensis var israelensis crystal deltaendotoxin: effects on insect and mammalian cells in vitro and in vivo. J. Cell Sci. 60, 181-197 (1983a).
    • (1983) J. Cell Sci. , vol.60 , pp. 181-197
    • Thomas, W.E.1    Ellar, D.J.2
  • 38
    • 0028155344 scopus 로고
    • Design of an aqueous two-phase system for the purification of ICP from Bacillus thuringiensis
    • Güereca, L., Bravo, A. & Quintero, R. Design of an aqueous two-phase system for the purification of ICP from Bacillus thuringiensis. Process Biochem. 29, 181-185 (1994).
    • (1994) Process Biochem. , vol.29 , pp. 181-185
    • Güereca, L.1    Bravo, A.2    Quintero, R.3
  • 39
    • 0026794931 scopus 로고
    • Evaluation of synergism among Bacillus thuringiensis toxins
    • Tabashnik, B. E. Evaluation of synergism among Bacillus thuringiensis toxins. Appl. Environ. Microbiol. 58, 3343-3346 (1992).
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 3343-3346
    • Tabashnik, B.E.1
  • 40
    • 78751498350 scopus 로고    scopus 로고
    • The amino-and carboxyl-terminal fragments of the Bacillus thuringiensis Cyt1Aa toxin have differential roles on toxin oligomerization and pore formation
    • Rodriguez-Almazán, C. et al. The amino-and carboxyl-terminal fragments of the Bacillus thuringiensis Cyt1Aa toxin have differential roles on toxin oligomerization and pore formation. Biochemistry. 50, 388-396 (2011).
    • (2011) Biochemistry. , vol.50 , pp. 388-396
    • Rodriguez-Almazán, C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.