Mode of action of mosquitocidal Bacillus thuringiensis toxins

Toxicon

Volumn 49, Issue 5, 2007, Pages 597-600

  Soberón, Mario ^a   Fernández, Luisa E ^a   Pérez, Claudia ^a   Gill, Sarjeet S ^b   Bravo, Alejandra ^a  

^a INSTITUTO DE BIOTECNOLOGÍA   (Mexico)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Bacillus thuringiensis; Cry; Cyt; Mode of action; Receptor; Synergism

Indexed keywords

BACILLUS THURINGIENSIS TOXIN; CRY1A PROTEIN; CYT1A PROTEIN; MEMBRANE RECEPTOR; PROTEIN; UNCLASSIFIED DRUG;

LARVA; LEPIDOPTERA; MOSQUITO; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FUNCTION; PROTEIN STRUCTURE; REVIEW;

ANIMALS; BACILLUS THURINGIENSIS; BACTERIAL TOXINS; CULICIDAE; LARVA; LEPIDOPTERA; MODELS, BIOLOGICAL; MODELS, MOLECULAR;

BACILLUS THURINGIENSIS; HEXAPODA;

EID: 33947390038     PISSN: 00410101     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.toxicon.2006.11.008     Document Type: Review

References (19)

1. Becker, N., 2000. Bacterial control of vector-mosquitoes and black flies. In: entomopathogenic bacteria: from laboratory to field application. Kluwer Academic Publishers, Dordrecht, pp. 383-398.
2. Boonserm P., Davis P., Ellar D.J., and Li J. Crystal structure of the mosquito-larvicidal toxin Cry4Ba and its biological implications. J. Mol. Biol. 348 (2005) 363-382
3. Bravo A., Gómez I., Conde J., Muñoz-Garay C., Sánchez J., Zhuang M., Gill S.S., and Soberón M. Oligomerization triggers differential binding of a pore-forming toxin to a different receptor leading to efficient interaction with membrane microdomains. Biochem. Biophys. Acta. 1667 (2004) 38-46
4. Bravo, A., Gill, S.S., Soberón, M., 2005. Bacillus thuringiensis Mechanisms and Use. In: Comprehensive Molecular Insect Science Elsevier BV, pp. 175-206.
5. Butko P., Huang F., Pusztai-Carey M., and Surewicz W.K. Interaction of the delta-endotoxin CytA from Bacillus thuringiensis var israelensis with lipid membranes. Biochemistry 36 (1997) 12862-12868
6. Buzdin A.A., Revina L.P., Kostina L.I., Zalunin I.A., and Chestukhina G.G. Interaction of 65- and 62-kD proteins from the apical membranes of the Aedes aegypti larvae midgut epithelium with Cry4B and Cry11A endotoxins of Bacillus thuringiensis Biochem. Biochemistry (Moscow) 67 (2002) 540-546
7. Fernández L.E., Pérez C., Segovia L., Rodríguez M.H., Gill S.S., Bravo A., and Soberón M. Cry11Aa toxin from Bacillus thuringiensis binds its receptor in Aedes aegypti mosquito larvae trough loop α-8 of domain II FEBS. Letters 79 (2005) 3508-3514
8. Fernández L.E., Aimanova K.G., Gill S.S., Bravo A., and Soberón M. A GPI-anchored alkaline phosphatase is a functional midgut receptor of Cry11Aa toxin in Aedes aegypti larvae. Biochem. J. 394 (2006) 77-84
9. Ferré J., and van Rie J. Biochemistry and genetics of insect resistance to Bacillus thuringiensis. Annu. Rev. Entomol. 47 (2002) 501-533
10. Gómez I., Sánchez J., Miranda R., Bravo A., and Soberón M. Cadherin-like receptor binding facilitates proteolytic cleavage of helix α-1 in domain I and oligomer pre-pore formation of Bacillus thuringiensis Cry1Ab toxin FEBS. Letters 513 (2002) 242-246
11. Jurat-Fuentes J.L., and Adang M.J. Characterization of a Cry1Ac-receptor alkaline phosphatase in susceptible and resistant Heliothis virescens larvae. Eur. J. Biochem. 271 (2004) 3127-3135
12. Knight P., Crickmore N., and Ellar D.J. The receptor for Bacillus thuringiensis CryIA(c) delta-endotoxin in the brush border membrane of the lepidopteran Manduca sexta is aminopeptidase N. Mol. Microbiol. 11 (1994) 429-436
13. Pérez C., Fernández L.E., Sun J., Folch J.L., Gill S.S., Soberón M., and Bravo A. Bacillus thuringiensis subsp. israelensis Cyt1Aa synergizes Cry11Aa toxin by functioning as a membrane-bound receptor. Proc. Natl. Acad. Sci. 102 (2005) 18303-18308
14. Promdonkoy B., and Ellar D.J. Investigation of the pore forming mechanism of a Cytolitic δ-endotoxin from Bacillus thuringiensis. Biochem. J 374 (2003) 255-259
15. Rausell C., Muñoz-Garay C., Miranda-CassoLuengo R., Gómez I., Rudiño-Piñera E., Soberón M., and Bravo A. Tryptophan spectroscopy studies and black lipid bilayer analysis indicate that the oligomeric structure of Cry1Ab toxin from Bacillus thuringiensis is the membrane-insertion intermediate. Biochemistry 43 (2004) 166-174
16. Vadlamudi R.K., Weber E., Ji I., Ji T.H., and Bulla Jr. L.A. Cloning and expression of a receptor for an insecticidal toxin of Bacillus thuringiensis. J. Biol. Chem. 270 (1995) 5490-5494
17. Valaitis A.P., Jenkins J.L., Lee M.K., Dean D.H., and Garner K.J. Isolation and partial characterization of Gypsy moth BTR-270 an anionic brush border membrane glycoconjugate that binds Bacillus thuringiensis Cry1A toxins with high affinity. Arch. Ins. Biochem. Physiol. 46 (2001) 186-200
18. Wirth M.C., Georghiou G.P., and Federeci 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. 94 (1997) 10536-10540
19. Zhuang M., Oltean D.I., Gómez I., Pullikuth A.K., Soberón M., Bravo A., and Gill S.S. Heliothis virescens and Manduca sexta lipid rafts are involved in Cry1A toxin binding to the midgut epithelium and subsequent pore formation. J. Biol. Chem. 277 (2002) 13863-13872