Cloning and epitope mapping of Cry11Aa-binding sites in the Cry11Aa-receptor alkaline phosphatase from Aedes aegypti

Biochemistry

Volumn 48, Issue 37, 2009, Pages 8899-8907

  Fernandez, Luisa E ^a   Martinez Anaya, Claudia ^a   Lira, Erandi ^a   Chen, Jianwu ^b   Evans, Amy ^b   Hernández Martínez, Salvador ^c   Lanz Mendoza, Humberto ^c   Bravo, Alejandra ^a   Gill, Sarjeet S ^b   Soberón, Mario ^a  

^a INSTITUTO DE BIOTECNOLOGÍA   (Mexico)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c INSTITUTO NACIONAL DE SALUD PÚBLICA   (Mexico)

Author keywords

[No Author keywords available]

Indexed keywords

AEDES AEGYPTI; ALKALINE PHOSPHATASE; BACILLUS THURINGIENSIS; BRUSH BORDER MEMBRANE VESICLES; CDNA CLONES; CRY11AA; EPITOPE MAPPING; FUNCTIONAL CHARACTERIZATION; ISOFORMS; SITE DIRECTED MUTAGENESIS; SPOT ARRAYS;

AMINES; BACTERIOLOGY; BINDING ENERGY; CELL MEMBRANES; CLONING; PEPTIDES; TOXICITY;

BINDING SITES;

ALKALINE PHOSPHATASE; ALKALINE PHOSPHATASE CRY11AA; ISOPROTEIN; UNCLASSIFIED DRUG;

AEDES AEGYPTI; AMINO ACID SEQUENCE; ARTICLE; BINDING SITE; BRUSH BORDER; CONTROLLED STUDY; EPITOPE MAPPING; MOLECULAR CLONING; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN INTERACTION;

AEDES; ALKALINE PHOSPHATASE; AMINO ACID SEQUENCE; ANIMALS; BACTERIAL PROTEINS; BINDING SITES; CLONING, MOLECULAR; ENDOTOXINS; EPITOPE MAPPING; HEMOLYSIN PROTEINS; ISOENZYMES; LARVA; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, CELL SURFACE; SEQUENCE ALIGNMENT;

AEDES AEGYPTI; BACILLUS THURINGIENSIS SEROVAR ISRAELENSIS;

EID: 70349154252     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi900979b     Document Type: Article

References (33)

1. Bravo, A., Gill, S. S., and Soberón, M. (2007) Mode of action of Bacillus thuringiensis toxins and their potential for insect control. Toxicon 49, 423-435. (Pubitemid 46350780)
2. Soberón, M., Gill, S. S., and Bravo, A. (2009) Signaling versus punching hole: How do Bacillus thuringiensis toxins kill insect midgut cells? Cell. Mol. Life Sci. 66, 1337-1349.
3. Chhabra, M., Mittal, V., Bhattacharya, D., Rana, U., and Lal, S. (2008) Chikungunya fever: A re-emerging viral infection. Indian J. Med. Microbiol. 26, 5-12.
4. Bravo, A., Gómez, I., Conde, J., Muñoz-Garay, C., Sánchez, J., Miranda, R., Zhuang, M., Gill, S. S., and Soberón, M. (2004) Oligomerization triggers differential binding of a pore-forming toxin to a different receptor leading to efficient interaction with membrane microdomains. Biochim. Biophys. Acta 1667, 38-46. (Pubitemid 39463332)
5. 1 receptor interact with loops R-8 and 2 in domain II of Cy1Ab toxin. Biochemistry 42, 10482-10489.
6. Gómez, I., Arenas, I., Benitez, I., Miranda-Ríos, J., Becerril, B., Grande, R., Almagro, J. C., Bravo, A., and Soberón, M. (2006) Specific epitopes of domains II and III of Bacillus thuringiensis Cry1Ab toxin involved in the sequential interaction with cadherin and aminopeptidase-N receptors in Manduca sexta. J. Biol. Chem. 281, 34032-34039.
7. Xie, R., Zhuang, M., Ross, L. S., Gómez, I., Oltean, D. I., Bravo, A., Soberón, M., and Gill, S. S. (2005) Single amino acid mutations in the cadherin receptor from Heliothis virescens affect its toxin binding ability to Cry1A toxins. J. Biol. Chem. 280, 8416-8425. (Pubitemid 40349746)
8. Gómez, I., Sánchez, J., Miranda, R., Bravo, A., and Soberón, M. (2002) Cadherin-like receptor binding facilitates proteolytic cleavage of helix R-1 in domain I and oligomer pre-pore formation of Bacillus thuringiensis Cry1Ab toxin. FEBS Lett. 513, 242-246.
9. Zhuang, M., Oltean, D. I., Gómez, I., Pullikuth, A. K., Soberón, M., Bravo, A., and Gill, S. S. (2002) 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, 13863-13872. (Pubitemid 34967992)
10. Hua, G., Zhang, R., Abdullah, M. A., and Adang, M. J. (2008) Anopheles gambiae cadherin AgCad1 binds the Cry4Ba toxin of Bacillus thuringiensis israelensis and a fragment of AgCad1 synergizes toxicity. Biochemistry 47, 5101-5110. (Pubitemid 351620748)
11. Abdullah, M. A., Valaitis, A. P., and Dean, D. H. (2006) Identification of a Bacillus thuringiensis Cry11Ba toxin-binding aminopeptidase from the mosquito, Anopheles quadrimaculatus. BMC Biochem. 7, 16.
12. Zhang, R., Hua, G., Andacht, T. M., and Adang, M. J. (2008) A 106-kDa aminopeptidase is a putative receptor for Bacillus thuringiensis Cry11Ba toxin in the mosquito Anopheles gambiae. Biochemistry 47, 11263-11272.
13. Fernández, L. E., Aimanova, K. G., Gill, S. S., Bravo, A., and Soberón, M. A (2006) GPI-anchored alkaline phosphatase is a functional midgut receptor of Cry11Aa toxin in Aedes aegypti larvae. Biochem. J. 394, 77-84.
14. Abdullah, M. A., Alzate, O., Mohammad, M., McNall, R. J., Adang, M. J., and Dean, D. H. (2003) Introduction of Culex toxicity into Bacillus thuringiensis Cry4Ba by protein engineering. Appl. Environm. Microbiol. 69, 5343-5353. (Pubitemid 37150758)
15. Fernández, L E., Pérez, C., Segovia, L., Rodríguez, M. H., Gill, S. S., Bravo, A., and Soberón, M. (2005) Cry11Aa toxin from Bacillus thuringiensis binds its receptor in Aedes aegypti mosquito larvae trough loop α-8 of domain II. FEBS Lett. 579, 3508-3514.
16. Tuntitippawan, T., Boonserm, P., Katzenmeier, G., and Angsuthanasombat, C. (2005) Targeted mutagenesis of loop residues in the receptor-binding domain of the Bacillus thuringiensis Cry4Ba toxin affects larvicidal activity. FEMS Microbiol. Lett. 242, 325-332. (Pubitemid 40038406)
17. Pérez, C., Muñoz-Garay, C., Portugal, L. C., Sánchez, J., Gill, S. S., Soberón, M., and Bravo, A. (2007) Bacillus thuringiensis subsp. israelensis Cyt1Aa enhances activity of Cry11Aa toxin by facilitating the formation of a pre-pore oligomeric structure. Cell. Microbiol. 9, 2931-2937. (Pubitemid 350066576)
18. Chang, C., Yu, Y. M., Dai, S. M., Law, S. K., and Gill, S. S. (1993) 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. (Pubitemid 23072361)
19. Lereclus, D., Arantes, O., Chaufaux, J., and Lecadet, M.-M. (1989) Transformation and expression of a cloned δ-endotoxin gene in Bacillus thuringiensis. FEMS Microbiol. Lett. 60, 211-218. (Pubitemid 19172381)
20. Lereclus, D., Agaisse, H., Gominet, M., and Chaufaux, J. (1995) Overproduction encapsulated insecticidal crystal proteins in a Bacillus thuringiensis spoOA mutant. Bio/Technol. 13, 67-71.
21. Thomas, W. E., and Ellar, D. J. (1983) Bacillus thuringiensis var israelensis crystal delta-endotoxin: effects on insect and mammalian cells in vitro and in vivo. J. Cell Sci. 60, 181-197.
22. Herrera-Ortiz, A., Lanz-Mendoza, H., Martínez-Barnetche, J., Hernández-Martínez, S., Villarreal-Treviño, Aguilar-Marcelino, L., and Rodríguez, M. H. (2004) Plasmodium berghei ookinetes induce nitric oxide production in Anopheles pseudopunctipennis midguts cultured in vitro. Insect Biochem. Mol. Biol. 34, 893-901. (Pubitemid 40047467)
23. Jin, X., Aimanova, K., Ross, L. S., and Gill, S. S. (2003) Identification, functional characterization and expression of a LAT type amino acid transporter from the mosquito Aedes aegypti. Insect Biochem. Mol. Biol. 33, 815-827. (Pubitemid 36922282)
24. Nielsen-LeRoux, C., and Charles, J. F. (1992) Binding of Bacillus sphaericus binary toxin to a specific receptor on midgut brush-border membranes from mosquito larvae. Eur. J. Biochem. 210, 585-590.
25. Kramer, A., and Schneider-Mergener, J. (1988) Synthesis and screening of peptide libraries on continuous cellulose membrane supports. Methods Mol. Biol. 87, 25-39.
26. Perera, O. P., Willis, J. D., Adang, M. J., and Jurat-Fuentes, J. L. (2009) Cloning and characterization of the Cry1Ac-binding alkaline phosphatase (HvALP) from Heliothis virescens. Insect Biochem. Mol. Biol. 39, 294-302.
27. De Backer, M., McSweeney, S., Rasmussen, H. B., Riise, B. W., Lindley, P., and Hough, E. (2002) The 1.9 Å crystal structure of heat-labile shrimp alkaline phosphatase. J. Mol. Biol. 318, 1265-1274. (Pubitemid 34753996)
28. Yamagiwa, M., Ogawa, R., Yasuda, K., Natsuyama, H., Sen, K., and Sakai, H. (2002) Active form of dipteran-specific insecticidal protein cryllA produced by Bacillus thuringiensis subsp. israelensis. Biosci. Biotechnol. Biochem. 66, 516-522. (Pubitemid 39251006)
29. Jurat-Fuentes, J. L., and Adang, M. J. (2004) Characterization of a Cry1Ac-receptor alkaline phosphatase in susceptible and resistant Heliothis virescens larvae. Eur. J. Biochem. 271, 3127-3135.
30. Valaitis, A. P., Jenkins, J. L., Lee, M. K., Dean, D. H., and Garner, K. J. (2001) 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. Insect Biochem. Physiol. 46, 186-200.
31. Ochoa-Campuzano, C., Real, M. D., Martínez-Ramírez, A. C., Bravo, A., and Rausell, C. (2007) An ADAM metalloprotease is a Cry3Aa Bacillus thuringiensis toxin receptor. Biochem. Biophys. Res. Commun. 362, 437-442.
32. Jenkins, J. L., Lee, M. K., Valaitis, A. P., Curtiss, A, and Dean, D. H. (2000) Bivalent sequential binding model of a Bacillus thuringiensis toxin to gypsy moth aminopeptidase N receptor. J. Biol. Chem. 275, 14423-14431. (Pubitemid 30339728)
33. Pardo-López, L., Gómez, I., Rausell, C., Sánchez, J., Soberón, M., and Bravo, A. (2006) Structural changes of the Cry1Ac oligomeric pre-pore from Bacillus thuringiensis induced by N-acetylgalactosamine facilitates toxin membrane insertion. Biochemistry 45, 10329-10336. (Pubitemid 44384808)