NDLI: 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.

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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.

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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.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Gómez, Isabel Pacheco, Sabino Rodríguez-almazán, Claudia Soberón, Mario Arenas, Ivan Saab-rincon, Gloria Bravo, Alejandra Gill, Sarjeet S.
Description	Author Affiliation: Pacheco S ( Instituto de Biotecnología, Universidad Nacional Autónoma de México, Apdo. Postal 510-3, Cuernavaca 62250, Morelos, Mexico.)
Abstract	Bacillus thuringiensis Cry toxins are used worldwide as insecticides in agriculture, in forestry, and in the control of disease transmission vectors. In the lepidopteran Manduca sexta, cadherin (Bt-R(1)) and aminopeptidase-N (APN) function as Cry1A toxin receptors. The interaction with Bt-R(1) promotes cleavage of the amino-terminal end, including helix alpha-1 and formation of prepore oligomer that binds to APN, leading to membrane insertion and pore formation. Loops of domain II of Cry1Ab toxin are involved in receptor interaction. Here we show that Cry1Ab mutants located in domain II loop 3 are affected in binding to both receptors and toxicity against Manduca sexta larvae. Interaction with both receptors depends on the oligomeric state of the toxin. Monomers of loop 3 mutants were affected in binding to APN and to a cadherin fragment corresponding to cadherin repeat 12 but not with a fragment comprising cadherin repeats 7-12. In contrast, the oligomers of loop 3 mutants were affected in binding to both Bt-R(1) fragments but not to APN. Toxicity assays showed that either monomeric or oligomeric structures of Cry1Ab loop 3 mutations were severely affected in insecticidal activity. These data suggest that loop 3 is differentially involved in the binding with both receptor molecules, depending on the oligomeric state of the toxin and also that possibly a 'ping pong' binding mechanism with both receptors is involved in toxin action.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	47
Volume Number	284
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2009-11-20
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Antigens, CD13 Chemistry Bacillus Thuringiensis Metabolism Bacterial Proteins Cadherins Endotoxins Hemolysin Proteins Manduca Animals Circular Dichroism Larva Microbiology Microvilli Immunology Mutagenesis, Site-Directed Mutation Plasmids Protein Binding Protein Structure, Secondary Protein Structure, Tertiary Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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