Interaction of Bacillus thuringiensis Cry1 and Vip3A Proteins with Spodoptera frugiperda Midgut Binding Sites

Vip3Aa, Vip3Af, Cry1Ab, and Cry1Fa were tested for their toxicities and binding interactions. Vip3A proteins were more toxic than Cry1 proteins. Binding assays showed independent specific binding sites for Cry1 and Vip3A proteins. Cry1Ab and Cry1Fa competed for the same binding sites, whereas Vip3Aa...

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Bibliographic Details
Published in:	Applied and Environmental Microbiology Vol. 75; no. 7; pp. 2236 - 2237
Main Authors:	Sena, Janete A.D, Hernández-Rodríguez, Carmen Sara, Ferré, Juan
Format:	Journal Article
Language:	English
Published:	United States American Society for Microbiology 01-04-2009 American Society for Microbiology (ASM)
Subjects:	Animals Bacillus thuringiensis - physiology Bacteria Bacterial proteins Bacterial Proteins - metabolism Bacterial Proteins - toxicity Binding sites Endotoxins - metabolism Endotoxins - toxicity Gastrointestinal Tract - microbiology Hemolysin Proteins - metabolism Hemolysin Proteins - toxicity Invertebrate Microbiology Larva - drug effects Lethal Dose 50 Microbiology Protein Binding Spodoptera - microbiology Toxicity
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Summary:	Vip3Aa, Vip3Af, Cry1Ab, and Cry1Fa were tested for their toxicities and binding interactions. Vip3A proteins were more toxic than Cry1 proteins. Binding assays showed independent specific binding sites for Cry1 and Vip3A proteins. Cry1Ab and Cry1Fa competed for the same binding sites, whereas Vip3Aa competed for those of Vip3Af.
Bibliography:	Present address: Universidade Estadual Paulista, Faculdade de Ciências Agrárias e Veterinárias, Departamento de Biologia Aplicada a Agropecuaria, Jaboticabal, São Paulo, Brazil. Corresponding author. Mailing address: Departamento de Genética, Facultad de CC. Biológicas, Dr. Moliner 50, 46100-Burjassot, Valencia, Spain. Phone: (34) 96 354 4506. Fax: (34) 96 354 3029. E-mail: juan.ferre@uv.es
ISSN:	0099-2240 1098-5336
DOI:	10.1128/AEM.02342-08