A membrane associated metalloprotease cleaves Cry3Aa Bacillus thuringiensis toxin reducing pore formation in Colorado potato beetle brush border membrane vesicles

Insect proteases are implicated in Bacillus thuringiensis insecticidal proteins mode of action determining toxin specificity and sensitivity. Few data are available on the involvement of proteases in the later steps of toxicity such as protease interaction with toxin-receptor complexes and the pore...

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Detalles Bibliográficos
Autores: Rausell, C, Ochoa-Campuzano, C, Martínez-Ramirez, AC, Bravo, A, Real, MD
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2007
País:México
Institución:Universidad Nacional Autónoma de México
Repositorio:Sistema de Información de la Facultad de Ciencias, UNAM
OAI Identifier:oai:repositorio.fciencias.unam.mx:11154/1086
Acceso en línea:http://hdl.handle.net/11154/1086
Access Level:acceso abierto
Palabra clave:Biochemistry & Molecular Biology
Biophysics
Bacillus thuringiensis
colorado potato beetle
insecticidal toxin
protease
Cry3Aa proteolysis
pore formation
Descripción
Sumario:Insect proteases are implicated in Bacillus thuringiensis insecticidal proteins mode of action determining toxin specificity and sensitivity. Few data are available on the involvement of proteases in the later steps of toxicity such as protease interaction with toxin-receptor complexes and the pore formation process. In this study, a Colorado potato beetle (CPB) midgut membrane metalloprotease was found to be involved in the proteolytic processing of Cry3Aa. Interaction of Cry3Aa with BBMV membrane proteases resulted in a distinct pattern of proteolysis. Cleavage was demonstrated to occur in protease accessible regions of domain III and was specifically inhibited by the metalloprotease inhibitors 1,10-phenanthroline and acetohydroxamic acid. Proteolytic inhibition by a peptide representing a segment of proteolysis in domain III and the metalloprotease inhibitor acetohydroxamic acid correlated with increased pore formation, evidencing that Cry3Aa is a specific target of a CPB membrane metalloprotease that degrades potentially active toxin. (c) 2007 Elsevier B.V. All rights reserved.