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Specific binding of Bacillus thuringiensis Cry2A insecticidal proteins to a common site in the midgut of Helicoverpa species

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Specific binding of Bacillus thuringiensis Cry2A insecticidal proteins to a common site in the midgut of Helicoverpa species

dc.contributor.author	Hernández Rodríguez, Carmen Sara
dc.contributor.author	Van Vliet, A.
dc.contributor.author	Bautsoens, Nadine
dc.contributor.author	Van Rie, Jeroen
dc.contributor.author	Ferré Manzanero, Juan
dc.date.accessioned	2015-12-15T10:04:44Z
dc.date.available	2015-12-15T10:04:44Z
dc.date.issued	2008
dc.identifier.citation	Hernández Rodríguez, Carmen Sara Van Vliet, A. Bautsoens, Nadine Van Rie, Jeroen Ferré Manzanero, Juan 2008 Specific binding of Bacillus thuringiensis Cry2A insecticidal proteins to a common site in the midgut of Helicoverpa species Applied and Environmental Microbiology 74 24 7654 7659
dc.identifier.uri	http://hdl.handle.net/10550/49239
dc.description.abstract	For a long time, it has been assumed that the mode of action of Cry2A toxins was unique and different from that of other three-domain Cry toxins due to their apparent nonspecific and unsaturable binding to an unlimited number of receptors. However, based on the homology of the tertiary structure among three-domain Cry toxins, similar modes of action for all of them are expected. To confirm this hypothesis, binding assays were carried out with 125 I-labeled Cry2Ab. Saturation assays showed that Cry2Ab binds in a specific and saturable manner to brush border membrane vesicles (BBMVs) of Helicoverpa armigera. Homologous-competition assays with 125 I-Cry2Ab demonstrated that this toxin binds with high affinity to binding sites in H. armigera and Helicoverpa zea midgut. Heterologous-competition assays showed a common binding site for three toxins belonging to the Cry2A family (Cry2Aa, Cry2Ab, and Cry2Ae), which is not shared by Cry1Ac. Estimation of Kd (dissociation constant) values revealed that Cry2Ab had around 35-fold less affinity than Cry1Ac for BBMV binding sites in both insect species. Only minor differences were found regarding Rt (concentration of binding sites) values. This study questions previous interpretations from other authors performing binding assays with Cry2A toxins and establishes the basis for the mode of action of Cry2A toxins.
dc.language.iso	eng
dc.relation.ispartof	Applied and Environmental Microbiology, 2008, vol. 74, num. 24, p. 7654-7659
dc.subject	Proteïnes
dc.subject	Bioquímica
dc.subject	Microbiologia
dc.subject	Plaguicides
dc.subject	Biotecnologia agrícola
dc.title	Specific binding of Bacillus thuringiensis Cry2A insecticidal proteins to a common site in the midgut of Helicoverpa species
dc.type	journal article	es_ES
dc.date.updated	2015-12-15T10:04:44Z
dc.identifier.doi	10.1128/AEM.01373-08
dc.identifier.idgrec	048688
dc.rights.accessRights	open access	es_ES