Identification of Aminopeptidase-N2 as a Cry2Ab binding protein in Manduca sexta.
Peptides
; 98: 93-98, 2017 Dec.
Article
em En
| MEDLINE
| ID: mdl-28108197
ABSTRACT
Bacillus thuringiensis Cry2Ab toxin has been used in combination with Cry1Ac for resistance management on the Bt-cotton that is widely planted worldwide. However, little is known regarding Cry2Ab mode of action. Particularly, there is a gap of knowledge on the identification of insect midgut proteins that bind Cry2Ab and mediate toxicity. In the case of Cry1Ab toxin, a transmembrane cadherin protein and glycosyl-phosphatidylinositol (GPI) anchored proteins like aminopeptidase-N1 (APN1) or alkaline-phosphatase (ALP) from Manduca sexta, have been shown to be important for oligomer formation and insertion into the membrane. Binding competition experiments showed that Cry2Ab toxin does not share binding sites with Cry1Ab toxin in M. sexta brush border membrane vesicles (BBMV). Also, that Cry2Ab shows reduced binding to the Cry1Ab binding molecules cadherin, APN1 or ALP. Finally, ligand blot experiments and protein sequence by LC-MS/MS identified APN2 isoform as a Cry2Ab binding protein. Cloning and expression of APN2 confirmed that APN2 is a Cry2Ab binding protein.
Palavras-chave
Texto completo:
1
Coleções:
01-internacional
Temas:
Geral
Base de dados:
MEDLINE
Assunto principal:
Proteínas de Bactérias
/
Receptores de Superfície Celular
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Manduca
/
Antígenos CD13
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Proteínas de Insetos
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Endotoxinas
/
Proteínas Hemolisinas
Tipo de estudo:
Diagnostic_studies
Limite:
Animals
Idioma:
En
Revista:
Peptides
Ano de publicação:
2017
Tipo de documento:
Article
País de afiliação:
México