title: Compatibility of garlic (Allium sativum L.) leaf agglutinin and Cry1Ac δ-endotoxin for gene pyramiding.
abstract: δ-Endotoxins produced by Bacillus thuringiensis (Bt) have been used as bio-pesticides for the control of lepidopteran insect pests. Garlic (Allium sativum L.) leaf agglutinin (ASAL), being toxic to several sap-sucking pests and some lepidopteran pests, may be a good candidate for pyramiding with δ-endotoxins in transgenic plants for enhancing the range of resistance to insect pests. Since ASAL shares the midgut receptors with Cry1Ac in Helicoverpa armigera, there is possibility of antagonism in their toxicity. Our study demonstrated that ASAL increased the toxicity of Cry1Ac against H. armigera while Cry1Ac did not alter the toxicity of ASAL against cotton aphids. The two toxins interacted and increased binding of each other to brush border membrane vesicle (BBMV) proteins and to the two important receptors, alkaline phosphatase (ALP) and aminopeptidase N (APN). The results indicated that the toxins had different binding sites on the ALP and APN but influenced mutual binding. We conclude that ASAL can be safely employed with Cry1Ac for developing transgenic crops for wider insect resistance.
authors.affiliation: National Botanical Research Institute, Council of Scientific and Industrial Research, Rana Pratap Marg, Lucknow, UP, India.
authors.forename: Santosh Kumar
authors.initials: SK
authors.lastname: Upadhyay
authors.forename: Seema
authors.initials: S
authors.lastname: Singh
authors.forename: Krishnappa
authors.initials: K
authors.lastname: Chandrashekar
authors.forename: Rakesh
authors.initials: R
authors.lastname: Tuli
authors.forename: Pradhyumna Kumar
authors.initials: PK
authors.lastname: Singh
mesh_terms: D000373:Agglutinins / Q000235:genetics / Q000494:pharmacology*; D000469:Alkaline Phosphatase / Q000737:chemistry / Q000378:metabolism; D000818:Animals; D001042:Aphids / Q000737:chemistry / Q000187:drug effects / Q000201:enzymology / Q000254:growth & development; D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins / Q000235:genetics / Q000494:pharmacology*; D001665:Binding Sites; D018826:CD13 Antigens / Q000737:chemistry / Q000378:metabolism; D004347:Drug Interactions; D004731:Endotoxins / Q000235:genetics / Q000494:pharmacology*; D005737:Garlic / Q000737:chemistry*; D006460:Hemolysin Proteins / Q000235:genetics / Q000494:pharmacology*; D019476:Insect Proteins / Q000378:metabolism; D009036:Moths / Q000737:chemistry / Q000187:drug effects / Q000201:enzymology / Q000254:growth & development; D018515:Plant Leaves / Q000737:chemistry*; D011485:Protein Binding
chemical_list: D000373:Agglutinins; D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins; D004731:Endotoxins; D006460:Hemolysin Proteins; D019476:Insect Proteins; C030956:insecticidal crystal protein, Bacillus Thuringiensis; D000469:Alkaline Phosphatase; D018826:CD13 Antigens