| Literature DB >> 18226423 |
Luisa Elena Fernández1, Isabel Gómez, Sabino Pacheco, Iván Arenas, Sarjeet S Gilla, Alejandra Bravo, Mario Soberón.
Abstract
Phage display is an in vitro method for selecting polypeptides with desired properties from a large collection of variants. The insecticidal Cry toxins produced by Bacillus thuringiensis are highly specific to different insects. Various proteins such as cadherin, aminopeptidase-N (APN) and alkaline phosphatase (ALP) have been characterized as potential Cry-receptors. We used phage display to characterize the Cry toxin-receptor interaction(s). By employing phage-libraries that display single-chain antibodies (scFv) from humans or from immunized rabbits with Cry1Ab toxin or random 12-residues peptides, we have identified the epitopes that mediate binding of lepidopteran Cry1Ab toxin with cadherin and APN receptors from Manduca sexta and the interaction of dipteran Cry11Aa toxin with the ALP receptor from Aedes aegypti. Finally we displayed in phages the Cry1Ac toxin and discuss the potential for selecting Cry variants with improved toxicity or different specificity.Entities:
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Year: 2007 PMID: 18226423 PMCID: PMC2267870 DOI: 10.1016/j.peptides.2007.07.035
Source DB: PubMed Journal: Peptides ISSN: 0196-9781 Impact factor: 3.750