New insight to structure-function relationship of GalNAc mediated primary interaction between insecticidal Cry1Ac toxin and HaALP receptor of Helicoverpa armigera.

ABSTRACT: Over the last few decades Cry1Ac toxin has been widely used in controlling the insect attack due to its high specificity towards target insects. The pore-forming toxin undergoes a complex mechanism in the insect midgut involving sequential interaction with specific glycosylated receptors in which terminal GalNAc molecule plays a vital role. Recent studies on Cry toxins interactions with specific receptors revealed the importance of several amino acid residues in domain III of Cry1Ac, namely Q509, N510, R511, Y513 and W545, serve as potential binding sites that surround the putative GalNAc binding pocket and mediate the toxin-receptor interaction. In the present study, alanine substitution mutations were generated in the Cry1Ac domain III region and functional significance of those key resi

SUBMITTER: Sengupta A 

PROVIDER: S-EPMC3813429 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature