In-silico Determination of Insecticidal Potential in Lepidopteron Specific Crystal Toxins with Midgut Alkaline Phosphatase Using Molecular Docking

Alkaline phosphatase (ALP) enzyme plays an important role in binding of lepidopteran specific insecticidal crystal toxins Cry1Ac and Cry1Ab on GPI-anchored membrane receptor. In most of the cases crystal toxin interaction with ALP or Aminopeptidase N (APN) mediated by the terminal N-acetyl galactosamine (GalNAc) moiety. Among toxins Cry1Ac (PDB Id-4ARY) and Cry1Ab (PDB Id -n642) expresses less binding affinity about (−5.79 and -5.62) to GalNAc inALP orAPN region, respectively. The diptera specific crystal toxins Cry4Ba structure resembles to the lepidopteran specific toxins as it mimics like Cry1Aa for binding to ALP receptor by showing least binding affinity about (−6.99). Cry4Ba may be repurposed along with the novel Bt crystal toxins for lepidopteron insects as toxicity over Cry1Ac or Cry1Ab which will effective to bind with ALP or APN for toxin receptor interaction and help to minimize the rate of resistance. The Cry4Ba pyramided in combination with other Cry genes in different crops like cotton and maize would be an efficient strategy to increase crop protection by delaying the lepidopteran insect resistance.