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In the everlasting races against the pests of agricultural importance, it is essential to develop a novel strategy for pest control.
For this a thorough understanding of biological system of the insect pest at the cellular and molecular levels is needed.
For instance, the recent trend involves the identification and characterization of physiologically and metabolically important
proteins like insect vitellogenin, vitellogenin receptor, storage protein and apolipoporin which can be subjected to various
refinements and manipulations for exploitation in pest management, in a target specific and eco-friendly manner. In the
present investigation, we have studied the vitellogenin and vitellogenin receptor interaction. The N-terminal Ligand Binding
Domain (LBD) of vitellogenin receptor is responsible for the transportation of vital protein (Vitellogenin) to the developing
oocyte through receptor mediated endocytosis pathway. Ligand binding domain (LBD) sequence of B. mori noted to be
completely different with that of Spodoptera litura though these two insects are coming under the lepidopteran group.The motif
in the LBD were also species specific. VgR LBD from B. mori and S. litura were isolated and cloned in pET30a+ vector for over
expression for structural studies. Since both insect with same order but LBD differences have pave way for understanding and
implementing a new approach for species specific target drug development to inhibit the binding of Vg to the receptor specific
to insect pest Spodoptera litura without affecting non-targeted system.
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