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Pore-forming protein targeting western corn rootworm

Latest publication in Nature Communications:

Pore-forming proteins are soluble proteins able to oligomerize into rings and undergo huge conformational changes to punch holes in their target cell membrane. Bacillus thuringiensis (Bt) pore-forming proteins have been successfully employed to protect maize, as some of them show activity against the coleopteran western corn rootworm (WCR), a devastating pest whose larval feeding causes root injury, resulting in reduced grain production and difficult harvesting. However, the notorious adaptability of WCR leading to resistance to these proteins makes it imperative to discover novel proteins with different modes/sites of action, to replace existing transgenic traits.

We identified a bacterial protein active against WCR, Mpf2Ba1, demonstrated its utility for transgenic control of WCR, and carried out the first comprehensive structure-function characterization of a non-Bt protein, revealing key steps of pore formation. High-resolution structures of Mpf2Ba1 soluble monomer, pre-pore and membrane-inserted pore conformations reveal unprecedented atomic details of inter- and intramolecular changes during these transitions for membrane attack complex perforins (MACPFs). Most of these newly discovered changes are conserved in bacterial MACPFs, adding insights into their mode of action. Our findings provide a mechanistic basis for Mpf2Ba1 effectiveness as an insecticidal protein, with excellent potential for biotechnology applications for food security.

Read the full publication as a preprint here.



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