A striking feature of the CPB identified prohibitin-1 is the predicted presence
of cadherin elements, potential binding sites for Cry toxins described in other Bt susceptible insects. We
also showed that CPB prohibitin-1 protein partitioned into both, detergent soluble and insoluble membrane
fractions, as well as a prohibitin-2 homologous protein, previously reported to form functional
complexes with prohibitin-1 in other organisms. Prohibitin complexes act as membrane scaffolds ensuring
the recruitment of membrane proteases to facilitate substrate processing. Accordingly, sequestration
of prohibitin-1 by an anti-prohibitin-1 antibody impaired the Cry3Aa toxin inhibition of the proteolytic
cleavage of a fluorogenic synthetic substrate of an ADAM-like metalloprotease previously reported to
proteolize this toxin. In this work, we also demonstrated that prohibitin-1 RNAi silencing in CPB larvae
produced deleterious effects and together with a LD50 Cry3Aa toxin treatment resulted in a highly efficient
short term response since 100% larval mortality was achieved just 5 days after toxin challenge.
Therefore, the combination of prohibitin RNAi and Cry toxin reveals as an effective strategy to improve
crop protection.