Dangerous Cry4B toxin found to be mediated by BT-R3
The Cry4B toxins are produced by Bacillus thuringiensis, which exert their insecticidal activity when they bind with high-affinity recreports on epithelial cells. When Cry4B binds with BT-R3, this starts a cell death pathways and can kill dangerous diseases like malaria.
"This kind of strategy will facilitate protein design for creation of new customized Cry proteins and peptide mimics that might be more effective than the natural toxins themselves against Anopheles gambiae and other mosquitoes, and, hopefully, less able to bring about insect host resistance," Dr. Mohamed Ibrahim, the senior author of the paper, said.
This new approach to malaria control is needed in a market where there are no current vaccines for the devastating disease. Using BT-R3 to bind Cry4B is a new approach that utilizes proteomics, genomics and bioinformatics to identify target proteins.
"Lee Bulla and his colleagues have combined genomics, proteomics and in silico analysis to establish the role of the cadherin receptor BT-R3 in the killing action of Cry4B mosquito toxin," Dr. Steve Goodman, the editor-in-chief of Experimental Biology and Medicine, said. "Understanding of this Cry4B-BT-R3 complex will allow the design of custom proteins and peptides to help control the spread of malaria by mosquitoes."