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Papers In Press, published online ahead of print February 8, 2002
Department of Cell Biology and Neuroscience, University of California, Riverside, CA 92521
Corresponding Author: Sarjeet.gill{at}ucr.edu
Lipid rafts are characterized by their insolubility in non-ionic detergents such as Triton X-100 at 4°C. They have been studied in mammals where they play critical roles in protein sorting and signal transduction. To understand the potential role of lipid rafts in lepidopteran insects, we isolated and analyzed the protein and lipid components of these lipid raft microdomains from the midgut epithelial membrane of Heliothis virescens and Manduca sexta. Like their mammalian counterparts, H. virescens and M. sexta lipid rafts are enriched in cholesterol, sphingolipids, and GPI-anchored proteins. In H. virescens and M. sexta, pretreatment of membranes with the cholesterol-depleting reagent saponin and methyl-b-cyclodextrin differentially disrupted the formation of lipid rafts, indicating an important role for cholesterol in lepidopteran lipid rafts structure. We showed that several putative Bacillus thuringiensis Cry1A receptors, including the 120- and 170-kDa aminopeptidases from H. virescens, the 120-kDa aminopeptidase from M. sexta, were preferentially partitioned into lipid rafts. Additionally the leucine aminopeptidase activity was enriched approximately two to three fold in these rafts compared to brush border membrane vesicles. We also demonstrated that Cry1A toxins were associated with lipid rafts, and that lipid raft integrity was essential for in vitro Cry1Ab pore-forming activity. Our study strongly suggests that these microdomains might be involved in Cry1A toxin aggregation and pore formation. This is the first study that demonstrated the association of B. thuringiensis Cry toxins with lipid rafts.
J. Biol. Chem, 10.1074/jbc.M110057200
Submitted on October 18, 2001
Revised on February 6, 2002
Accepted on February 8, 2002
Heliothis virescens and Manduca sexta lipid rafts are involved in Cry1A toxin binding to the midgut epithelium and subsequent pore formation
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