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J. Biol. Chem., Vol. 277, Issue 16, 13863-13872, April 19, 2002
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From the Lipid rafts are characterized by their
insolubility in nonionic 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 glycosylphosphatidylinositol-anchored
proteins. In H. virescens and M. sexta,
pretreatment of membranes with the cholesterol-depleting reagent
saponin and methyl-
Heliothis virescens and Manduca sexta
Lipid Rafts Are Involved in Cry1A Toxin Binding to the Midgut
Epithelium and Subsequent Pore Formation*
§,§,§
Environmental Toxicology Graduate Program
and the § Department of Cell Biology and Neuroscience,
University of California, Riverside, California 92521 and the
¶ Instituto de Biotecnología, Departamento de
Microbiología, Universidad Nacional Autónoma de
México, Apdo. postal 510-3, Cuernavaca,
Morelos 62250, México
-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 and the 120-kDa aminopeptidase from M. sexta, were preferentially
partitioned into lipid rafts. Additionally, the leucine aminopeptidase
activity was enriched approximately 2-3-fold in these rafts compared
with 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 work was supported in part by the University of
California Agricultural Experimental Station; United States Department of Agriculture Grant 96-353-0-3820; fellowships from the University of
California Toxic Substances Research and Teaching Program (to M. Z. and D. I. O.); and Consejo Nacional de Ciencia y
Tecnologia (CONACYT) Grant 27637-N; Dirección de Apoyo al
Personal Académico-Universidad Nacional Autónoma de
México IN206200 and IN216300; and the University of California
Mexico-United States CONACYT grant.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: 5429 Boyce Hall,
Dept. of Cell Biology and Neuroscience, Environmental Toxicology Graduate Program, University of California, Riverside, CA 92521. Fax:
909-787-3087; E-mail: sarjeet.gill@ucr.edu.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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