title: Composition of the Putative Prepore Complex ofBacillus thuringiensisCry1Ab Toxin.
abstract: Prepore formation is hypothesized to be an obligate step in the insertion of Cry1Ab toxin into insect brush border membrane vesicles. We examined the architecture of the putative prepore when isolated using the published protocols [1] [2]. Our results demonstrate that the putative prepore form of Cry1Ab is a combination of receptor proteins attached to the toxin, when purified. The results also suggest that this prepore form as prepared by the methods published is different from other membrane-extracted oligomeric forms of Cry toxins and prepore of other toxins in general. While most other known prepores are composed of multimers of a single protein, the Cry1Ab prepore, as generated, is a protein-receptor complex oligomer and monomers of Cry toxins.
authors.affiliation: Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH, USA ; Aaron Diamond AIDS Research Center, Rockefeller University, New York, NY, USA.
authors.forename: Manoj S
authors.initials: MS
authors.lastname: Nair
authors.affiliation: Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH, USA.
authors.forename: Donald H
authors.initials: DH
authors.lastname: Dean
keywords: Brush Border Membrane Vesicles; Cry1Ab Protein; LC-MS/MS; Prepore; Protein-Receptor Interactions; Small Unilamellar Vesicles