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Bacillus thuringiensis Cry1Ab, but not Cry1Aa or Cry1Ac, disrupts liposomes |
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| Authors: | Taisuke Kato Ryo Endo Kousuke Haginoya Tohru Hayakawa Ryoichi Sato |
| Institution: | a Graduate School of Science and Technology, Niigata University, Niigata 950-2181, Japan b Advanced Technology Institute, Kubota Corporation, Ibaraki 301-0852, Japan c Graduate School, Tokyo University of Agriculture and Technology, Tokyo 184-8588, Japan |
| Abstract: | We evaluated the ability of Cry1Aa9, Cry1Ab4, and Cry1Ac1 insecticidal toxins from Bacillus thuringiensis to destroy liposomes. Cry1A toxins are thought to form pores in midgut apical cell membranes (BBMV), thereby disrupting midgut cells. Liposomes containing fluorescent calcein were prepared using phosphatidylcholine (PC) and phosphatidylserine (PS) (PC/PS-Liposomes) or PC alone (PC-Liposomes). Cry1Ab (1.4 μM), but not Cry1Aa or Cry1Ac, disrupted PC/PS-Liposomes and PC-Liposomes. PC/PS-Liposomes containing cholesterol and oligosaccharylceramide from Plutella xylostella midgut were damaged even more extensively by Cry1Ab, but the inclusion of either lipid alone had no effect. The initial velocity of Cry1Ab-mediated liposome disruption increased 17-fold when liposomes were prepared with Triton X-100-soluble proteins from Bombyx mori BBMV and PC (PC/Proteo-Liposomes), and Cry1Aa and Cry1Ac also caused slight disruption. These data suggest that Cry1Ab achieves higher penetration into PC/PS-Liposomes, PC-Liposomes, and PC/Proteo-Liposomes compared with Cry1Aa or Cry1Ac and that Cry1Ab may interact with membrane proteins. |
| Keywords: | Bacillus thuringiensis Insecticidal Cry1A toxins Liposome Calcein Phosphatidylcholine Phosphatidylserine Brush border membrane vesicle Bombyx mori |
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