caa a22 4500 475746872 CHVBK 20180406123515.0 cr unu---uuuuu 170329e20001001xx s 000 0 eng 10.1007/s002840010134 doi (NATIONALLICENCE)springer-10.1007/s002840010134 Toxicity and Receptor Binding Properties of Bacillus thuringiensis δ-Endotoxins to the Midgut Brush Border Membrane Vesicles of the Rice Leaf Folders, Cnaphalocrocis medinalis and Marasmia patnalis [Elektronische Daten] [Shahid Karim, D. H. Dean] Pesticidal activity and receptor-binding properties of Bacillus thuringiensis toxins to rice leaf folders, Cnaphalocrocis medinalis and Marasmia patnalis, were investigated. Saturation and competition binding experiments were done with iodine (1251)-labeled Bt proteins and brush border membrane vesicles prepared from the midgut of C. medinalis and M. patnalis. The results show saturable, specific, and high-affinity binding of all toxins except Cry2A toxin. Cry1Aa and Cry2A toxins were bound with low affinity but with high binding site concentration. Heterologous competition experiments showed that Cry1Aa, Cry1Ab, and Cry1Ac recognized or shared the same binding site that is different from the binding site for Cry2A toxin. Iodine (125I)-labeled Cry1Ac and Cry1Ab toxins were used in ligand blot experiments to detect specific binding proteins in brush border membrane vesicles of C. medinalis and M. patnalis. Cry1Ab toxin protein binds to 205-kDa and 200-kDa proteins respectively in case of C. medinalis and M. patnalis. The apparent molecular mass of the protein bound to labeled Cry1Ac toxins was identified as a 120-kDa protein in both C. medinalis and M. patnalis. Springer-Verlag New York Inc., 2000 Karim Shahid Department of Biochemistry, Ohio State University, Columbus, OH 43210, USA, US aut Dean D. H. Department of Biochemistry, Ohio State University, Columbus, OH 43210, USA, US aut https://doi.org/10.1007/s002840010134 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s002840010134 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Karim Shahid Department of Biochemistry, Ohio State University, Columbus, OH 43210, USA, US aut NATIONALLICENCE 700 1- Dean D. H. Department of Biochemistry, Ohio State University, Columbus, OH 43210, USA, US aut Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer