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Toxin-Binding Proteins Isolated from Yellow Mealworm Tenebrio molitor and Wax Moth Galleria mellonella

N. V. Bulushova1*, D. P. Zhuzhikov2, L. I. Lyutikova2, N. E. Kirillova1, I. A. Zalunin1, and G. G. Chestukhina1

1Scientific Research Institute for Genetics and Selection of Industrial Microorganisms, 1-yi Dorozhnyi Proezd 1, 113545 Moscow, Russia; fax: (495) 315-0501; E-mail: nat86@yandex.ru; ingvarzal@mail.ru

2Faculty of Biology, Lomonosov Moscow State University, 119991 Moscow, Russia; fax: (495) 939-4309

* To whom correspondence should be addressed.

Received September 22, 2010; Revision received October 19, 2010
A 67-kDa protein that can specifically bind the activated Cry9A endotoxin under ligand-blotting conditions was purified from midgut epithelium apical membranes of wax moth Galleria mellonella by affinity chromatography. N-Terminal amino acid sequencing enabled identification of this protein as aminopeptidase N. In similar experiments, 66- and 58-kDa proteins specific to endotoxin Cry3A were isolated from the midgut epithelium apical membranes of Tenebrio molitor larvae. Mass spectrometry showed close similarity of the 58-kDa protein to the Tenebrio molitor α-amylase.
KEY WORDS: δ-endotoxin, Bacillus thuringiensis, Galleria mellonella, Tenebrio molitor, toxin-binding protein

DOI: 10.1134/S0006297911020064