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

---

N. V. Bulushova^1*, 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

---