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The cadherin‐like protein is essential to specificity determination and cytotoxic action of the Bacillus thuringiensis insecticidal CryIAa toxin
Author(s) -
Nagamatsu Yasunori,
Koike Takashi,
Sasaki Kazuhiro,
Yoshimoto Akihiro,
Furukawa Yasuo
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01327-7
Subject(s) - bacillus thuringiensis , toxin , spodoptera , sf9 , anthrax toxin , bombyx mori , brush border , biology , microbiology and biotechnology , midgut , exotoxin , cadherin , biochemistry , membrane , cell , bacteria , recombinant dna , gene , vesicle , fusion protein , botany , genetics , larva
The Bacillus thuringiensis CryIAa toxin binds a cadherin‐like protein (BtR175) on the brush‐border membranes of the Bombyx mori midgut columnar cells, which are the targets. By introducing the BtR175 gene with a baculovirus, Spodoptera frugiperda Sf9 cells expressed BtR175 protein on the cell membrane and became susceptible to the CryIAa toxin. The toxin bound the cadherin repeat adjacent to the membrane and made a pore that passed inorganic ions, causing the cell to swell and burst. This was not observed with a BtR175 variant lacking the toxin‐binding site. This in vitro experiment mimicked the specific insecticidal action of the toxin in vivo well.