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A cadherin‐like protein functions as a receptor for Bacillus thuringiensis Cry1Aa and Cry1Ac toxins on midgut epithelial cells of Bombyx mori larvae
Author(s) -
Hara Hirotaka,
Atsumi Shogo,
Yaoi Katsuro,
Nakanishi Kazuko,
Higurashi Satoshi,
Miura Nami,
Tabunoki Hiroko,
Sato Ryoichi
Publication year - 2003
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(03)00117-0
Subject(s) - midgut , cry1ac , bombyx mori , bacillus thuringiensis , microbiology and biotechnology , aminopeptidase , biology , cadherin , lytic cycle , proteases , cell , biochemistry , larva , immunology , amino acid , bacteria , transgene , gene , botany , genetically modified crops , genetics , leucine , virus , enzyme
Aminopeptidase N (APN) and cadherin‐like protein (BtR175) from Bombyx mori larvae were examined for their roles in Cry1Aa‐ and Cry1Ac‐induced lysis of B. mori midgut epithelial cells (MECs). APNs and BtR175 were present in all areas of the midgut, were particularly abundant in the posterior region, and were found only on columnar cell microvilli and not on the lateral membrane that makes cell–cell contacts. This distribution was in accordance with the distribution of Cry1A‐susceptible MECs in the midgut. The lytic activity of Cry1Aa and Cry1Ac on collagenase‐dissociated MECs was linearly dependent on toxin concentration. Although pre‐treatment of MECs with anti‐BtR175 antibody was observed to partially inhibit the lytic activity exerted by 0.1–1 nM Cry1Aa toxin or 5 nM Cry1Ac toxin, no significant inhibition was observed when MECs were pre‐treated with anti‐APN antibody. These results suggest that BtR175 functions as a major receptor for Cry1A toxins in the midgut of B. mori larvae.