A Novel 96-kDa Aminopeptidase Localized on Epithelial Cell Membranes of Bombyx mori Midgut, Which Binds to Cry1Ac Toxin of Bacillus thuringiensis

2006 ◽  
Vol 139 (2) ◽  
pp. 223-233 ◽  
Author(s):  
Yasuyuki Shitomi ◽  
Tohru Hayakawa ◽  
Delwar M. Hossain ◽  
Masahiro Higuchi ◽  
Kazuhisa Miyamoto ◽  
...  
Keyword(s):  
Bacillus Thuringiensis ◽  
Epithelial Cell ◽  
Bombyx Mori ◽  
Cell Membranes ◽  
Cry1ac Toxin

Transcriptome reveal the response to Cry1Ac toxin in susceptible Bombyx mori

2021 ◽  
Author(s):  
Sheng Qin ◽  
Shu Zhang ◽  
Xia Sun ◽  
Yunhui Kong ◽  
Chengxiang Hou ◽  
...  
Keyword(s):  
Bombyx Mori ◽  
Cry1ac Toxin

scholarly journals Blocking binding of Bacillus thuringiensis Cry1Aa to Bombyx mori cadherin receptor results in only a minor reduction of toxicity

2008 ◽  
Vol 9 (1) ◽  
pp. 3 ◽  
Author(s):  
Taek H You ◽  
Mi K Lee ◽  
Jeremy L Jenkins ◽  
Oscar Alzate ◽  
Donald H Dean
Keyword(s):  
Bacillus Thuringiensis ◽  
Bombyx Mori ◽  
A Minor

Binding of Phylogenetically Distant Bacillus thuringiensis Cry Toxins to a Bombyx mori Aminopeptidase N Suggests Importance of Cry Toxin's Conserved Structure in Receptor Binding

1999 ◽  
Vol 39 (1) ◽  
pp. 14-20 ◽  
Author(s):  
Ayaka Shinkawa ◽  
Katsuro Yaoi ◽  
Tomoyuki Kadotani ◽  
Morikazu Imamura ◽  
Nobuo Koizumi ◽  
...  
Keyword(s):  
Bacillus Thuringiensis ◽  
Bombyx Mori ◽  
Receptor Binding ◽  
Aminopeptidase N ◽  
Cry Toxins

scholarly journals Characterization of glycopeptides labelled from d-[2-3H]mannose and l-[6-3H]fucose in intestinal epithelial cell membranes during differentiation

1980 ◽  
Vol 192 (1) ◽  
pp. 145-153 ◽  
Author(s):  
A Herscovics ◽  
B Bugge ◽  
A Quaroni ◽  
K Kirsch
Keyword(s):  
Epithelial Cell ◽  
Intestinal Epithelial Cell ◽  
Time Course ◽  
Cell Membranes ◽  
Alkali Treatment ◽  
Gel Filtration ◽  
Intestinal Epithelial ◽  
Membrane Glycoproteins ◽  
High Mannose ◽  
Fraction I

The labelled glycopeptides obtained by Pronase digestion of rat intestinal epithelial cell membranes were examined by gel filtration after injection of D-[2-3H]mannose and L-[6-3H]fucose. Three labelled fraction were eluted in the following order from Bio-Gel P-6, Fraction I, which was excluded from the gel, was labelled mostly with [3H]fucose and slightly with [3H]mannose. Fraction II contained “complex” asparagine-linked oligosaccharides since it was labelled with [3H]mannose and [3H]fucose, was stable to mild alkali treatment, and resistant to endo-beta-N-acetyl-glucosaminidase H. Fraction III contained “high-mannose” asparagine-linked oligosaccharides, which were labelled with [3H]mannose, but not with [3H]fucose; these were sensitive to endo-beta-N-acetylglucosaminidase H, and were adsorbed on concanavalin A-Sepharose and subsequently eluted with methyl alpha-D-mannopyranoside. The time course of incorporation of [3H]mannose into these glycopeptides in microsomal fractions showed that high-mannose oligosaccharides were precursors of complex oligosaccharides. The rate of this processing was faster in rapidly dividing crypt cells than in differentiated villus cells. The ratio of radioactively labelled complex oligosaccharides to high-mannose oligosaccharides, 3h after [3H]mannose injection, was greater in crypt than in villus-cell lateral membranes. Luminal membranes of both crypt and villus cells were greatly enriched in labelled complex oligosaccharides compared with the labelling in lateral-basal membranes. These studies show that intestinal epithelial cells are polarized with respect to the structure of the asparagine-linked oligosaccharides on their membrane glycoproteins. During differentiation of these cells quantitative differences in labelled membrane glycopeptides, But no major qualitative change, were observed.

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