A 104 kDa Aedes aegypti aminopeptidase N is a putative receptor for the Cry11Aa toxin from Bacillus thuringiensis subsp. israelensis.
A 104 kDa Aedes aegypti aminopeptidase N is a putative receptor for the Cry11Aa toxin from Bacillus thuringiensis subsp. israelensis.
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DOI:
10.1016/j.ibmb.2013.09.007
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发表时间:
2013-12
影响因子:
3.8
通讯作者:
Gill, Sarjeet S.
中科院分区:
文献类型:
--
作者:
Chen, Jianwu;Likitvivatanavong, Supaporn;Aimanova, Karlygash G.;Gill, Sarjeet S.
The Cry11Aa protein produced in Bacillus thuringiensis subsp. israelensis, a bacterial strain used worldwide for the control of Aedes aegypti larvae, binds midgut brush border membrane vesicles (BBMV) with an apparent Kd of 29.8 nM. Previously an aminopeptidase N (APN), named AaeAPN2, was identified as a putative Cry11Aa toxin binding protein by pull-down assays using biotinylated Cry11Aa toxin ( Insect Biochem Mol Biol., 39: 688–696). Here we show this protein localizes to the apical membrane of epithelial cells in proximal and distal regions of larval caeca. The AaeAPN2 protein binds Cry11Aa with high affinity, 8.6 nM. The full-length and fragments of AaeAPN2 were cloned and expressed in Escherichia coli. The toxin-binding region was identified and further competitive assays demonstrated that Cry11Aa binding to BBMV was efficiently competed by the full-length AaeAPN2 and the fragments of AaeAPN2b and AaeAPN2e. In bioassays against Ae. aegypti larvae, the presence of full-length and a partial fragment (AaeAPN2b) of AaeAPN2 enhanced Cry11Aa larval mortality. Taken together, we conclude that AaeAPN2 is a binding protein and plays a role in Cry11Aa toxicity.
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影响因子:
--
作者:
Abdullah MA;Valaitis AP;Dean DH
通讯作者:
Dean DH
DOI:
10.1152/ajprenal.00487.2005
发表时间:
2007-05-01
影响因子:
4.2
作者:
Kang'ethe, Wanyoike;Aimanova, Karlygash G.;Gill, Sarjeet S.
通讯作者:
Gill, Sarjeet S.
影响因子:
3.8
作者:
Chen, Jianwu;Aimanova, Karlygash G.;Pan, Songqin;Gill, Sarjeet S.
通讯作者:
Gill, Sarjeet S.
影响因子:
4.4
作者:
Atsumi, S;Mizuno, E;Sato, R
通讯作者:
Sato, R
影响因子:
4.8
作者:
GILL, SS;COWLES, EA;FRANCIS, V
通讯作者:
FRANCIS, V