Abstract:
:Galectins are a family of β-galactoside binding proteins, and insect galectins play a role in immune responses and may also affect Cry toxin activity. In this study, we aimed to further understand the function and molecular mechanism of Aedes aegypti galectin-6 in modulation of Cry11Aa toxicity. A. aegypti galectin-6 was cloned, and the recombinant galectin-6 was expressed and purified. Bioassays indicated that galectin-6 could reduce the toxicity of Cry11Aa, protecting A. aegypti larvae. To determine interactions among galectin-6, Cry11Aa and putative toxin receptors, Octet Red System, western blotting, far-western blotting and ELISA assays were performed. Octet Red System showed that galectin-6 bound to BBMVs of A. aegypti larvae with lower affinity than that of Cry11Aa. Western blotting and far-western blotting analyses demonstrated that galectin-6 bound to A. aegypti ALP1 and APN2 as well as to BBMVs, consistent with the results of ELISA and protein docking simulations. However, galectin-6 did not bind to Cadherin in far-western blotting or ELISA assay, though the protein docking simulations suggested their binding potential. These findings support the conclusion that galectin-6 may block Cry11Aa from binding to ALP1 and APN2 due to structural similarity, which might decrease the mosquitocidal toxicity of Cry11Aa.
journal_name
Pestic Biochem Physioljournal_title
Pesticide biochemistry and physiologyauthors
Hu X,Chen H,Xu J,Zhao G,Huang X,Liu J,Batool K,Wu C,Wu S,Huang E,Wu J,Chowhury M,Zhang J,Guan X,Yu XQ,Zhang Ldoi
10.1016/j.pestbp.2019.09.010subject
Has Abstractpub_date
2020-01-01 00:00:00pages
96-104eissn
0048-3575issn
1095-9939pii
S0048-3575(19)30462-6journal_volume
162pub_type
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