Effects of Destruxin A on Silkworm’s Immunophilins
Destruxin A (DA), a major secondary metabolite of <i>Metarhizium anisopliae</i>, has anti-immunity to insects. However, the detailed mechanism and its interactions with target proteins are elusive. Previously, three immunophilins, peptidyl−prolyl cis−trans isomerase (...
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MDPI AG
2019-06-01
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author | Jingjing Wang Qunfang Weng Qiongbo Hu |
author_facet | Jingjing Wang Qunfang Weng Qiongbo Hu |
author_sort | Jingjing Wang |
collection | DOAJ |
description | Destruxin A (DA), a major secondary metabolite of <i>Metarhizium anisopliae</i>, has anti-immunity to insects. However, the detailed mechanism and its interactions with target proteins are elusive. Previously, three immunophilins, peptidyl−prolyl cis−trans isomerase (BmPPI), FK506 binding-protein 45 (BmFKBP45) and BmFKBP59 homologue, were isolated from the silkworm, <i>Bombyx mori</i> Bm12 cell line following treatment with DA, which suggested that these proteins were possible DA-binding proteins. To validate the interaction between DA and the three immunophilins, we performed bio-layer interferometry (BLI) assay, and the results showed that DA has interaction with BmPPI, whose affinity constant value is 1.98 × 10<sup>−3</sup> M and which has no affinity with FKBP45 and FKBP59 homologue in vitro. Furthermore, we investigated the affinity between DA and human PPI protein (HsPPIA) and the affinity constant (K<sub>D</sub>) value is 2.22 × 10<sup>−3</sup> M. Additionally, we compared the effects of silkworm and human PPI proteins produced by DA and immunosuppressants, cyclosporine A (CsA), and tacrolimus (FK506), by employing I2H (insect two-hybrid) in the SF-9 cell line. The results indicated that in silkworm, the effects created by DA and CsA were stronger than FK506. Furthermore, the effects created by DA in silkworm were stronger than those in humans. This study will offer new thinking to elucidate the molecular mechanism of DA in the immunity system of insects. |
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language | English |
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spelling | doaj.art-83eca417ddba41999bf2d3cd4e148e482022-12-22T04:03:57ZengMDPI AGToxins2072-66512019-06-0111634910.3390/toxins11060349toxins11060349Effects of Destruxin A on Silkworm’s ImmunophilinsJingjing Wang0Qunfang Weng1Qiongbo Hu2Key Laboratory of Natural Pesticide & Chemical Biology, Ministry of Education; College of Agriculture, South China Agricultural University, Guangzhou 510642, ChinaKey Laboratory of Natural Pesticide & Chemical Biology, Ministry of Education; College of Agriculture, South China Agricultural University, Guangzhou 510642, ChinaKey Laboratory of Natural Pesticide & Chemical Biology, Ministry of Education; College of Agriculture, South China Agricultural University, Guangzhou 510642, ChinaDestruxin A (DA), a major secondary metabolite of <i>Metarhizium anisopliae</i>, has anti-immunity to insects. However, the detailed mechanism and its interactions with target proteins are elusive. Previously, three immunophilins, peptidyl−prolyl cis−trans isomerase (BmPPI), FK506 binding-protein 45 (BmFKBP45) and BmFKBP59 homologue, were isolated from the silkworm, <i>Bombyx mori</i> Bm12 cell line following treatment with DA, which suggested that these proteins were possible DA-binding proteins. To validate the interaction between DA and the three immunophilins, we performed bio-layer interferometry (BLI) assay, and the results showed that DA has interaction with BmPPI, whose affinity constant value is 1.98 × 10<sup>−3</sup> M and which has no affinity with FKBP45 and FKBP59 homologue in vitro. Furthermore, we investigated the affinity between DA and human PPI protein (HsPPIA) and the affinity constant (K<sub>D</sub>) value is 2.22 × 10<sup>−3</sup> M. Additionally, we compared the effects of silkworm and human PPI proteins produced by DA and immunosuppressants, cyclosporine A (CsA), and tacrolimus (FK506), by employing I2H (insect two-hybrid) in the SF-9 cell line. The results indicated that in silkworm, the effects created by DA and CsA were stronger than FK506. Furthermore, the effects created by DA in silkworm were stronger than those in humans. This study will offer new thinking to elucidate the molecular mechanism of DA in the immunity system of insects.https://www.mdpi.com/2072-6651/11/6/349Destruxin Apeptidyl-prolyl isomeraseFK506 binding proteincyclosporine AFK506<i>Bombyx mori</i> |
spellingShingle | Jingjing Wang Qunfang Weng Qiongbo Hu Effects of Destruxin A on Silkworm’s Immunophilins Toxins Destruxin A peptidyl-prolyl isomerase FK506 binding protein cyclosporine A FK506 <i>Bombyx mori</i> |
title | Effects of Destruxin A on Silkworm’s Immunophilins |
title_full | Effects of Destruxin A on Silkworm’s Immunophilins |
title_fullStr | Effects of Destruxin A on Silkworm’s Immunophilins |
title_full_unstemmed | Effects of Destruxin A on Silkworm’s Immunophilins |
title_short | Effects of Destruxin A on Silkworm’s Immunophilins |
title_sort | effects of destruxin a on silkworm s immunophilins |
topic | Destruxin A peptidyl-prolyl isomerase FK506 binding protein cyclosporine A FK506 <i>Bombyx mori</i> |
url | https://www.mdpi.com/2072-6651/11/6/349 |
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