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<p>The present study focuses on the response of microalgae <i>Graesiella emersonii</i> NC-M1 to alpha-cypermethrin exposure at the molecular level using 2-D gel electrophoresis coupled with mass spectrometry and in-silico analysis. The proteins such as NAD(P)H-quinone oxidoreductase subunit I (+ 1.61), Heat shock proteins 70 (+ 3.01), Cytochrome P450 (+ 2.81), ABC transporters (+ 1.68), Benzoate carboxyl methyltransferase (+ 5.13), and 6(G)-Fructosyltransferase (− 3.95) were advocated as key players against alpha-cypermethrin. The accumulation pattern of these proteins was validated by a gene-expression study using qPCR. Furthermore, in-silico analysis was constructed using 3D modelling of the selected proteins, followed by the model quality assessment. The binding energy between most selected proteins and alpha-cypermethrin shows a strong interaction, except for protein benzoate carboxyl methyltransferase. Docking the ligand and the receptor offers strong binding energy, but the selected ligand, alpha-cypermethrin, is binding at the surface groove/surface-exposed binding pocket or allosteric site of the protein that can modulate other functions. The binding of alpha-cypermethrin on the selected proteins might trigger some defensive mechanism, causing them to up-accumulate under stress. Further, qPCR and docking studies supported the down-accumulation of 6(G)-fucosyltransferase (6G-FT). Taken together, these proteins were involved in the detoxification of the insecticide, DNA damage repair, and maintaining cellular homeostasis, thereby liberating the <i>G. emersonii</i> NC-M1 from stress conditions.</p>

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Integrated proteomics and in-silico analysis unveil the alpha-cypermethrin detoxification mechanism in Graesiella Emersonii

  • 期刊论文

  • 发表日期：

    2025年10月24日

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  • Ng. Kunjarani Chanu,
  • Madan Kumar Mandal,
  • Shilpi Singh,
  • Mukesh Kumar Yadav,
  • Prashant Kumar Singh,
  • Neha Chaurasia

摘要

The present study focuses on the response of microalgae Graesiella emersonii NC-M1 to alpha-cypermethrin exposure at the molecular level using 2-D gel electrophoresis coupled with mass spectrometry and in-silico analysis. The proteins such as NAD(P)H-quinone oxidoreductase subunit I (+ 1.61), Heat shock proteins 70 (+ 3.01), Cytochrome P450 (+ 2.81), ABC transporters (+ 1.68), Benzoate carboxyl methyltransferase (+ 5.13), and 6(G)-Fructosyltransferase (− 3.95) were advocated as key players against alpha-cypermethrin. The accumulation pattern of these proteins was validated by a gene-expression study using qPCR. Furthermore, in-silico analysis was constructed using 3D modelling of the selected proteins, followed by the model quality assessment. The binding energy between most selected proteins and alpha-cypermethrin shows a strong interaction, except for protein benzoate carboxyl methyltransferase. Docking the ligand and the receptor offers strong binding energy, but the selected ligand, alpha-cypermethrin, is binding at the surface groove/surface-exposed binding pocket or allosteric site of the protein that can modulate other functions. The binding of alpha-cypermethrin on the selected proteins might trigger some defensive mechanism, causing them to up-accumulate under stress. Further, qPCR and docking studies supported the down-accumulation of 6(G)-fucosyltransferase (6G-FT). Taken together, these proteins were involved in the detoxification of the insecticide, DNA damage repair, and maintaining cellular homeostasis, thereby liberating the G. emersonii NC-M1 from stress conditions.