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<p>An attempt is made in the present investigation to test the efficacy of lectin purified from <i>C. rosea</i> against the major stored product insect pest, <i>C. maculatus</i>. Biochemical analysis carried out as the part of preliminary characterisation revealed the presence of a mannose-specific lectin (<i>Cr</i>MBL) from the crude seed kernel extract of <i>C. rosea.</i> The haemagglutinating (HA) activity of the extract was found to be divalent cation-independent and EDTA insensitive. Furthermore, the HA activity remained stable between pH 5 and 8 and unaffected between temperatures 10&#xa0;°C and 70 °C. The lectin, <i>Cr</i>MBL from the crude seed kernel extracts of <i>C. rosea</i> was purified through single-step affinity chromatography using the mannose-coupled epoxy-activated sepharose 6B. The purified lectin showed highest affinity to the simple carbohydrate, mannose. Various biochemical assays of the <i>Cr</i>MBL revealed a similar profile of results as observed in the preliminary characterisation. Its molecular characterisation using gel electrophoresis revealed five different polypeptide subunits viz., 98&#xa0;kDa, 80&#xa0;kDa, 50&#xa0;kDa, 30&#xa0;kDa, and 15&#xa0;kDa with a native mass of 273&#xa0;kDa. Q-TOF–LC/MS of <i>Cr</i>MBL and MALDI–TOF–MS analysis of the 30&#xa0;kDa polypeptide subunit of <i>Cr</i>MBL showed molecular similarity to several lectins, especially from Leguminosae family. The feeding bioassay with <i>Cr</i>MBL showed significant protection against the infestation of the stored product insect pest, <i>C. maculatus</i>. Lectin from <i>C. rosea</i> with more resistance to the activity of insect detoxifying enzymes could offer effective way of insect pest control with its suitability for employing this molecule as a component of integrated pest management.</p>

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A mannose-specific lectin from the seeds of Canavalia rosea and its potential insecticidal activity against the stored product pest Callosobruchus maculatus

  • 期刊论文

  • 发表日期：

    2025年9月4日

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  • Meenakumari Mani,
  • Nivetha Ramanathan,
  • Mahi Dev Ayikkara Peroor,
  • Janarthanan Sundaram

摘要

An attempt is made in the present investigation to test the efficacy of lectin purified from C. rosea against the major stored product insect pest, C. maculatus. Biochemical analysis carried out as the part of preliminary characterisation revealed the presence of a mannose-specific lectin (CrMBL) from the crude seed kernel extract of C. rosea. The haemagglutinating (HA) activity of the extract was found to be divalent cation-independent and EDTA insensitive. Furthermore, the HA activity remained stable between pH 5 and 8 and unaffected between temperatures 10 °C and 70 °C. The lectin, CrMBL from the crude seed kernel extracts of C. rosea was purified through single-step affinity chromatography using the mannose-coupled epoxy-activated sepharose 6B. The purified lectin showed highest affinity to the simple carbohydrate, mannose. Various biochemical assays of the CrMBL revealed a similar profile of results as observed in the preliminary characterisation. Its molecular characterisation using gel electrophoresis revealed five different polypeptide subunits viz., 98 kDa, 80 kDa, 50 kDa, 30 kDa, and 15 kDa with a native mass of 273 kDa. Q-TOF–LC/MS of CrMBL and MALDI–TOF–MS analysis of the 30 kDa polypeptide subunit of CrMBL showed molecular similarity to several lectins, especially from Leguminosae family. The feeding bioassay with CrMBL showed significant protection against the infestation of the stored product insect pest, C. maculatus. Lectin from C. rosea with more resistance to the activity of insect detoxifying enzymes could offer effective way of insect pest control with its suitability for employing this molecule as a component of integrated pest management.