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Toxicity, Activation Process, and Histopathological Effect of Bacillus thuringiensis Vegetative Insecticidal Protein Vip3Aa16 on Tuta absoluta

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Abstract

Tuta absoluta is a destructive moth of Solanaceae plants and especially tomatoes. Here, we considered the entomopathogenic activity of the Bacillus thuringiensis Vip3Aa16 protein heterologously produced by Escherichia coli against T. absoluta. Purified Vip3Aa16 showed lower lethal concentration 50 % against third instar larvae (Toxin/tomato leaf) (335 ± 17 ng/cm2) compared to that of B. thuringiensis kurstaki HD1 δ-endotoxins (955 ± 4 ng/cm2) (P < 0.05). Action mode examination showed that Vip3Aa16 (88 kDa) was more sensitive to proteolysis activation by the chymotrypsin than the trypsin or the larvae gut soluble proteases, yielding derivative proteins essentially of about 62 and 33 kDa. The gut-soluble proteases could contain trypsin-like enzymes implicated in Vip3Aa16 activation since the proteolysis was inhibited using specific protease inhibitors. Additionally, we showed that the histopathological effect of Vip3Aa16 on T. absoluta larva midguts consisted on a microvillus damage and an epithelial cell rupture.

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Abbreviations

B :

Bacillus

T :

Tuta

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Acknowledgments

This study was supported by grant from the Tunisian “Ministère de l’Enseignement Supérieur et de la Recherche Scientifique (MESRS).”

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Authors and Affiliations

  1. Biopesticides Team (LPAP), Center of Biotechnology of Sfax, University of Sfax, P.O. Box 1177, 3018, Sfax, Tunisia

    Sameh Sellami, Maroua Cherif, Lobna Abdelkefi-Mesrati, Slim Tounsi & Kaïs Jamoussi

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  1. Sameh Sellami
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  2. Maroua Cherif
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  3. Lobna Abdelkefi-Mesrati
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  4. Slim Tounsi
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  5. Kaïs Jamoussi
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Correspondence to Kaïs Jamoussi.

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Sellami, S., Cherif, M., Abdelkefi-Mesrati, L. et al. Toxicity, Activation Process, and Histopathological Effect of Bacillus thuringiensis Vegetative Insecticidal Protein Vip3Aa16 on Tuta absoluta . Appl Biochem Biotechnol 175, 1992–1999 (2015). https://doi.org/10.1007/s12010-014-1393-1

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  • DOI: https://doi.org/10.1007/s12010-014-1393-1

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