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Ascertaining variations in the activity of larval midgut enzymes of Helicoverpa armigera by dietary emamectin benzoate through biochemical and in silico docking study.
Dagar, Vinay Singh; Mishra, Monika; Sharma, Aarti; Sankar, Manu; Goyal, Shubham; Pal, Ranjan; Kumar, Sarita.
Afiliação
  • Dagar VS; Department of Zoology, Acharya Narendra Dev College (University of Delhi), Govindpuri, New Delhi, India; Department of Zoology, Deen Dayal Upadhyaya College, University of Delhi, Sector-3, Dwarka, New Delhi, India. Electronic address: vinaydagar04@gmail.com.
  • Mishra M; Department of Zoology, Acharya Narendra Dev College (University of Delhi), Govindpuri, New Delhi, India. Electronic address: mishra_monika7@yahoo.co.in.
  • Sharma A; Galgotias University, School of Biological and Life Sciences, Greater Noida, Uttar Pradesh, India. Electronic address: aartisharma@galgotiasuniversity.edu.in.
  • Sankar M; Department of Zoology, Acharya Narendra Dev College (University of Delhi), Govindpuri, New Delhi, India. Electronic address: sankarmanu00@gmail.com.
  • Goyal S; Department of Microbiology, University of Manitoba, Winnipeg City, Manitoba Province, Canada. Electronic address: Sggoyal742@gmail.com.
  • Pal R; Department of Biotechnology, University of Wroclaw, Wroclaw, Poland. Electronic address: paulranjan843@gmail.com.
  • Kumar S; Department of Zoology, Acharya Narendra Dev College (University of Delhi), Govindpuri, New Delhi, India. Electronic address: saritakumar@andc.du.ac.in.
Chemosphere ; 359: 142288, 2024 Jul.
Article em En | MEDLINE | ID: mdl-38750729
ABSTRACT
Helicoverpa armigera, a ubiquitous polyphagous pest, poses a significant threat to global agriculture, causing substantial economic losses and demonstrating resistance to synthetic pesticides. This study investigates the potential of emamectin benzoate (EMB), an avermectin derivative, as an effective control agent against H. armigera. The larvae of the NBII-MP-NOC-01 strain of H. armigera were reared on an artificial diet. The impact of dietary EMB was examined on four midgut enzymes; alanine aminotransferase (ALT), aspartate aminotransferase (AST), acid phosphatase (ACP), and alkaline phosphatase (ALP). Results showed a dose-dependent and time-dependent reduction in ALT and AST activity, while an initial increase and subsequent decline in ACP and ALP activity at higher EMB concentrations. Computational modelling of enzyme structures and molecular docking studies revealed differential binding of EMB with the midgut enzymes. The strongest interaction was observed between EMB and ALT residues, contrasting with weakest interactions observed with AST. The study also showed that decreased activity of transaminases in H. armigera caused by EMB may be because of stability-activity trade-off, while in phosphatases reverse may be the case. This research provides crucial insights into the biochemical responses and the intricate insecticide-enzyme interactions in H. armigera caused by EMB exposure. This study lays the foundation for further research aimed at developing environmentally friendly approaches for managing H. armigera, addressing the challenges associated with conventional pesticides.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Aspartato Aminotransferases / Fosfatase Ácida / Ivermectina / Alanina Transaminase / Fosfatase Alcalina / Simulação de Acoplamento Molecular / Inseticidas / Larva / Mariposas Limite: Animals Idioma: En Revista: Chemosphere Ano de publicação: 2024 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Aspartato Aminotransferases / Fosfatase Ácida / Ivermectina / Alanina Transaminase / Fosfatase Alcalina / Simulação de Acoplamento Molecular / Inseticidas / Larva / Mariposas Limite: Animals Idioma: En Revista: Chemosphere Ano de publicação: 2024 Tipo de documento: Article