Bovine pancreatic trypsin inhibitor and soybean Kunitz trypsin inhibitor: Differential effects on proteases and larval development of the soybean pest Anticarsia gemmatalis (Lepidoptera: Noctuidae)

Pestic Biochem Physiol. 2022 Oct:187:105188. doi: 10.1016/j.pestbp.2022.105188. Epub 2022 Aug 1.

Abstract

Pest management is challenged with resistant herbivores and problems regarding human health and environmental issues. Indeed, the greatest challenge to modern agriculture is to protect crops from pests and still maintain environmental quality. This study aimed to analyze by in silico, in vitro, and in vivo approaches to the feasibility of using the inhibitory protein extracted from mammals - Bovine Pancreatic Trypsin Inhibitor (BPTI) as a potential inhibitor of digestive trypsins from the pest Anticarsia gemmatalis and comparing the results with the host-plant inhibitor - Soybean Kunitz Trypsin Inhibitor (SKTI). BPTI and SKTI interacts with A. gemmatalis trypsin-like enzyme competitively, through hydrogen and hydrophobic bonds. A. gemmatalis larvae exposed to BPTI did not show two common adaptative mechanisms i.e., proteolytic degradation and overproduction of proteases, presenting highly reduced trypsin-like activity. On the other hand, SKTI-fed larvae did not show reduced trypsin-like activity, presenting overproduction of proteases and SKTI digestion. In addition, the larval survival was reduced by BPTI similarly to SKTI, and additionally caused a decrease in pupal weight. The non-plant protease inhibitor BPTI presents intriguing element to compose biopesticide formulations to help decrease the use of conventional refractory pesticides into integrated pest management programs.

Keywords: Adaptative responses; Electrophoresis; Enzyme kinetics; Inhibition; Molecular dynamics; Protease inhibitors.

MeSH terms

  • Animals
  • Aprotinin / pharmacology
  • Biological Control Agents* / pharmacology
  • Cattle
  • Glycine max*
  • Hydrogen / pharmacology
  • Larva
  • Moths*
  • Peptide Hydrolases / metabolism
  • Pesticides* / pharmacology
  • Protease Inhibitors / pharmacology
  • Trypsin
  • Trypsin Inhibitors / pharmacology

Substances

  • Biological Control Agents
  • Pesticides
  • Protease Inhibitors
  • Trypsin Inhibitors
  • Hydrogen
  • Aprotinin
  • Peptide Hydrolases
  • Trypsin