Inga laurina trypsin inhibitor (ILTI) obstructs Spodoptera frugiperda trypsins expressed during adaptive mechanisms against plant protease inhibitors

Arch Insect Biochem Physiol. 2017 Aug;95(4). doi: 10.1002/arch.21393. Epub 2017 Jun 29.

Abstract

Plant protease inhibitors (PIs) are elements of a common plant defense mechanism induced in response to herbivores. The fall armyworm, Spodoptera frugiperda, a highly polyphagous lepidopteran pest, responds to various PIs in its diet by expressing genes encoding trypsins. This raises the question of whether the PI-induced trypsins are also inhibited by other PIs, which we posed as the hypothesis that Inga laurina trypsin inhibitor (ILTI) inhibits PI-induced trypsins in S. frugiperda. In the process of testing our hypothesis, we compared its properties with those of selected PIs, soybean Kunitz trypsin inhibitor (SKTI), Inga vera trypsin inhibitor (IVTI), Adenanthera pavonina trypsin inhibitor (ApTI), and Entada acaciifolia trypsin inhibitor (EATI). We report that ILTI is more effective in inhibiting the induced S. frugiperda trypsins than SKTI and the other PIs, which supports our hypothesis. ILTI may be more appropriate than SKTI for studies regarding adaptive mechanisms to dietary PIs.

Keywords: Inga laurina; Spodoptera frugiperda; plant defense mechanism; protease inhibitor.

MeSH terms

  • Animals
  • Fabaceae / chemistry*
  • Insect Control*
  • Insect Proteins / antagonists & inhibitors*
  • Insect Proteins / isolation & purification
  • Larva
  • Spodoptera / enzymology*
  • Trypsin Inhibitor, Kunitz Soybean
  • Trypsin Inhibitors / chemistry*
  • Trypsin Inhibitors / isolation & purification

Substances

  • Insect Proteins
  • Trypsin Inhibitors
  • Trypsin Inhibitor, Kunitz Soybean