Suppression of a leucine-rich repeat receptor-like kinase enhances host plant resistance to a specialist herbivore

Plant Cell Environ. 2020 Oct;43(10):2571-2585. doi: 10.1111/pce.13834. Epub 2020 Jul 28.

Abstract

The mechanisms by which herbivores induce plant defenses are well studied. However, how specialized herbivores suppress plant resistance is still poorly understood. Here, we discovered a rice (Oryza sativa) leucine-rich repeat receptor-like kinase, OsLRR-RLK2, which is induced upon attack by gravid females of a specialist piercing-sucking herbivore, the brown planthopper (BPH, Nilaparvata lugens). Silencing OsLRR-RLK2 decreases the constitutive activity of mitogen-activated protein kinase (OsMPK6) and alters BPH-induced transcript levels of several defense-related WRKY transcription factors. Moreover, silencing OsLRR-RLK2 reduces BPH-induction of jasmonic acid and ethylene but promotes the biosynthesis of both elicited salicylic acid and H2 O2 ; silencing also enhances the production of volatiles emitted from rice plants infested with gravid BPH females. These changes decrease BPH preference and performance in the glasshouse and the field. These findings suggest that OsLRR-RLK2, by regulating the plant's defense-related signaling profile, increases the susceptibility of rice to BPH, and that BPH infestation influences the expression of OsLRR-RLK2, suppressing the resistance of rice to BPH.

Keywords: H2O2; Nilaparvata lugens; ethylene; jasmonic acid; mitogen-activated protein kinase; rice; salicylic acid; transcription factor.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cloning, Molecular
  • Gene Expression Regulation, Plant
  • Hemiptera*
  • Oryza / metabolism
  • Oryza / physiology*
  • Plant Defense Against Herbivory*
  • Plant Proteins / genetics
  • Plant Proteins / metabolism
  • Plant Proteins / physiology*
  • Plants, Genetically Modified
  • Protein Serine-Threonine Kinases / genetics
  • Protein Serine-Threonine Kinases / metabolism
  • Protein Serine-Threonine Kinases / physiology*
  • RNA Interference
  • Sequence Analysis, DNA
  • Transcriptome

Substances

  • Plant Proteins
  • Protein Serine-Threonine Kinases