Multitasking antimicrobial peptides in plant development and host defense against biotic/abiotic stress

Plant Sci. 2014 Nov:228:135-49. doi: 10.1016/j.plantsci.2014.05.012. Epub 2014 May 28.

Abstract

Crop losses due to pathogens are a major threat to global food security. Plants employ a multilayer defense against a pathogen including the use of physical barriers (cell wall), induction of hypersensitive defense response (HR), resistance (R) proteins, and synthesis of antimicrobial peptides (AMPs). Unlike a complex R gene-mediated immunity, AMPs directly target diverse microbial pathogens. Many a times, R-mediated immunity breaks down and plant defense is compromised. Although R-gene dependent pathogen resistance has been well studied, comparatively little is known about the interactions of AMPs with host defense and physiology. AMPs are ubiquitous, low molecular weight peptides that display broad spectrum resistance against bacteria, fungi and viruses. In plants, AMPs are mainly classified into cyclotides, defensins, thionins, lipid transfer proteins, snakins, and hevein-like vicilin-like and knottins. Genetic distance lineages suggest their conservation with minimal effect of speciation events during evolution. AMPs provide durable resistance in plants through a combination of membrane lysis and cellular toxicity of the pathogen. Plant hormones - gibberellins, ethylene, jasmonates, and salicylic acid, are among the physiological regulators that regulate the expression of AMPs. Transgenically produced AMP-plants have become a means showing that AMPs are able to mitigate host defense responses while providing durable resistance against pathogens.

Keywords: Biotechnology; Hypersensitive response; Microbe interactions; Plant immunity; Reactive oxygen species; Transgenic plants.

Publication types

  • Review

MeSH terms

  • Antimicrobial Cationic Peptides / physiology*
  • Host-Pathogen Interactions
  • Immunity, Innate*
  • Plant Development*
  • Plant Immunity*
  • Stress, Physiological

Substances

  • Antimicrobial Cationic Peptides