Glucosylation prevents plant defense activation in phloem-feeding insects

Nat Chem Biol. 2020 Dec;16(12):1420-1426. doi: 10.1038/s41589-020-00658-6. Epub 2020 Sep 28.

Abstract

The metabolic adaptations by which phloem-feeding insects counteract plant defense compounds are poorly known. Two-component plant defenses, such as glucosinolates, consist of a glucosylated protoxin that is activated by a glycoside hydrolase upon plant damage. Phloem-feeding herbivores are not generally believed to be negatively impacted by two-component defenses due to their slender piercing-sucking mouthparts, which minimize plant damage. However, here we document that glucosinolates are indeed activated during feeding by the whitefly Bemisia tabaci. This phloem feeder was also found to detoxify the majority of the glucosinolates it ingests by the stereoselective addition of glucose moieties, which prevents hydrolytic activation of these defense compounds. Glucosylation of glucosinolates in B. tabaci was accomplished via a transglucosidation mechanism, and two glycoside hydrolase family 13 (GH13) enzymes were shown to catalyze these reactions. This detoxification reaction was also found in a range of other phloem-feeding herbivores.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Arabidopsis / immunology
  • Arabidopsis / metabolism
  • Arabidopsis / parasitology*
  • Feeding Behavior / physiology
  • Gene Expression
  • Glucosinolates / chemistry*
  • Glucosinolates / metabolism
  • Glycoside Hydrolases / classification
  • Glycoside Hydrolases / genetics
  • Glycoside Hydrolases / metabolism*
  • Glycosylation
  • Hemiptera / classification
  • Hemiptera / enzymology*
  • Hemiptera / genetics
  • Host-Parasite Interactions / immunology
  • Insect Proteins / classification
  • Insect Proteins / genetics
  • Insect Proteins / metabolism*
  • Phloem / immunology
  • Phloem / metabolism
  • Phloem / parasitology*
  • Phylogeny
  • Plant Immunity

Substances

  • Glucosinolates
  • Insect Proteins
  • Glycoside Hydrolases