Potential detoxification of gossypol by UDP-glycosyltransferases in the two Heliothine moth species Helicoverpa armigera and Heliothis virescens.

TitlePotential detoxification of gossypol by UDP-glycosyltransferases in the two Heliothine moth species Helicoverpa armigera and Heliothis virescens.
Publication TypeJournal Article
Year of Publication2016
AuthorsKrempl, C, Sporer, T, Reichelt, M, Ahn, S-J, Heidel-Fischer, H, Vogel, H, Heckel, DG, Joußen, N
JournalInsect Biochem Mol Biol
Volume71
Pagination49-57
Date Published2016 Apr
ISSN1879-0240
KeywordsAnimals, Glycosyltransferases, Gossypol, Insect Proteins, Insecticides, Larva, Moths, Uridine Diphosphate
Abstract

The cotton bollworm Helicoverpa armigera and the tobacco budworm Heliothis virescens are closely related generalist insect herbivores and serious pest species on a number of economically important crop plants including cotton. Even though cotton is well defended by its major defensive compound gossypol, a toxic sesquiterpene dimer, larvae of both species are capable of developing on cotton plants. In spite of severe damage larvae cause on cotton plants, little is known about gossypol detoxification mechanisms in cotton-feeding insects. Here, we detected three monoglycosylated and up to five diglycosylated gossypol isomers in the feces of H. armigera and H. virescens larvae fed on gossypol-supplemented diet. Candidate UDP-glycosyltransferase (UGT) genes of H. armigera were selected by microarray studies and in silico analyses and were functionally expressed in insect cells. In enzymatic assays, we show that UGT41B3 and UGT40D1 are capable of glycosylating gossypol mainly to the diglycosylated gossypol isomer 5 that is characteristic for H. armigera and is absent in H. virescens feces. In conclusion, our results demonstrate that gossypol is partially metabolized by UGTs via glycosylation, which might be a crucial step in gossypol detoxification in generalist herbivores utilizing cotton as host plant.

DOI10.1016/j.ibmb.2016.02.005
Alternate JournalInsect Biochem. Mol. Biol.
PubMed ID26873292