An IDS-Type Sesquiterpene Synthase Produces the Pheromone Precursor (Z)-α-Bisabolene in Nezara viridula

Insects use a wide range of structurally diverse pheromones for intra-specific communication. Compounds in the class of terpenes are emitted as sex, aggregation, alarm, or trail pheromones. Despite the common occurrence of terpene pheromones in different insect lineages, their origin from dietary ho...

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Bibliographic Details
Published in:Journal of chemical ecology 2019-02, Vol.45 (2), p.187-197
Main Authors: Lancaster, Jason, Lehner, Bryan, Khrimian, Ashot, Muchlinski, Andrew, Luck, Katrin, Köllner, Tobias G., Weber, Donald C., Gundersen-Rindal, Dawn E., Tholl, Dorothea
Format: Article
Language:English
Subjects:
Agglomeration
Agriculture
Biochemistry
Biological Microscopy
Biomedical and Life Sciences
Biosynthesis
Bisabolene
Chemical communication
Cuticles
Diet
Ecology
Engraving
Entomology
Host plants
Insects
Ips pini
Life Sciences
Lysates
Nezara viridula
Pentatomidae
Pheromones
Precursors
Proteins
Sesquiterpene synthase
Sesquiterpenes
Sex
Sex pheromone
Substrates
Terpene synthase
Terpenes
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Summary:Insects use a wide range of structurally diverse pheromones for intra-specific communication. Compounds in the class of terpenes are emitted as sex, aggregation, alarm, or trail pheromones. Despite the common occurrence of terpene pheromones in different insect lineages, their origin from dietary host plant precursors or de novo biosynthetic pathways often remains unknown. Several stink bugs (Hemiptera: Pentatomidae) release bisabolene-type sesquiterpenes for aggregation and mating. Here we provide evidence for de novo biosynthesis of the sex pheromone trans− / cis -( Z )-α-bisabolene epoxide of the Southern green stink bug, Nezara viridula . We show that an enzyme ( Nv TPS) related to isoprenyl diphosphate synthases (IDSs) of the core terpene metabolic pathway functions as a terpene synthase (TPS), which converts the general intermediate ( E , E )-farnesyl diphosphate (FPP) to the putative pheromone precursor (+)-( S , Z )-α-bisabolene in vitro and in protein lysates. A second identified IDS-type protein ( Nv FPPS) makes the TPS substrate ( E , E )-FPP and functions as a bona fide FPP synthase. NvTPS is highly expressed in male epidermal tissue associated with the cuticle of ventral sternites, which is in agreement with the male specific release of the pheromone from glandular cells in this tissue. Our study supports findings of the function of similar TPS enzymes in the biosynthesis of aggregation pheromones from the pine engraver beetle Ips pini , the striped flea beetle Phyllotreta striolata , and the harlequin bug Murgantia histrionica, and hence provides growing evidence for the evolution of terpene de novo biosynthesis by IDS-type TPS families in insects.
ISSN:0098-0331
1573-1561
DOI:10.1007/s10886-018-1019-0