A diterpene synthase from the sandfly Lutzomyia longipalpis produces the pheromone sobralene

Ducker, Charles; Baines, Cameron; Guy, Jennifer; Euzébio Goulart Santana, Antônio; Pickett, John A.; Oldham, Neil J.

Abstract

The phlebotomine sandfly, Lutzomyia longipalpis, a major vector of the Leishmania parasite, uses terpene pheromones to attract conspecifics for mating. Examination of the L. longipalpis genome revealed a putative terpene synthase (TPS), which—upon heterologous expression in, and purification from, Escherichia coli—yielded a functional enzyme. The TPS, termed LlTPS, converted geranyl diphosphate (GPP) into a mixture of monoterpenes with low efficiency, of which β-ocimene was the major product. (E,E)-farnesyl diphosphate (FPP) principally produced small amounts of (E)-β-farnesene, while (Z,E)- and (Z,Z)-FPP yielded a mixture of bisabolene isomers. None of these mono- and sesquiterpenes are known volatiles of L. longipalpis. Notably, however, when provided with (E,E,E)-geranylgeranyl diphosphate (GGPP), LlTPS gave sobralene as its major product. This diterpene pheromone is released by certain chemotypes of L. longipalpis, in particular those found in the Ceará state of Brazil. Minor diterpene components were also seen as products of the enzyme that matched those seen in a sandfly pheromone extract.

Citation

Ducker, C., Baines, C., Guy, J., Euzébio Goulart Santana, A., Pickett, J. A., & Oldham, N. J. (2024). A diterpene synthase from the sandfly Lutzomyia longipalpis produces the pheromone sobralene. Proceedings of the National Academy of Sciences, 121(12), Article e2322453121. https://doi.org/10.1073/pnas.2322453121

• Journal Article Type: Article
• Acceptance Date: Feb 6, 2024
• Online Publication Date: Mar 12, 2024
• Publication Date: Mar 19, 2024
• Deposit Date: Mar 13, 2024
• Publicly Available Date: Sep 13, 2024
• Journal: Proceedings of the National Academy of Sciences
• Print ISSN: 0027-8424
• Electronic ISSN: 1091-6490
• Publisher: National Academy of Sciences
• Peer Reviewed: Peer Reviewed
• Volume: 121
• Issue: 12
• Article Number: e2322453121
• DOI: https://doi.org/10.1073/pnas.2322453121
• Keywords: BIOLOGICAL SCIENCES; BIOCHEMISTRY; PHYSICAL SCIENCES; CHEMISTRY
• Public URL: https://nottingham-repository.worktribe.com/output/32460078
• Publisher URL: https://www.pnas.org/doi/10.1073/pnas.2322453121