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Two functionally distinct CYP4G genes of Anopheles gambiae contribute to cuticular hydrocarbon biosynthesis

Kefi, Mary, Balabanidou, Vasileia, Douris, Vassilis, Lycett, Gareth ORCID:, Feyereisen, René and Vontas, John (2019) 'Two functionally distinct CYP4G genes of Anopheles gambiae contribute to cuticular hydrocarbon biosynthesis'. Insect Biochemistry and Molecular Biology, Vol 110, pp. 52-59.

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Cuticular hydrocarbon (CHC) biosynthesis is a major pathway of insect physiology. In Drosophila melanogaster the cytochrome P450 CYP4G1 catalyses the insect-specific oxidative decarbonylation step, while in the malaria vector Anopheles gambiae, two CYP4Gs paralogues, CYP4G16 and CYP4G17 are present. Analysis of
the subcellular localization of CYP4G17 and CYP4G16 in larval and pupal stages revealed that CYP4G16 preserves its PM localization across developmental stages analyzed; however CYPG17 is differentially localized in two distinct types of pupal oenocytes, presumably oenocytes of larval and adult developmental specificity.
Western blot analysis showed the presence of two CYP4G17 forms, potentially associated with each oenocyte type. Both An. gambiae CYP4Gs were expressed in D. melanogaster flies in a Cyp4g1 silenced background in order to functionally characterize them in vivo. CYP4G16, CYP4G17 or their combination rescued the
lethal phenotype of Cyp4g1-knock down flies, demonstrating that CYP4G17 is also a functional decarbonylase, albeit of somewhat lower efficiency than CYP4G16 in Drosophila. Flies expressing mosquito CYP4G16 and/or CYP4G17 produced similar CHC profiles to ‘wild-type’ flies expressing the endogenous CYP4G1, but they also
produce very long-chain dimethyl-branched CHCs not detectable in wild type flies, suggesting that the specificity of the CYP4G enzymes contributes to determine the complexity of the CHC blend. In conclusion, both An. gambiae CYP4G enzymes contribute to the unique Anopheles CHC profile, which has been associated to
defense, adult desiccation tolerance, insecticide penetration rate and chemical communication.

Item Type: Article
Subjects: QU Biochemistry > Proteins. Amino Acids. Peptides > QU 55 Proteins
QX Parasitology > Insects. Other Parasites > QX 510 Mosquitoes
QX Parasitology > Insects. Other Parasites > QX 515 Anopheles
WC Communicable Diseases > Tropical and Parasitic Diseases > WC 750 Malaria
Faculty: Department: Biological Sciences > Vector Biology Department
Digital Object Identifer (DOI):
Depositing User: Stacy Murtagh
Date Deposited: 22 May 2019 10:48
Last Modified: 30 Apr 2020 01:02


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