Dataset Information

Seminal fluid and sperm proteomics of Aedes aegypti

ABSTRACT: Sperm samples were extracted from adult A. aegypti male seminal vesicles. Semen samples were extracted from bursa of recently mated bursa of N15 labeled females. The goal was to differentiate between the contribution of seminal fluid proteins and sperm proteins in the semen transfered to the female. Our results yield insights into the molecular function, genome organization, regulation, and evolution of sperm proteins and SFPs in this important disease vector.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Aedes Aegypti

TISSUE(S): Spermatozoon, Sperm, Semen

SUBMITTER: Kirill Borziak

LAB HEAD: Laura C. Harrington

PROVIDER: PXD010293 | Pride | 2018-12-17

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	EthanDegner10368590_1-1.raw	Raw
	EthanDegner10368590_1-1_reindex.mzML	Mzml
	EthanDegner10368590_1-2.raw	Raw
	EthanDegner10368590_1-2_reindex.mzML	Mzml
	EthanDegner10368590_1-3.raw	Raw

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Publications

Proteins, Transcripts, and Genetic Architecture of Seminal Fluid and Sperm in the Mosquito <i>Aedes aegypti</i>.

Degner Ethan C EC Ahmed-Braimah Yasir H YH Borziak Kirill K Wolfner Mariana F MF Harrington Laura C LC Dorus Steve S

Molecular & cellular proteomics : MCP 20181214 Suppl 1

The yellow fever mosquito, <i>Aedes aegypti,</i>, transmits several viruses causative of serious diseases, including dengue, Zika, and chikungunya. Some proposed efforts to control this vector involve manipulating reproduction to suppress wild populations or to replace them with disease-resistant mosquitoes. The design of such strategies requires an intimate knowledge of reproductive processes, yet our basic understanding of reproductive genetics in this vector remains largely incomplete. To acc ...[more]

PMID: 30552291

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Project description:Seminal fluid contains some of the fastest evolving proteins currently known. These seminal fluid proteins (Sfps) play crucial roles in reproduction, such as supporting sperm function, and – particularly in insects – modifying female physiology and behaviour. Identification of Sfps in small animals is challenging, and often relies on samples taken from the female reproductive tract after mating. A key pitfall of this method is that it might miss Sfps that are of low abundance due to dilution in the female-derived sample or rapid processing in females. Here we present a new and complimentary method, which provides added sensitivity to Sfp identification. We applied label-free quantitative proteomics to Drosophila melanogaster male reproductive tissue – where Sfps are unprocessed, and highly abundant – and quantified Sfps before and immediately after mating, to infer those transferred during copulation. We also analysed female reproductive tracts immediately before and after copulation to confirm the presence and abundance of known and candidate Sfps, where possible. Results were cross-referenced with transcriptomic and sequence databases to improve confidence in Sfp detection. Our data was consistent with 124 previously reported Sfps. We found 8 high-confidence novel candidate Sfps, which were both depleted in mated versus unmated males and identified within the reproductive tract of mated but not virgin females. We also identified 31 more candidates that are likely Sfps based on their abundance, known expression and predicted characteristics, and revealed that four proteins previously identified as Sfps are at best minor contributors to the ejaculate. The estimated copy numbers for our candidate Sfps were lower than for previously identified Sfps, supporting the idea that our technique provides a deeper analysis of the Sfp proteome than previous studies. Our results demonstrate a novel, high-sensitivity approach to the analysis of seminal fluid proteomes, whose application will further our understanding of reproductive biology.