Dataset Information

Characterization of extracellular vesicles in human seminal plasma: a multiomic analysis

ABSTRACT: Extracellular Vesicles (EVs) derived from seminal plasma have achieved considerable attention due to their potential role in male reproductive physiology and pathology. In this study, we employed a comprehensive proteomic and transcriptomic approach to investigate the molecular signatures of EVs isolated from human seminal plasma. EVs from Normozoospermic (NORMO,15), OligoAsthenoTeratozoospermic (OAT,12) and Azoospermic (AZO,12) subjects, were isolated by an in house modified polymer precipitation-based protocol and characterized for their size and morphology by NTA and TEM. Full proteomic analysis, by gel-free and gel-based approaches, revealed distinct protein profiles in each group, highlighting potential molecules and pathways implicated in sperm function and fertility. Furthermore, transcriptomic analysis confirmed the trend of general down-regulation of AZO and OAT groups compared to NORMO offering insights into the regulatory mechanisms underlying sperm development and function. Bioinformatic tools were applied for functional Omics analysis; integration of proteomic and transcriptomic data provided a comprehensive understanding of the cargo content and regulatory networks. This study contributes to elucidating the key role of EVs in the paracrine communication regulating spermatogenesis. The full understanding of these pathways not only suggests potential mechanisms regulating male fertility but also offers new insight for the development of diagnostic tools targeting male reproductive disorders.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Seminal Plasma, Extracellular Vesicle

DISEASE(S): Oligoasthenoteratozoospermia,Azoospermia

SUBMITTER: Enxhi Shaba

LAB HEAD: Prof. Claudia Landi

PROVIDER: PXD051361 | Pride | 2025-06-30

REPOSITORIES: Pride

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Publications

Unraveling the Multi-Omic Landscape of Extracellular Vesicles in Human Seminal Plasma.

Governini Laura L Haxhiu Alesandro A Shaba Enxhi E Vantaggiato Lorenza L Mori Alessia A Bruttini Marco M Loria Francesca F Zarovni Natasa N Piomboni Paola P Landi Claudia C Luddi Alice A

Biomolecules 20250607 6

Extracellular Vesicles (EVs) from seminal plasma have achieved attention due to their potential physiopathological role in male reproductive systems. This study employed a comprehensive proteomic and transcriptomic approach to investigate the composition and molecular signatures of EVs isolated from human seminal plasma. EVs from Normozoospermic (NORMO), OligoAsthenoTeratozoospermic (OAT), and Azoospermic (AZO) subjects were isolated using a modified polymer precipitation-based protocol and char ...[more]

PMID: 40563475

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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.

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	sample_2.msfView	Msf
	sample_2.raw	Raw