Oral Presentation ESA-SRB-APEG-NZSE 2022

Defining the core sperm proteome; Highly conserved targets for reproductive biology research (#39)

Taylor Pini 1 , Brett Nixon 2 3 , Timothy Karr 4 , David Skerrett-Byrne 2 3
  1. School of Veterinary Science, The University of Queensland, Gatton, QLD, Australia
  2. Infertility and Reproduction Research Program, Hunter Medical Research Institute, New Lambton Heights, NSW, Australia
  3. Priority Research Centre for Reproductive Science, School of Environmental and Life Sciences, The University of Newcastle, Callaghan, NSW, Australia
  4. The Biodesign Institute, Mass Spectrometry Core Facility, Arizona State University, Tempe, AZ, USA

Reproductive biology is often considered in the three siloed areas of humans, domesticated animals and wildlife. There are common needs across these species, notably treatment of infertility, development of assisted reproductive technologies and effective contraception. To efficiently develop solutions applicable to all species, we must develop a better understanding of the common biology underpinning reproductive processes. To this end, we performed an in-silico analysis of publicly available sperm proteomic data to define the core sperm proteome; a collection of highly conserved proteins which are critical for sperm structure and function. >2TB of RAW spectral data was sourced from ProteomeXchange and processed through a strict, uniform search and ID validation in-house pipeline. Sperm proteome data was available for 18 vertebrate species, however due to data quality, only 12 species were analysed (Figure 1). A combined total of 12,144 unique proteins were identified, highly biased towards human (9186 IDs total) and mouse (4462 IDs total). In some species >90% of the proteins identified were only predicted or inferred from homology, indicating that experimental evidence for the existence of most proteins remains poor in non-model species. While the mouse sperm proteome captured almost all proteins present in other species (e.g. 93.1% of koala, 89.8% of pig), less than half (42.0%) of the mouse sperm proteome was common to the extensive human sperm proteome. A total of 27 proteins were conserved across all species, with significant enrichment for proteins involved in acetylation and phosphorylation, proteins contained within secretory granules, chaperones, proteasome function and glycolysis. A total of 85 proteins were conserved across all orders, showcasing additional enrichment for mitochondrial respiration. These early results suggest that there are key conserved pathways likely to be critical for sperm function in all species, particularly post translational modification, protein folding and recycling, acrosome function and energy generation.

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