ArticleBMC biology2022
Female factors modulate Sex Peptide's association with sperm in Drosophila melanogaster.
Article in BMC biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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5 citing papers in PubMed, 11 citations in OpenAlex.
- Correlated Gene Copy Number Changes in a Seminal Fluid Protein Network inbioRxiv : the preprint server for biology · 2025Article
- Synthesis and Scope of the Role of Postmating Prezygotic Isolation in Speciation.Cold Spring Harbor perspectives in biology · 2024Review
- O-Glycosylation of a male seminal fluid protein influences sperm binding and female postmating behavior.PNAS nexus · 2024Article
- The Drosophila melanogaster Y-linked gene, WDY, is required for sperm to swim in the female reproductive tract.Communications biology · 2024Article
- The seminal odorant binding protein Obp56g is required for mating plug formation and male fertility ineLife · 2023Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
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Abstract
backgroundMale-derived seminal fluid proteins (SFPs) that enter female fruitflies during mating induce a myriad of physiological and behavioral changes, optimizing fertility of the mating pair. Some post-mating changes in female Drosophila melanogaster persist for ~10-14 days. Their long-term persistence is because the seminal protein that induces these particular changes, the Sex Peptide (SP), is retained long term in females by binding to sperm, with gradual release of its active domain from sperm. Several other "long-term response SFPs" (LTR-SFPs) "prime" the binding of SP to sperm. Whether female factors play a role in this process is unknown, though it is important to study both sexes for a comprehensive physiological understanding of SFP/sperm interactions and for consideration in models of sexual conflict.
resultsWe report here that sperm in male ejaculates bind SP more weakly than sperm that have entered females. Moreover, we show that the amount of SP, and other SFPs, bound to sperm increases with time and transit of individual seminal proteins within the female reproductive tract (FRT). Thus, female contributions are needed for maximal and appropriate binding of SP, and other SFPs, to sperm. Towards understanding the source of female molecular contributions, we ablated spermathecal secretory cells (SSCs) and/or parovaria (female accessory glands), which contribute secretory proteins to the FRT. We found no dramatic change in the initial levels of SP bound to sperm stored in mated females with ablated or defective SSCs and/or parovaria, indicating that female molecules that facilitate the binding of SP to sperm are not uniquely derived from SSCs and parovaria. However, we observed higher levels of SP (and sperm) retention long term in females whose SSCs and parovaria had been ablated, indicating secretions from these female tissues are necessary for the gradual release of Sex Peptide's active region from stored sperm.
conclusionThis study reveals that the SP-sperm binding pathway is not entirely male-derived and that female contributions are needed to regulate the levels of SP associated with sperm stored in their storage sites.
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