ArticleInsect biochemistry and molecular biology2018
Long-term interaction between Drosophila sperm and sex peptide is mediated by other seminal proteins that bind only transiently to sperm.
Article in Insect biochemistry and molecular biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed.
- Abdominal-B regulates the male seminal fluid transferome and new fecundity factors required for sperm sex peptide binding.PLoS genetics · 2026Article
- Pervasive convergent evolution of sperm conjugation across the Arthropoda tree of life.Nature communications · 2026Review
- Neprilysin 4 controls acrosome structure and male fertility in Drosophila melanogaster.Communications biology · 2025Article
- Correlated Gene Copy Number Changes in a Seminal Fluid Protein Network inbioRxiv : the preprint server for biology · 2025Article
- Gene age shapes functional and evolutionary properties of theProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Phylogenetic Relatedness Does not Predict Patterns of Parallel Transcriptome Adaptation in Drosophila.Genome biology and evolution · 2025Article
- O-Glycosylation of a male seminal fluid protein influences sperm binding and female postmating behavior.PNAS nexus · 2024Article
- The Origin and Evolution of Sex Peptide and Sex Peptide Receptor Interactions.Molecular biology and evolution · 2024Article
- The Origin and Evolution of Sex Peptide and Sex Peptide Receptor Interactions.bioRxiv : the preprint server for biology · 2024Article
- Decoupled evolution of theProceedings of the National Academy of Sciences of the United States of America · 2024Article
- The seminal odorant binding protein Obp56g is required for mating plug formation and male fertility ineLife · 2023Article
- Decoupled evolution of thebioRxiv : the preprint server for biology · 2023Article
- A predominant role of genotypic variation in both expression of sperm competition genes and paternity success inProceedings. Biological sciences · 2023Article
- Review
- Evolutionary Quantitative Proteomics of Reproductive Protein Divergence in Drosophila.Molecular & cellular proteomics : MCP · 2023Article
- Female factors modulate Sex Peptide's association with sperm in Drosophila melanogaster.BMC biology · 2022Article
- On how to identify a seminal fluid protein: A commentary on Hurtado et al.Insect molecular biology · 2022Article
- The evolution of sex peptide: sexual conflict, cooperation, and coevolution.Biological reviews of the Cambridge Philosophical Society · 2022Article
- A single mating is sufficient to induce persistent reduction of immune defense in mated female Drosophila melanogaster.Journal of insect physiology · 2022Article
- The life history ofProceedings of the National Academy of Sciences of the United States of America · 2022Article
Corrections and comments
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6 authors.
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Abstract
Seminal fluid proteins elicit several post-mating physiological changes in mated Drosophila melanogaster females. Some of these changes persist for over a week after mating because the seminal protein that causes these changes, the Sex Peptide (SP), binds to sperm that are stored in the female reproductive tract. SP's sperm binding is mediated by a network of at least eight seminal proteins. We show here that some of these network proteins (CG1656, CG1652, CG9997 and Antares) bind to sperm within 2 h of mating, like SP. However, while SP remains bound to sperm at 4 days post-mating, none of the other network proteins are detectable at this time. We also observed that the same network proteins are detectable at 2 h post-mating in seminal receptacle tissue from which sperm have been removed, but are no longer detectable there by 4 days post-mating, suggesting short-term retention of these proteins in this female sperm storage organ. Our results suggest that these network proteins act transiently to facilitate the conditions for SP's binding to sperm, perhaps by modifying SP or the sperm surface, but are not part of a long-acting complex that stably attaches SP to sperm.
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