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Long-term interaction between Drosophila sperm and sex peptide is mediated by other seminal proteins that bind only transiently to sperm

机译:果蝇精子和性肽之间的长期相互作用由其他精髓粘合的其他精髓蛋白介导的

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摘要

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.
机译:精髓液蛋白质在交配的果蝇黑素体女性中引发了几种后交配的生理变化。在交配后,其中一些变化持续存在,因为导致这些变化的精髓(SP),与储存在雌性生殖道中的精子结合的精髓蛋白质。 SP的精子结合由至少八个精髓蛋白的网络介导。我们在这里展示了一些这些网络蛋白质(CG1656,CG1652,CG9997和Antares)与相配的2小时内结合,如SP。然而,虽然在交配后4天,SP保持与精子结合,但在此时没有其他网络蛋白质可以检测到。我们还观察到,相同的网络蛋白质在术后2小时,从中除去精子,但在交配后4天不再可检测到其中,表明这些蛋白质的短期保留女性精子储存器官。我们的研究结果表明,这些网络蛋白瞬时行动,以促进SP与精子的结合的条件,也许通过修改SP或精子表面,而是不稳定地附着SP至精子的长作用络合物的一部分。

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