Mating-regulated atrial proteases control reinsemination rates in Anopheles gambiae females.

Mating-regulated atrial proteases control reinsemination rates in Anopheles gambiae females.
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交配调节的心房蛋白酶控制冈比亚按蚊雌性的再授精率。

DOI:
10.1038/s41598-020-78967-y
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发表时间:
2020-12-15
期刊:
影响因子:
4.6
通讯作者:
Catteruccia F
Catteruccia F
中科院分区:
综合性期刊3区
文献类型:
--
作者:
Bascuñán P;Gabrieli P;Mameli E;Catteruccia F

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冈比亚按蚊是人类疟疾最重要的传播媒介。这些蚊子的繁殖成功依赖于一个单一的交配事件后,大多数女性成为永久难治性进一步交配。这种不应性行为至少部分由雄性合成的类固醇激素20-羟基蜕皮激素(20 E)介导,该激素与其他精液分泌物一起包装成凝胶状交配塞,并在交配期间转移到雌性心房。在这项研究中,我们表明,20 E调节糜蛋白酶样丝氨酸蛋白酶特异性表达在生殖道的An。冈比亚雌性在调节雌性对交配的敏感性方面发挥重要作用。通过RNA干扰沉默这些蛋白酶会损害正确的插塞加工,并减缓类固醇激素20 E从交配插塞的释放。反过来,消耗这些蛋白酶之一,交配调节心房蛋白酶1(MatRAP 1),减少女性对进一步交配的不应性,因此很大一部分女性再次交配。显微镜分析表明,MatRAP 1是本地化的一个以前未检测到的围食基质样结构周围的交配插头。这些数据提供了新的见解,形成这些重要的疟疾病媒交配后生物学的分子机制。
Anopheles gambiae mosquitoes are the most important vectors of human malaria. The reproductive success of these mosquitoes relies on a single copulation event after which the majority of females become permanently refractory to further mating. This refractory behavior is at least partially mediated by the male-synthetized steroid hormone 20-hydroxyecdysone (20E), which is packaged together with other seminal secretions into a gelatinous mating plug and transferred to the female atrium during mating. In this study, we show that two 20E-regulated chymotrypsin-like serine proteases specifically expressed in the reproductive tract of An. gambiae females play an important role in modulating the female susceptibility to mating. Silencing these proteases by RNA interference impairs correct plug processing and slows down the release of the steroid hormone 20E from the mating plug. In turn, depleting one of these proteases, the Mating Regulated Atrial Protease 1 (MatRAP1), reduces female refractoriness to further copulation, so that a significant proportion of females mate again. Microscopy analysis reveals that MatRAP1 is localized on a previously undetected peritrophic matrix-like structure surrounding the mating plug. These data provide novel insight into the molecular mechanisms shaping the post-mating biology of these important malaria vectors.
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