Drosophila serpin 27A is a likely target for immune suppression of the blood cell-mediated melanotic encapsulation response.
Drosophila serpin 27A is a likely target for immune suppression of the blood cell-mediated melanotic encapsulation response.
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DOI：
10.1016/j.jinsphys.2004.10.013
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发表时间：
2005-02
影响因子：
2.2
通讯作者：
A. Nappi;F. Frey;Y. Carton
中科院分区：
文献类型：
--
作者：
A. Nappi;F. Frey;Y. Carton
内寄生蜂Leptopilina boulardi的无毒菌株屈服于黑腹果蝇宿主幼虫中血细胞介导的黑色素包囊反应。有毒黄蜂菌株有效地消除了细胞反应，引入宿主的物质特异性靶向并有效抑制一种或多种免疫信号传导途径，包括控制酚氧化酶介导的黑色素包囊的元件。本研究暗示参与果蝇Toll途径在细胞先天免疫调节丝氨酸蛋白酶抑制剂丝氨酸蛋白酶抑制剂27 A（Spn27 A），这通常是作为一个负调节酚氧化酶。将Spn27A导入正常高免疫活性的D.黑腹果蝇幼虫在卵周围形成黑色素囊的能力显著降低。布拉迪。这项研究证实了Spn27A在黑化级联反应中的作用，并确定该途径和相关的血细胞反应可以通过寄生激活。酚氧化酶的激活和随后的黑色素反应的位点特异性定位是血细胞反应的关键组成部分，Spn27 A和介导其活性的信号传导元件可能代表L.布拉迪。
Avirulent strains of the endoparasitoid Leptopilina boulardi succumb to a blood cell-mediated melanotic encapsulation response in host larvae of Drosophila melanogaster. Virulent wasp strains effectively abrogate the cellular response with substances introduced into the host that specifically target and effectively suppress one or more immune signaling pathways, including elements that control phenoloxidase-mediated melanotic encapsulation. The present study implicates involvement of the Drosophila Toll pathway in cellular innate immunity by regulating the serine protease inhibitor Serpin 27A (Spn27A), which normally functions as a negative regulator of phenoloxidase. The introduction of Spn27A into normally highly immune competent D. melanogaster larvae significantly reduced their ability to form melanotic capsules around eggs of L. boulardi. This study confirms the role of Spn27A in the melanization cascade and establishes that this pathway and associated blood cell responses can be activated by parasitization. The activation of phenoloxidase and the site-specific localization of the ensuing melanotic response are such critical components of the blood cell response that Spn27A and the signaling elements mediating its activity are likely to represent prime targets for immune suppression by L. boulardi.