WITHDRAWN: C-type lectin interacting with β-integrin enhances hemocytic encapsulation in the cotton bollworm, Helicoverpa armigera.
WITHDRAWN: C-type lectin interacting with β-integrin enhances hemocytic encapsulation in the cotton bollworm, Helicoverpa armigera.
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DOI：
10.1016/j.ibmb.2017.02.004
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发表时间：
2017-02
影响因子：
3.8
通讯作者：
Pan Wang;Xiao-Rong Zhuo;L. Tang;Xu-Sheng Liu;Yu-Feng Wang;Guo-xiu Wang;Xiao-qiang Yu;Jia‐Lin Wang
中科院分区：
文献类型：
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作者：
Pan Wang;Xiao-Rong Zhuo;L. Tang;Xu-Sheng Liu;Yu-Feng Wang;Guo-xiu Wang;Xiao-qiang Yu;Jia‐Lin Wang
无脊椎动物的包膜反应类似于脊椎动物肉芽肿的形成，当蜕皮激素信号被阻断时，这种反应会严重受损。然而，该包埋反应的分子机制以及蜕皮激素对其的调节仍不清楚。在我们以前的研究中，我们发现棉铃虫的C型凝集素HaCTL3作为模式识别受体(PRR)参与了抗细菌免疫反应。在目前的研究中，我们证明了HaCTL3参与了对寄生虫的防御，并直接结合到线虫的表面。Ourin和vitroandin的活体研究表明，HaCTL3增强了血细胞的包膜和黑化，而位于血细胞表面的棉铃虫整合素(Haβ-Integrin，Haβ-整合素)参与了包埋。此外，免疫共沉淀实验表明，HaCTL3与Haβ整合素相互作用，Haβ整合素的敲除导致包被HaCTL3的微球的包封率降低。这些结果表明，在包埋反应中，Haβ整合素是HaCTL3的血细胞受体。此外，我们证明了20-羟基蜕皮激素(20E)治疗显著诱导HaCTL3的表达，而20E受体(ECR)/超阿司匹林(USP)的敲除则取消了这一反应。总体而言，本研究首次提供了存在血细胞受体(Haβ整合素)的证据，该受体与PrR HaCTL3相互作用，促进昆虫的包膜反应，并证明了类固醇激素蜕皮激素对这一过程的调节。
The encapsulation reaction in invertebrates is analogous to granuloma formation in vertebrates, and this reaction is severely compromised when ecdysone signaling is blocked. However, the molecular mechanism underlying the encapsulation reaction and its regulation by ecdysone remains obscure. In our previous study, we found that the C-type lectin HaCTL3, from the cotton bollwormHelicoverpa armigera, is involved in anti-bacterial immune response, acting as a pattern recognition receptor (PRR). In the current study, we demonstrate that HaCTL3 is involved in defense against parasites and directly binds to the surface of nematodes. Ourin vitroandin vivostudies indicate that HaCTL3 enhances hemocytic encapsulation and melanization, whereasH. armigeraβ-integrin (Haβ-integrin), located on the surface of hemocytes, participates in encapsulation. Additionally, co-immunoprecipitation experiments reveal HaCTL3 interacts with Haβ-integrin, and knockdown of Haβ-integrin leads to reduced encapsulation of HaCTL3-coated beads. These results indicate that Haβ-integrin serves as a hemocytic receptor of HaCTL3 during the encapsulation reaction. Furthermore, we demonstrate that 20-hydroxyecdysone (20E) treatment dramatically induces the expression of HaCTL3, and knockdown of the 20E receptor (EcR)/ultraspiracle (USP), abrogates this response. Overall, this study provides the first evidence of the presence of a hemocytic receptor (Haβ-integrin), that interacts with the PRR HaCTL3 to facilitate encapsulation reaction in insects and demonstrates the regulation of this process by the steroid hormone ecdysone.