Interferon functional analog activates antiviral Jak/Stat signaling through integrin in an arthropod

• Main Authors: Jie Gao, Bao-Rui Zhao, Hui Zhang, Yan-Lin You, Fang Li, Xian-Wei Wang
• Format: Article
• Language: English
• Published: Elsevier 2021-09-01
• Series: Cell Reports
• Subjects: invertebrate; arthropod; cytokine; vago; ficolin; white spot syndrome virus
• Online Access: http://www.sciencedirect.com/science/article/pii/S2211124721012158

Summary: Drosophila Vago is a small antiviral peptide. Its ortholog in Culex mosquito was found to be an interferon-like cytokine that limits virus replication through activating Jak/Stat signaling. However, this activation is independent of Domeless, the sole homolog of vertebrate type I cytokine receptor. How Vago activates the Jak/Stat pathway remains unknown. Herein, we report this process is dependent on integrin in kuruma shrimp (Marsupenaeus japonicus). Shrimp Vago-like (MjVago-L) plays an antiviral role by activating the Jak/Stat pathway and inducing Stat-regulated Ficolin. Blocking integrin abrogates the role of MjVago-L. The interaction between MjVago-L and integrin β3 is confirmed. An Asp residue in MjVago-L is found critical for the interaction and MjVago-L’s antiviral role. Moreover, Fak, a key adaptor of integrin signaling, mediates MjVago-L-induced Jak/Stat activation. Therefore, this study reveals that integrin, as the receptor of MjVago-L, mediates Jak/Stat activation. The establishment of the MjVago-L/integrin/Fak/Jak/Stat/Ficolin axis provides insights into antiviral cytokine signaling in invertebrates.