Interaction between 038R and 125R of Cherax quadricarinatus iridovirus (CQIV) and their effects on virus replication.

Iridovirids are a group icosahedral viruses containing linear double-stranded DNA, and mainly infect invertebrates and poikilothermic vertebrates. Cherax quadricarinatus iridovirus (CQIV) is a new species of the family Iridoviridae and can cause high mortality in shrimps. In CQIV genome, there are 25 conserved genes and the putative products are involved in several viral processes. In this study, three core protein including CQIV-032R, CQIV-125R and CQIV-160L were identified to interact with CQIV-038R by yeast two-hybrid (Y2H), and the interaction between CQIV-038R and CQIV-125R was further confirmed by co-immunoprecipitation (Co-IP) assays. In the expression system, EGFP-038R and mCherry-125R were colocalized in the cytoplasm when co-expressed in Sf9 cells. Moreover, silencing the expression of 038R, 125R or both of these two proteins respectively in C. quadricarinatus cells by small interfering RNAs showed significantly inhibit CQIV replication. Collectively, we identified the interaction between 038R and 125R, and demonstrated they are essential for CQIV replication.

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

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 ß3 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.