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　beta　3　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.