Scallop RIG-I-like receptor 1 responses to polyinosinic:polycytidylic acid challenge and its interactions with the mitochondrial antiviral signaling protein

Abstract

Retinoic acid-inducible gene I (RIG-I)-like receptors (RLRs) are a class of pattern recognition receptors located in the cytoplasm that play a key role in antiviral innate immunity in animals. However, few studies have been conducted on the function of RLR proteins in invertebrates. In this study, the complete coding sequence of the RLR gene of the Zhikong scallop, Chlamys farreri, was obtained and named CfRLR1 with an aim to study the response of CfRLR1 to polyinosinic:polycytidylic acid [poly (I:C)] stimulation and the interaction between the CfRLR1 and C. farreri mitochondrial antiviral signaling (MAVS) protein. Sequence analysis revealed that CfRLR1 encodes 1161 amino acids, and the encoded protein covers two tandem caspase activation and recruitment domains (CARDs), a helicase domain, and a C-terminal regulatory domain. Phylogenetic analysis revealed that CfRLR1 belongs to the RLR family of mollusks. Quantitative real-time polymerase chain reaction showed that CfRLR1 mRNA was expressed in all tested tissues, with its highest expression observed in feet and gill tissues. Furthermore, CfRLR1 expression in the gill tissues was significantly induced after the poly (I:C) challenge. Finally, the results of co-immunoprecipitation and yeast two-hybrid assays revealed that CfRLR1 can bind to the CfMAVS protein via CARD–CARD interactions. Overall, our results elucidate the immune function of invertebrate RLR proteins and provide valuable information on viral disease control for scallop farming.