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A small open reading frame (smORF) or short open reading frame (sORF) encodes a polypeptide of <100 amino acids in eukaryotes (50 amino acids in prokaryotes). Studies have shown that several sORF-encoded peptides (SEPs) have important physiological functions in different organisms. Many ribosomal proteins belonging to SEPs play important roles in several cellular processes, such as DNA damage repair and apoptosis. Several studies have implicated SEPs in response to infection and innate immunity, but the mechanisms have been unclear for most of them. In this study, we identified a sORF-encoded ribosomal protein S27 (RPS27) in  Marsupenaeus japonicus . The expression of  MjRPS27  was significantly upregulated in shrimp infected with white spot syndrome virus (WSSV). After knockdown of  MjRPS27  by RNA interference, WSSV replication increased significantly. Conversely, after  Mj RPS27 overexpression, WSSV replication decreased in shrimp and the survival rate of the shrimp increased significantly. These results suggested that  Mj RPS27 inhibited viral replication. Further study showed that, after  Mj RPS27 knockdown, the mRNA expression level of  Mj Dorsal,  Mj Relish, and antimicrobial peptides (AMPs) decreased, and the nuclear translocation of  Mj Dorsal and  Mj Relish into the nucleus also decreased. These findings indicated that  Mj RPS27 might activate the NF-κB pathway and regulate the expression of AMPs in shrimp after WSSV challenge, thereby inhibiting viral replication. We also found that  Mj RPS27 interacted with WSSV's envelope proteins, including VP19, VP24, and VP28, suggesting that  Mj RPS27 may inhibit WSSV proliferation by preventing virion assembly in shrimp. This study was the first to elucidate the function of the ribosomal protein  Mj RPS27 in the antiviral immunity of shrimp.

RPS27, a sORF-Encoded Polypeptide, Functions Antivirally by Activating the NF-κB Pathway and Interacting With Viral Envelope Proteins in Shrimp