Abstract
In addition to ribosomal protein synthesis and protein translation, ribosomal proteins also participate in tumorigenesis and tumor progression, immune responses, and viral replication. Here, we show that ribosomal protein L13 (RPL13) participates in the antiviral immune response induced by foot-and-mouth disease virus (FMDV), inhibiting FMDV replication. The overexpression of RPL13 promoted the induction and activation of the promoters of the nuclear factor-κB (NF-κB) and interferon-β (IFN-β) genes, and the expression and protein secretion of the antiviral factor IFN-β and proinflammatory cytokine interleukin-6 (IL-6). The knockdown of RPL13 had the opposite effects. We also found that the FMDV 3Cpro protease interacts with RPL13, and that its activity reduces the expression of RPL13, thus antagonizing the RPL13-mediated antiviral activity. This study extends our knowledge of the extraribosomal functions of ribosomal proteins and provides new scientific information on cellular antiviral defenses and virus-antagonizing mechanisms.
Highlights
In eukaryotes, the ribosome is the site of protein biosynthesis in cells
We demonstrated that when BHK-21 cells are infected with foot-and-mouth disease virus (FMDV), ribosomal protein L13 (RPL13), a molecule downstream from DEAD box helicase 3 (DDX3), synergistically promotes FMDV internal ribosome entry site (IRES)-dependent translation and viral replication [25]
We further investigated the function of RPL13 in PK-15 cells during FMDV infection
Summary
The ribosome is the site of protein biosynthesis in cells. The mature ribosome (80S) includes the large (60S) ribosomal subunit and the small (40S) ribosomal subunit. The 40S subunit contains 30 ribosomal proteins (RPs), whereas the 60S subunit contains 49 RPs. In normal cells, the ribosome biogenesis process is monitored in a complex and elaborate manner to ensure that the ribosomes are assembled accurately and function normally [1]. The specific stimulation of cells including stimulation of chemical agents or radiation, lack of nutrients and deregulation of genes required for ribosome biogenesis often causes the dysfunction of RPs and regulatory proteins in the nucleolus, inducing ‘ribosomal stress’. Under these conditions, ribosome synthesis is blocked and a large number of free RPs accumulate in the nucleus. Some ribosomal proteins evade those cellular regulatory processes and exert ribosome-independent functions, such as regulating the immune response [2]
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