Abstract
Protein phosphatase-1 (PP1) has an important role in many cell functions, such as cell differentiation, development, immune response and tumorigenesis. However, the specific role of PP1 in the antiviral response in fish remains to be elucidated. In this study, the PPP1R3G homolog was identified in the grass carp (Ctenopharyngodon idella) and its role in defence against the GCRV infection was investigated. Phylogenetic analysis demonstrated that CiPPP1R3G clustered with homologues from other teleosts. Temporal expression analysis in vivo revealed that the expression level of CiPPP1R3G was significantly up-regulated in response to GCRV infection in grass carps, especially in the intestine and head-kidney. Cellular distribution analysis revealed that CiPPP1R3G was located in the nucleus and cytoplasm. Overexpression of CiPPP1R3G significantly negatively regulated the expression of CiIRF3, thus inhibiting its activation. In summary, we systematically analyzed the PPP1R3G gene in grass carp and illustrated its function as a negative regulator in the anti-GCRV immune responses.
Highlights
Protein phosphatase 1 (PP1), a serine (Ser)/threonine (Thr) phosphatase, is a member of the phosphoprotein phosphatase (PPP) superfamily [1,2,3]
BLASTP analysis showed that CiPPP1R3G had highest similarity to Gobiocypris rarus PPP1R3G (92.8%) (GenBank ID., MT833844), followed by PPP1R3G of Cyprinus carpio (86.9%) (GenBank ID., XM_019066810) and Carassius auratus (84.8%) (GenBank ID., XM_026200865)
A previous study reported that PP1 can modulate the phosphorylation of the capsid of Venezuelan equine encephalitis virus (VEEV), and the inhibition of PP1 could slow down the viral replication in human cells
Summary
Protein phosphatase 1 (PP1), a serine (Ser)/threonine (Thr) phosphatase, is a member of the phosphoprotein phosphatase (PPP) superfamily [1,2,3]. It is one of the most conserved proteins in eukaryotic cells [4]. PP1 plays crucial roles in many biological processes including cell division and meiosis, metabolism, cell cycle arrest and apoptosis. It exerts these functions through the PPP1R3G Negatively Regulates IRF3 nucleophilic attack to catalyse the hydrolysis of serine/threoninelinked phosphate monoesters, and dephosphorylates the substrate [4, 5]. These regulatory subunits are very important for the function of PP1, and seven genes that encode different G subunits have been recognised so far: PPP1R3A to PPP1R3G [4]
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