{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Chen Y"],"funding":["Modern Agro-industry Technology Research System","Public Welfare Special Funds for Agriculture Scientific Research","NSFC Guangdong of China"],"pagination":["128-135"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7117435"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["219"],"pubmed_abstract":["The nucleocapsid (N) protein is the most abundant protein of porcine reproductive and respiratory syndrome virus (PRRSV). It has been shown to be multiphosphorylated. However, the phosphorylation sites are still unknown. In this study, we used liquid chromatography tandem mass spectrometry (LC-MS/MS) to analyze the phosphorylation sites of N protein expressed in Sf9 cells. The results showed that N protein contains two phosphorylation sites. Since N protein can regulate IL-10, which may facilitate PRRSV replication, we constructed four plasmids (pCA-XH-GD, pCA-A105, pCA-A120 and pCA-A105-120) and transfected them into Pig alveolar macrophages (PAMs,3D4/2). The qPCR results showed that mutations at residues 105 and 120 were associated with down-regulation of the IL-10 mRNA level, potentiall"],"journal":["Veterinary microbiology"],"pubmed_title":["Serine 105 and 120 are important phosphorylation sites for porcine reproductive and respiratory syndrome virus N protein function."],"pmcid":["PMC7117435"],"funding_grant_id":["201203039","CARS-35","U0931003"],"pubmed_authors":["Zhang G","He S","Xing X","Han X","Chen Y","Li Q","Feng S"],"additional_accession":[]},"is_claimable":false,"name":"Serine 105 and 120 are important phosphorylation sites for porcine reproductive and respiratory syndrome virus N protein function.","description":"The nucleocapsid (N) protein is the most abundant protein of porcine reproductive and respiratory syndrome virus (PRRSV). It has been shown to be multiphosphorylated. However, the phosphorylation sites are still unknown. In this study, we used liquid chromatography tandem mass spectrometry (LC-MS/MS) to analyze the phosphorylation sites of N protein expressed in Sf9 cells. The results showed that N protein contains two phosphorylation sites. Since N protein can regulate IL-10, which may facilitate PRRSV replication, we constructed four plasmids (pCA-XH-GD, pCA-A105, pCA-A120 and pCA-A105-120) and transfected them into Pig alveolar macrophages (PAMs,3D4/2). The qPCR results showed that mutations at residues 105 and 120 were associated with down-regulation of the IL-10 mRNA level, potentiall","dates":{"release":"2018-01-01T00:00:00Z","publication":"2018 Jun","modification":"2025-04-04T22:45:43.81Z","creation":"2020-05-22T15:35:06Z"},"accession":"S-EPMC7117435","cross_references":{"pubmed":["29778185"],"doi":["10.1016/j.vetmic.2018.04.010"]}}