About: Serine 105 and 120 are important phosphorylation sites for porcine reproductive and respiratory syndrome virus N protein function

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About: Serine 105 and 120 are important phosphorylation sites for porcine reproductive and respiratory syndrome virus N protein function Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Serine 105 and 120 are important phosphorylation sites for porcine reproductive and respiratory syndrome virus N protein function
Creator	He, Shuyi Zhang, Guihong Li, Qi Chen, Yao Feng, Songlin Han, Xiaoliang Xing, Xiulin
Source	Elsevier; Medline; PMC
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, potentially decreasing the viral growth ability. Then, we mutated the phosphorylation sites (S105A and S120A) and rescued three mutated viruses, namely, A105, A120 and A105-120. Compared with wild-type virus titers, the titers of the mutated viruses at 48 hpi were significantly decreased. The Nsp(non-structural protein) 9 qPCR results were consistent with the multistep growth kinetics results. The infected PAMs (primary PAMs) results were similar with Marc-145.The findings indicated that the mutations impaired the viral replication ability. The confocal microscopy results suggested that mutations to residues 105 and 120 did not affect N protein distribution. Whether the mutations affected other functions of N protein and what the underlying mechanisms are need further investigation. In conclusion, our results show that residues 105 and 120 are phosphorylation sites and are important for N protein function and for viral replication ability.
has issue date	2018-04-07(xsd:dateTime)
bibo:doi	10.1016/j.vetmic.2018.04.010
bibo:pmid	29778185
has license	no-cc
sha1sum (hex)	60c83cfedf98238b33cbcb76551180c494eebd5d
schema:url	https://doi.org/10.1016/j.vetmic.2018.04.010
resource representing a document's title	Serine 105 and 120 are important phosphorylation sites for porcine reproductive and respiratory syndrome virus N protein function
has PubMed Central identifier	PMC7117435
has PubMed identifier	29778185
schema:publication	Vet Microbiol
resource representing a document's body	covid:60c83cfedf98238b33cbcb76551180c494eebd5d#body_text
is schema:about of	named entity 'PROTEIN FUNCTION' named entity 'protein' named entity 'study' named entity 'protein' named entity 'confocal microscopy' named entity 'mutations' named entity 'phosphorylation' named entity 'Serine' named entity 'ALVEOLAR MACROPHAGES' named entity 'INFECTED' named entity 'REGULATE' named entity 'MARC' named entity 'ABILITY' named entity 'CONCLUSION' named entity 'FUNCTIONS' named entity 'CONSISTENT WITH' named entity 'STUDY' named entity 'USED' named entity 'WILD-TYPE' named entity 'MUTATED' named entity 'GROWTH ABILITY' named entity 'REPLICATION' named entity 'PAMS' named entity 'EXPRESSED' named entity 'TYPE VIRUS' named entity 'VIRAL' named entity 'DID' named entity 'IMPORTANT' named entity 'ABUNDANT' named entity 'PCA' named entity 'VIRUSES' named entity 'PROTEIN CAN' named entity 'N PROTEIN' named entity 'MRNA' named entity 'N PROTEIN' named entity '105' named entity 'SF9 CELLS' named entity 'NEED' named entity '105' named entity 'HPI' named entity 'PORCINE REPRODUCTIVE AND RESPIRATORY SYNDROME VIRUS' named entity 'VIRAL REPLICATION' named entity 'COMPARED' named entity '120' named entity 'CONTAINS' named entity 'UNDERLYING' named entity 'OUR' named entity 'MULTISTEP' named entity 'IMPAIRED' named entity 'CONSTRUCTED' named entity 'PHOSPHORYLATION SITES' named entity 'SERINE' named entity 'GROWTH KINETICS' named entity 'ASSOCIATED WITH' named entity 'DECREASED' named entity 'PROTEIN DISTRIBUTION' named entity 'IMPORTANT' named entity 'PORCINE REPRODUCTIVE AND RESPIRATORY SYNDROME VIRUS' named entity 'RESULTS' named entity 'AFFECTED' named entity 'DECREASING' named entity 'PIG' named entity '145' named entity 'MECHANISMS' named entity '10%' named entity 'INVESTIGATION' named entity '120' named entity 'PHOSPHORYLATION SITES' named entity 'FINDINGS' named entity 'LEVEL' named entity 'SIMILAR' named entity 'NUCLEOCAPSID' named entity 'STRUCTURAL PROTEIN' named entity 'PROTEIN ' named entity 'DOWN-REGULATION'

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