About: The nonstructural protein 11 of porcine reproductive and respiratory syndrome virus inhibits NF-κB signaling by means of its deubiquitinating activity

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About: The nonstructural protein 11 of porcine reproductive and respiratory syndrome virus inhibits NF-κB signaling by means of its deubiquitinating activity Goto Sponge NotDistinct Permalink

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

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	The nonstructural protein 11 of porcine reproductive and respiratory syndrome virus inhibits NF-κB signaling by means of its deubiquitinating activity
Creator	Chen, Huanchun Zhang, Huan Fang, Liurong Luo, Rui Wang, Dang Xiao, Shaobo Li, Kui Ouyang, Chao Ouyang, Haiping Fan, Jinxiu
Source	Elsevier; Medline; PMC
abstract	Abstract Since its emergence in the late 1980s, porcine reproductive and respiratory syndrome (PRRS) has been devastating the swine industry worldwide. The causative agent is an Arterivirus, referred to as PRRS virus (PRRSV). The pathogenic mechanisms of PRRS are poorly understood, but are believed to correlate with the ability of PRRSV to inhibit immune responses of the host. However, precisely how the virus is capable of doing so remains obscure. In this study, we showed that PRRSV infection led to reduced ubiquitination of cellular proteins. Screening all of the 12 nonstructural proteins (Nsps) encoded by PRRSV revealed that, apart from the Nsp2 which contains the deubiqintinating (DUB) ovarian tumor (OTU) domain, Nsp11, which encodes a unique and conserved endoribonuclease (NendoU) throughout the Nidovirus order, also possesses DUB activity. In vivo assay demonstrated that Nsp11 specifically removed lysine 48 (K48)-linked polyubiquitin chains and the conserved sites C112, H144, D173, K180, and Y219 were critical for its DUB activity. Remarkably, DUB activity was responsible for the capacity of Nsp11 to inhibit nuclear factor κB (NF-κB) activation. Mutations abrogating the DUB activity of Nsp11 toward K48-linked polyubiquitin chains of IκBα nullified the suppressive effect on NF-κB. Our data add Nsp11 to the list of DUBs encoded by PRRSV and uncover a novel mechanism by which PRRSV cripples host innate immune responses.
has issue date	2015-12-31(xsd:dateTime)
bibo:doi	10.1016/j.molimm.2015.08.011
bibo:pmid	26342881
has license	els-covid
sha1sum (hex)	e14818bce005d0dcb0c8edea070e7567577bab02
schema:url	https://doi.org/10.1016/j.molimm.2015.08.011
resource representing a document's title	The nonstructural protein 11 of porcine reproductive and respiratory syndrome virus inhibits NF-κB signaling by means of its deubiquitinating activity
has PubMed Central identifier	PMC7112538
has PubMed identifier	26342881
schema:publication	Molecular Immunology
resource representing a document's body	covid:e14818bce005d0dcb0c8edea070e7567577bab02#body_text
is schema:about of	named entity 'demonstrated' named entity 'domain' named entity 'unique' named entity 'encodes' named entity 'DUB' named entity 'removed' named entity 'cellular proteins' named entity 'lysine' named entity 'PRRS' named entity 'nonstructural protein' named entity 'virus' covid:arg/e14818bce005d0dcb0c8edea070e7567577bab02 named entity 'OTU' named entity 'host' named entity 'activity' named entity 'mechanisms' named entity 'study' named entity 'PRRS' named entity 'RNA synthesis' named entity '1.6' named entity 'Arteriviridae' named entity 'primers' named entity 'polyubiquitin chains' named entity 'emergence' named entity 'assay' named entity 'correlate' named entity 'believed' named entity 'worldwide' named entity 'sites' named entity 'referred' named entity 'PRRS' named entity 'immune responses' named entity 'virus' named entity 'PRRSV' named entity 'porcine reproductive and respiratory syndrome' named entity 'PRRSV' named entity 'Nidovirus' named entity 'PRRSV' named entity 'PRRSV' named entity 'Promega' named entity 'antibodies' named entity 'plasmid' named entity 'luciferase' named entity 'ubiquitination' named entity 'swine' named entity 'high fever' named entity 'U.S.A.' named entity 'genotypes' named entity 'immunoprecipitated' named entity 'ubiquitin-like' named entity 'antibody' named entity 'NF-B' named entity 'cysteine' named entity 'epitope tag' named entity 'amino acid sequences' named entity 'MOIs' named entity 'NF-B' named entity 'coronaviruses' named entity 'cysteine' named entity 'ubiquitination' named entity 'ubiquitin' named entity 'Protein' named entity 'EAV' named entity 'ubiquitinated' named entity 'sodium dodecyl sulfate' named entity 'EAV' named entity 'CCL5' named entity 'ubiquitin' named entity 'cysteine' named entity 'MG132' named entity 'HEK293 cells' named entity 'nonstructural proteins'

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