About: Modulation of host cell responses and evasion strategies for porcine reproductive and respiratory syndrome virus

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About: Modulation of host cell responses and evasion strategies for porcine reproductive and respiratory syndrome virus Goto Sponge NotDistinct Permalink

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

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Modulation of host cell responses and evasion strategies for porcine reproductive and respiratory syndrome virus
Creator	Sun, Yan Yoo, Dongwan Du, Yijun Kim, Oekyung Song, Cheng Liu, Hsiao-Ching
Source	Elsevier; Medline; PMC
abstract	Abstract The immune surveillance system protects host cells from viral infection, and viruses have evolved to escape this system for efficient proliferation in the host. Host cells produce cytokines and chemokines in response to viral infection, and among such effector molecules, type I interferons are the principal antiviral cytokines and therefore effective targets for viruses to disarm host surveillance. Porcine reproductive and respiratory syndrome virus (PRRSV) expresses proteins that circumvent the IFN response and other cellular processes, and to compensate the small coding capacity of PRRSV, these proteins are multifunctional. To date, at least four viral proteins have been identified and studied as viral antagonists of host defenses: N as a structural protein and three non-structural proteins, Nsp1 (Nsp1α and Nsp1β), Nsp2, and Nsp11. Among these, N and Nsp1 are nuclear-cytoplasmic proteins distributed in both the nucleus and cytoplasm of cells. Nsp1 and Nsp2 are viral proteases while Nsp11 is an endoribonuclease. This review describes the current understanding of the role of these proteins in modulating the host innate immune responses. Blocking against virus-mediated inhibition of the innate response may lead to the future development of effective vaccines. The understanding of viral mechanisms modulating the normal cellular processes will be a key to the design of an effective control strategy for PRRS.
has issue date	2010-12-31(xsd:dateTime)
bibo:doi	10.1016/j.virusres.2010.07.019
bibo:pmid	20655963
has license	els-covid
sha1sum (hex)	92fa1b14f2644d87fb2117e50b6372a5d3c5fb59
schema:url	https://doi.org/10.1016/j.virusres.2010.07.019
resource representing a document's title	Modulation of host cell responses and evasion strategies for porcine reproductive and respiratory syndrome virus
has PubMed Central identifier	PMC7114477
has PubMed identifier	20655963
schema:publication	Virus Research
resource representing a document's body	covid:92fa1b14f2644d87fb2117e50b6372a5d3c5fb59#body_text
is schema:about of	named entity 'Host cells' named entity 'proteases' named entity 'cellular processes' named entity 'immune surveillance' named entity 'cytokines' named entity 'M180' named entity 'cytokine' named entity 'viruses' named entity 'gene' named entity 'Cajal body' named entity 'proteasome' named entity 'dimerization' named entity 'cytoplasmic' named entity 'IFN' named entity 'small nucleolar RNAs' named entity 'genome' named entity 'genotypes' named entity 'response element' named entity 'kidney cells' named entity 'histones' named entity 'RNase' named entity 'amino acids' named entity 'phosphorylation' named entity 'Nsp2' named entity 'coronaviruses' named entity 'P-TEFb' named entity 'STATs' named entity 'long terminal repeats' named entity 'La Rocca' named entity 'infection' named entity 'IRF3' named entity 'ISRE' named entity 'STAT1' named entity 'endoribonuclease' named entity 'IFN' named entity 'SARS-CoV' named entity 'protein complex' named entity 'N-terminus' named entity 'Infection' named entity 'cDNA clone' named entity 'Nsp1' named entity 'pre-rRNA' named entity 'nucleocapsid' named entity 'ribosomal RNA' named entity 'RIG-I' named entity 'pathogenesis' named entity 'protein' named entity 'IL-10' named entity 'confocal microscopy' named entity 'pig' named entity 'protein' named entity 'methylation' named entity 'infection' named entity 'type I IFN' named entity 'phosphorylation' named entity 'down-regulation' named entity 'glycoprotein' named entity 'antiviral' named entity 'cytoplasm' named entity 'infection' named entity 'secondary bacterial infections' named entity 'ubiquitinylation' named entity 'downregulation' named entity 'Nsp2' named entity 'PRD' named entity 'Golgi complex' named entity 'nucleocapsid' named entity 'PIAS1' named entity 'viral genome' named entity 'immune surveillance' named entity 'genetic markers' named entity 'AP-1' named entity 'NF-B' named entity 'gene expression' named entity 'dimerization' named entity 'EAV'

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