About: Aspartic acid at residue 185 modulates the capacity of HP-PRRSV nsp4 to antagonize IFN-I expression

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About: Aspartic acid at residue 185 modulates the capacity of HP-PRRSV nsp4 to antagonize IFN-I expression 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	Aspartic acid at residue 185 modulates the capacity of HP-PRRSV nsp4 to antagonize IFN-I expression
Creator	Liu, Fang Feng, Wen-Hai Li, Yu Wang, Y Li, F Chen, Z.-D Chen, Zhong-Zhou Feng, Z.-Z Liu, Z.-Y Wang, Hong-Lei Wei, Ze-Yu Zhang, H.-L Zhang, Zi-Ding
Source	Elsevier; Medline; PMC
abstract	Abstract In a previous study, we have shown that highly-pathogenic PRRSV (HP-PRRSV) nonstructural protein 4 (nsp4) antagonizes type I IFN expression induced by poly(I:C). Here, we demonstrated that the mutation of Aspartic acid 185 (Asp185) impaired the ability of nsp4 to inhibit IFN-I production induced by poly(I:C). Subsequently, we verified that all the mutants at the residue 185, regardless of amino acid size (including Cys and Ser) and charge (including Glu and Lys), impaired nsp4 catalytic activity. However, when Asp185 in nsp4 was replaced by a similar structure amino acid Asparagine 185 (Asn185), nsp4 stayed but with a decreased protease activity. Importantly, the recombinant virus with Asn185 mutation in HP-PRRSV-nsp4 exhibited slower replication rate and higher ability to induce IFN-I expression compared with wild-type (wt) HP-PRRSV.
has issue date	2020-04-21(xsd:dateTime)
bibo:doi	10.1016/j.virol.2020.04.007
bibo:pmid	32452419
has license	els-covid
sha1sum (hex)	0b2dbadf20a5eb3e7114d06bc309f7a2dd7aa714
schema:url	https://doi.org/10.1016/j.virol.2020.04.007
resource representing a document's title	Aspartic acid at residue 185 modulates the capacity of HP-PRRSV nsp4 to antagonize IFN-I expression
has PubMed Central identifier	PMC7172695
has PubMed identifier	32452419
schema:publication	Virology
resource representing a document's body	covid:0b2dbadf20a5eb3e7114d06bc309f7a2dd7aa714#body_text
is schema:about of	named entity 'activity' named entity 'induced' named entity 'stayed' named entity 'capacity' named entity 'Aspartic acid' named entity 'PATHOGENIC' named entity 'POLY' named entity 'IMPAIRED' covid:arg/0b2dbadf20a5eb3e7114d06bc309f7a2dd7aa714 named entity 'demonstrated' named entity 'production' named entity 'type I IFN' named entity 'nonstructural protein' named entity 'structure' named entity 'wild-type' named entity 'Aspartic acid' named entity 'nonstructural protein' named entity 'induce' named entity 'expression' named entity 'However' named entity 'IFN' named entity 'recombinant virus' named entity 'type I IFN' named entity 'Lys' named entity 'Aspartic acid' named entity 'IFN' named entity 'Asparagine' named entity 'mutants' named entity 'nsp4' named entity 'IFN' named entity 'substrate' named entity 'serine protease' named entity 'nsp4' named entity 'nsp4' named entity 'nsp4' named entity 'nsp3' named entity 'nsp2' named entity 'nsp3' named entity 'protease' named entity 'amino acids' named entity 'nsp4' named entity 'PAMs' named entity 'mutation' named entity 'protease' named entity 'negatively charged' named entity 'hydrogen bonds' named entity 'hydrogen bonds' named entity 'proteolytic activity' named entity 'nsp4' named entity 'nsp4' named entity 'nsp3' named entity 'Nsp4' named entity 'nsp4' named entity 'nsp4' named entity 'moiety' named entity 'asparagine' named entity 'nsp3' named entity 'substrates' named entity 'substrates' named entity '4A-C' named entity 'substrates' named entity 'protease' named entity 'proteolytic activity' named entity 'Leu159' named entity 'nsp4' named entity 'amino acid' named entity 'protease' named entity 'nsp3' named entity 'mutation'

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