About: Enterovirus 71 protease 2A(pro) and 3C(pro) differentially inhibit the cellular endoplasmic reticulum-associated degradation (ERAD) pathway via distinct mechanisms, and enterovirus 71 hijacks ERAD component p97 to promote its replication

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About: Enterovirus 71 protease 2A(pro) and 3C(pro) differentially inhibit the cellular endoplasmic reticulum-associated degradation (ERAD) pathway via distinct mechanisms, and enterovirus 71 hijacks ERAD component p97 to promote its replication 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
title	Enterovirus 71 protease 2A(pro) and 3C(pro) differentially inhibit the cellular endoplasmic reticulum-associated degradation (ERAD) pathway via distinct mechanisms, and enterovirus 71 hijacks ERAD component p97 to promote its replication
Creator	Huang, He Zhao, Zhendong Wang, Jianwei Wang, Tao Jin, Qi Zhu, Yuanmei Sun, Lei Cheng, Chaofei Pei, Bin Zhang, Chongyang
topic	covid:90967c73d3f3e10ba8ab863b3deba3a40ca22fd1#this
source	Medline; PMC
abstract	Endoplasmic reticulum-associated degradation (ERAD) is an important function for cellular homeostasis. The mechanism of how picornavirus infection interferes with ERAD remains unclear. In this study, we demonstrated that enterovirus 71 (EV71) infection significantly inhibits cellular ERAD by targeting multiple key ERAD molecules with its proteases 2A(pro) and 3C(pro) using different mechanisms. Ubc6e was identified as the key E2 ubiquitin-conjugating enzyme in EV71 disturbed ERAD. EV71 3C(pro) cleaves Ubc6e at Q219G, Q260S, and Q273G. EV71 2A(pro) mainly inhibits the de novo synthesis of key ERAD molecules Herp and VIMP at the protein translational level. Herp differentially participates in the degradation of different glycosylated ERAD substrates α-1 antitrypsin Null Hong Kong (NHK) and the C-terminus of sonic hedgehog (SHH-C) via unknown mechanisms. p97 was identified as a host factor in EV71 replication; it redistributed and co-exists with the viral protein and other known replication-related molecules in EV71-induced replication organelles. Electron microscopy and multiple-color confocal assays also showed that EV71-induced membranous vesicles were closely associated with the endoplasmic reticulum (ER), and the ER membrane molecule RTN3 was redistributed to the viral replication complex during EV71 infection. Therefore, we propose that EV71 rearranges ER membranes and hijacks p97 from cellular ERAD to benefit its replication. These findings add to our understanding of how viruses disturb ERAD and provide potential anti-viral targets for EV71 infection.
has issue date	2017-10-06(xsd:dateTime)
bibo:doi	10.1371/journal.ppat.1006674
bibo:pmid	28985237
has license	cc-by
sha1sum (hex)	90967c73d3f3e10ba8ab863b3deba3a40ca22fd1
schema:url	https://doi.org/10.1371/journal.ppat.1006674
resource representing a document's title	Enterovirus 71 protease 2A(pro) and 3C(pro) differentially inhibit the cellular endoplasmic reticulum-associated degradation (ERAD) pathway via distinct mechanisms, and enterovirus 71 hijacks ERAD component p97 to promote its replication
has PubMed Central identifier	PMC5650186
has PubMed identifier	28985237
schema:publication	PLoS Pathog
resource representing a document's body	covid:90967c73d3f3e10ba8ab863b3deba3a40ca22fd1#body_text
is http://vocab.deri.ie/void#inDataset of	proxy:http/ns.inria.fr/covid19/90967c73d3f3e10ba8ab863b3deba3a40ca22fd1
is schema:about of	named entity 'DIFFERENT' named entity 'HOW' named entity 'STUDY' named entity 'VESICLES' named entity 'VIMP' named entity 'DEMONSTRATED' named entity 'RTN3' named entity 'MULTIPLE' named entity 'DISTINCT' named entity 'USING' named entity 'CLEAVES' named entity 'POTENTIAL' named entity 'UNDERSTANDING' named entity 'MECHANISM' named entity 'CELLULAR' named entity 'VIRAL' named entity 'ORGANELLES' named entity 'MOLECULE' named entity 'ANTITRYPSIN' named entity 'PROTEASES' named entity 'FUNCTION' named entity 'ENTEROVIRUS 71' named entity 'ERAD' named entity 'add' named entity 'translational' named entity 'pro' named entity 'The mechanism' named entity 'replication' named entity 'mechanisms' named entity 'de novo synthesis' named entity 'multiple' named entity 'rearranges' named entity 'remains' named entity 'ERAD' named entity 'PATHWAY' named entity 'PROMOTE' named entity 'SONIC HEDGEHOG' named entity 'INDUCED' named entity 'ORG' named entity 'PROTEASE' named entity 'HERP' named entity 'FINDINGS' named entity 'ER MEMBRANE' named entity 'RELATED' named entity 'TARGETS' named entity 'ERAD' named entity 'VIRUSES' named entity 'HTTPS' named entity 'IDENTIFIED' named entity 'PICORNAVIRUS INFECTION' named entity 'HOST FACTOR' named entity 'VIRAL REPLICATION COMPLEX' named entity 'INFECTION' named entity 'KNOWN' named entity 'CELLULAR HOMEOSTASIS' named entity 'PROTEIN ' named entity '2F10' named entity 'LEVEL' named entity 'ENDOPLASMIC RETICULUM-ASSOCIATED DEGRADATION' named entity 'REPLICATION' named entity 'DISTINCT' covid:arg/90967c73d3f3e10ba8ab863b3deba3a40ca22fd1 named entity 'ENTEROVIRUS 71' named entity 'MECHANISMS' named entity 'ENDOPLASMIC RETICULUM-ASSOCIATED DEGRADATION' named entity 'PROTEASE' named entity 'COMPONENT' named entity 'CELLULAR' named entity 'ITS' named entity 'P97'

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