About: Caspase-1 Promotes Epstein-Barr Virus Replication by Targeting the Large Tegument Protein Deneddylase to the Nucleus of Productively Infected Cells

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About: Caspase-1 Promotes Epstein-Barr Virus Replication by Targeting the Large Tegument Protein Deneddylase to the Nucleus of Productively Infected Cells 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	Caspase-1 Promotes Epstein-Barr Virus Replication by Targeting the Large Tegument Protein Deneddylase to the Nucleus of Productively Infected Cells
Creator	Callegari, Simone Chen, Xinsong Gastaldello, Stefano Everett, Roger Masucci, Maria
Source	Medline; PMC
abstract	The large tegument proteins of herpesviruses contain N-terminal cysteine proteases with potent ubiquitin and NEDD8-specific deconjugase activities, but the function of the enzymes during virus replication remains largely unknown. Using as model BPLF1, the homologue encoded by Epstein-Barr virus (EBV), we found that induction of the productive virus cycle does not affect the total level of ubiquitin-conjugation but is accompanied by a BPLF1-dependent decrease of NEDD8-adducts and accumulation of free NEDD8. Expression of BPLF1 promotes cullin degradation and the stabilization of cullin-RING ligases (CRLs) substrates in the nucleus, while cytoplasmic CRLs and their substrates are not affected. The inactivation of nuclear CRLs is reversed by the N-terminus of CAND1, which inhibits the binding of BPLF1 to cullins and prevents efficient viral DNA replication. Targeting of the deneddylase activity to the nucleus is dependent on processing of the catalytic N-terminus by caspase-1. Inhibition of caspase-1 severely impairs viral DNA synthesis and the release of infectious virus, pointing a previously unrecognized role of the cellular response to danger signals triggered by EBV reactivation in promoting virus replication.
has issue date	2013-10-10(xsd:dateTime)
bibo:doi	10.1371/journal.ppat.1003664
bibo:pmid	24130483
has license	cc-by
sha1sum (hex)	bdb16338832867fb4c294b2694e8e23da78f3597
schema:url	https://doi.org/10.1371/journal.ppat.1003664
resource representing a document's title	Caspase-1 Promotes Epstein-Barr Virus Replication by Targeting the Large Tegument Protein Deneddylase to the Nucleus of Productively Infected Cells
has PubMed Central identifier	PMC3795028
has PubMed identifier	24130483
schema:publication	PLoS Pathog
resource representing a document's body	covid:bdb16338832867fb4c294b2694e8e23da78f3597#body_text
is schema:about of	named entity 'degradation' named entity 'cytoplasmic' named entity 'Large' named entity 'Targeting' named entity 'Infected' named entity 'CASPASE-1' named entity 'TEGUMENT PROTEIN' named entity 'LARGE' named entity 'CATALYTIC' named entity 'IMPAIRS' named entity 'RING' named entity 'NEDD8' named entity 'EXPRESSION' named entity 'TEGUMENT PROTEINS' named entity 'NUCLEUS' named entity 'THEIR' named entity 'CYCLE' named entity 'DNA SYNTHESIS' named entity 'DECREASE' named entity 'SEVERELY' named entity 'UNKNOWN' named entity 'PREVENTS' named entity 'VIRUS REPLICATION' named entity 'DEGRADATION' named entity 'INFECTIOUS' named entity 'VIRAL DNA' named entity 'LIGASES' named entity 'CONTAIN' named entity 'VIRAL DNA REPLICATION' named entity 'RELEASE' named entity 'CULLIN' named entity 'DEPENDENT' named entity 'HOMOLOGUE' named entity 'DENEDDYLASE ACTIVITY' named entity 'TRIGGERED BY' named entity 'CELLULAR RESPONSE' named entity 'AFFECTED' named entity 'SIGNALS' named entity 'CAND1' named entity 'ROLE' named entity 'PROCESSING' named entity 'EPSTEIN-BARR VIRUS' named entity 'TARGETING' named entity 'INFECTED' named entity 'POINTING' named entity 'AFFECT' named entity 'UBIQUITIN' named entity 'UNRECOGNIZED' named entity 'USING' named entity 'CYSTEINE PROTEASES' named entity 'N-TERMINAL ' named entity 'PREVIOUSLY' named entity 'INACTIVATION' named entity 'INHIBITION' named entity 'LARGE' named entity 'ACCUMULATION' named entity 'NUCLEUS' named entity 'OF FREE' named entity 'CASPASE-1' named entity 'REVERSED' named entity 'PROTEIN ' named entity 'EFFICIENT' named entity 'VIRUS' named entity 'RESPONSE TO' named entity 'NUCLEAR' named entity 'CONJUGATION' named entity 'INDUCTION' named entity 'N-TERMINUS' named entity 'DANGER' named entity 'EPSTEIN-BARR VIRUS' named entity 'MODEL' named entity 'FOUND' named entity 'LEVEL' named entity 'EBV REACTIVATION' named entity 'BINDING' named entity 'ACTIVITIES' named entity 'TARGETING'

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