About: Viperin Targets Flavivirus Virulence by Inducing Assembly of Noninfectious Capsid Particles

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About: Viperin Targets Flavivirus Virulence by Inducing Assembly of Noninfectious Capsid Particles 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
title	Viperin Targets Flavivirus Virulence by Inducing Assembly of Noninfectious Capsid Particles
Creator	Pichlmair, Andreas Hubel, Philipp Lundmark, Richard Nilsson, Emma Pasto, Jenny Upadhyay, Arunkumar Vonderstein, Kirstin Skalman, Larsård
source	Medline; PMC
abstract	Efficient antiviral immunity requires interference with virus replication at multiple layers targeting diverse steps in the viral life cycle. We describe here a novel flavivirus inhibition mechanism that results in interferon-mediated obstruction of tick-borne encephalitis virus particle assembly and involves release of malfunctioning membrane-associated capsid (C) particles. This mechanism is controlled by the activity of the interferon-induced protein viperin, a broad-spectrum antiviral interferon-stimulated gene. Through analysis of the viperin-interactome, we identified the Golgi brefeldin A-resistant guanine nucleotide exchange factor 1 (GBF1) as the cellular protein targeted by viperin. Viperin-induced antiviral activity, as well as C-particle release, was stimulated by GBF1 inhibition and knockdown and reduced by elevated levels of GBF1. Our results suggest that viperin targets flavivirus virulence by inducing the secretion of unproductive noninfectious virus particles via a GBF1-dependent mechanism. This as-yet-undescribed antiviral mechanism allows potential therapeutic intervention. IMPORTANCE The interferon response can target viral infection on almost every level; however, very little is known about the interference of flavivirus assembly. We show here that interferon, through the action of viperin, can disturb the assembly of tick-borne encephalitis virus. The viperin protein is highly induced after viral infection and exhibit broad-spectrum antiviral activity. However, the mechanism of action is still elusive and appears to vary between the different viruses, indicating that cellular targets utilized by several viruses might be involved. In this study, we show that viperin induces capsid particle release by interacting and inhibiting the function of the cellular protein Golgi brefeldin A-resistant guanine nucleotide exchange factor 1 (GBF1). GBF1 is a key protein in the cellular secretory pathway and is essential in the life cycle of many viruses, also targeted by viperin, implicating GBF1 as a novel putative drug target.
has issue date	2017-12-14(xsd:dateTime)
bibo:doi	10.1128/jvi.01751-17
bibo:pmid	29046456
has license	cc-by
sha1sum (hex)	0330ede445d96dd0a27f474f945d6ce2e7085f15
schema:url	https://doi.org/10.1128/jvi.01751-17
resource representing a document's title	Viperin Targets Flavivirus Virulence by Inducing Assembly of Noninfectious Capsid Particles
has PubMed Central identifier	PMC5730767
has PubMed identifier	29046456
schema:publication	J Virol
resource representing a document's body	covid:0330ede445d96dd0a27f474f945d6ce2e7085f15#body_text
is schema:about of	named entity 'ASSEMBLY' named entity 'obstruction' named entity 'guanine nucleotide exchange factor' named entity 'particles' named entity 'release' named entity 'POTENTIAL' named entity 'CAPSID' named entity 'VIRULENCE' named entity 'VIPERIN' named entity 'FLAVIVIRUS' named entity 'ANALYSIS' named entity 'TARGETED' named entity 'HERE' named entity 'DESCRIBE' covid:arg/0330ede445d96dd0a27f474f945d6ce2e7085f15 named entity 'TARGETS' named entity 'INDUCING' named entity 'CAPSID' named entity 'VIRUS PARTICLE ASSEMBLY' named entity 'SPECTRUM' named entity 'IDENTIFIED' named entity 'NONINFECTIOUS' named entity 'INTERFERON' named entity 'PARTICLES' named entity 'PARTICLES' named entity 'TARGETS' named entity 'INDUCING' named entity 'MEMBRANE' named entity 'BREFELDIN A' named entity 'RELEASE' named entity 'MULTIPLE' named entity 'INTERFERENCE' named entity 'MECHANISM' named entity 'EFFICIENT' named entity 'PROTEIN ' named entity 'RESULTS' named entity 'TARGETING' named entity 'LEVELS' named entity 'CONTROLLED BY' named entity 'SECRETION' named entity 'INTERACTOME' named entity 'DEPENDENT' named entity 'GENE' named entity 'VIRUS PARTICLES' named entity 'INDUCED' named entity 'ANTIVIRAL' named entity 'THERAPEUTIC INTERVENTION' named entity 'MEDIATED' named entity 'ELEVATED' named entity 'MALFUNCTIONING' named entity 'RESISTANT' named entity 'INHIBITION' named entity 'UNPRODUCTIVE' named entity 'LAYERS' named entity 'ALLOWS' named entity 'ASSOCIATED' named entity 'VIRULENCE' named entity 'SUGGEST' named entity 'NONINFECTIOUS' named entity 'VIRUS REPLICATION' named entity 'VIPERIN' named entity 'REDUCED' named entity 'OBSTRUCTION' named entity 'DIVERSE' named entity 'GBF1' named entity 'BROAD' named entity 'IMMUNITY' named entity 'STEPS' named entity 'ANTIVIRAL ACTIVITY' named entity 'VIRAL LIFE CYCLE' named entity 'TICK-BORNE ENCEPHALITIS VIRUS' named entity 'GOLGI' named entity 'STIMULATED' named entity 'ACTIVITY'

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