About: Host-Virus Protein Interaction Network Reveals the Involvement of Multiple Host Processes in the Life Cycle of Hepatitis E Virus

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: Host-Virus Protein Interaction Network Reveals the Involvement of Multiple Host Processes in the Life Cycle of Hepatitis E 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
title	Host-Virus Protein Interaction Network Reveals the Involvement of Multiple Host Processes in the Life Cycle of Hepatitis E Virus
Creator	Anang, Saumya Kaushik, Nidhi Surjit, Milan Nayak, Baibaswata Subramani, Chandru Pareek, Madhu Saha, Sudipto Srivastava, Akriti Nair, Vidya Ranjith-Kumar, C Ct, Ranjith-Kumar Das Mandal, Sukhen Sd, Mandal Subramani, Citation Vp, Nair
topic	covid:3702eb1540a20656d1f723b180c1a8607c6cb4a6#this
source	PMC
abstract	Comprehensive knowledge of host-pathogen interactions is central to understand the life cycle of a pathogen and devise specific therapeutic strategies. Protein-protein interactions (PPIs) are key mediators of host-pathogen interactions. Hepatitis E virus (HEV) is a major cause of viral hepatitis in humans. Recent reports also demonstrate its extrahepatic manifestations in the brain. Toward understanding the molecular details of HEV life cycle, we screened human liver and fetal brain cDNA libraries to identify the host interaction partners of proteins encoded by genotype 1 HEV and constructed the virus-host PPI network. Analysis of the network indicated a role of HEV proteins in modulating multiple host biological processes such as stress and immune responses, the ubiquitin-proteasome system, energy and iron metabolism, and protein translation. Further investigations revealed the presence of multiple host translation regulatory factors in the viral translation/replication complex. Depletion of host translation factors such as eIF4A2, eIF3A, and RACK1 significantly reduced the viral replication, whereas eIF2AK4 depletion had no effect. These findings highlight the ingenuity of the pathogen in manipulating the host machinery to its own benefit, a clear understanding of which is essential for the identification of strategic targets and development of specific antivirals against HEV. IMPORTANCE Hepatitis E virus (HEV) is a pathogen that is transmitted by the fecal-oral route. Owing to the lack of an efficient laboratory model, the life cycle of the virus is poorly understood. During the course of infection, interactions between the viral and host proteins play essential roles, a clear understanding of which is essential to decode the life cycle of the virus. In this study, we identified the direct host interaction partners of all HEV proteins and generated a PPI network. Our functional analysis of the HEV-human PPI network reveals a role of HEV proteins in modulating multiple host biological processes such as stress and immune responses, the ubiquitin-proteasome system, energy and iron metabolism, and protein translation. Further investigations revealed an essential role of several host factors in HEV replication. Collectively, the results from our study provide a vast resource of PPI data from HEV and its human host and identify the molecular components of the viral translation/replication machinery.
has issue date	2018-01-23(xsd:dateTime)
bibo:doi	10.1128/msystems.00135-17
bibo:pmid	29404423
has license	cc-by
sha1sum (hex)	3702eb1540a20656d1f723b180c1a8607c6cb4a6
schema:url	https://doi.org/10.1128/msystems.00135-17
resource representing a document's title	Host-Virus Protein Interaction Network Reveals the Involvement of Multiple Host Processes in the Life Cycle of Hepatitis E Virus
has PubMed Central identifier	PMC5781259
has PubMed identifier	29404423
schema:publication	mSystems
resource representing a document's body	covid:3702eb1540a20656d1f723b180c1a8607c6cb4a6#body_text
is http://vocab.deri.ie/void#inDataset of	proxy:http/ns.inria.fr/covid19/3702eb1540a20656d1f723b180c1a8607c6cb4a6 https://covidontheweb.inria.fr:4443/about/id/http/ns.inria.fr/covid19/3702eb1540a20656d1f723b180c1a8607c6cb4a6
is schema:about of	named entity 'ANTIVIRALS' named entity 'EIF3A' named entity 'UNDERSTAND' named entity 'HUMANS' named entity 'HEPATITIS E VIRUS' named entity 'STRESS' named entity 'BIOLOGICAL PROCESSES' named entity 'PPI' named entity 'ESSENTIAL' named entity 'MANIPULATING' named entity 'DEPLETION' named entity 'KEY' named entity 'PROTEIN-PROTEIN INTERACTIONS' named entity 'RESULTS' named entity 'INVESTIGATIONS' named entity 'ENCODED' named entity 'REPORTS' named entity 'HOST' named entity 'FETAL BRAIN' named entity 'REVEALED' named entity 'THERAPEUTIC' named entity 'STRATEGIC' named entity 'IRON METABOLISM' named entity 'TRANSMITTED BY' named entity 'PATHOGEN' named entity 'VIRAL REPLICATION' named entity 'EIF2AK4' named entity 'SPECIFIC' named entity 'MULTIPLE' named entity 'VIRAL TRANSLATION' named entity 'REDUCED' named entity 'HEV' named entity 'ROLE' named entity 'PARTNERS' named entity 'RESOURCE' named entity 'MOLECULAR' named entity 'MODEL' named entity 'energy' named entity 'investigations' named entity 'brain' named entity 'Recent' named entity 'factors' named entity 'model' named entity 'study' named entity 'host' named entity 'demonstrate' named entity 'development' named entity 'essential' named entity 'Multiple' named entity 'PROTEIN INTERACTION' covid:arg/3702eb1540a20656d1f723b180c1a8607c6cb4a6 named entity 'IDENTIFIED' named entity 'UNDERSTOOD' named entity 'CAUSE' named entity 'ROLES' named entity 'FINDINGS' named entity 'EIF4A2' named entity 'FUNCTIONAL ANALYSIS' named entity 'UBIQUITIN-PROTEASOME SYSTEM' named entity 'STUDY' named entity 'A MAJOR' named entity 'COMPLEX' named entity 'RECENT' named entity 'ANALYSIS'

Faceted Search & Find service v1.13.91 as of Mar 24 2020

Alternative Linked Data Documents: Sponger | ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3229 as of Jul 10 2020, on Linux (x86_64-pc-linux-gnu), Single-Server Edition (94 GB total memory)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2025 OpenLink Software