Structural and molecular biology of hepatitis E virus

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dc.contributor.authorWang, Boen
dc.contributor.authorMeng, Xiang-Jinen
dc.contributor.departmentCenter for Emerging, Zoonotic, and Arthropod-borne Pathogensen
dc.contributor.departmentBiomedical Sciences and Pathobiologyen
dc.date.accessioned2021-08-25T16:17:35Zen
dc.date.available2021-08-25T16:17:35Zen
dc.date.issued2021-01-01en
dc.date.updated2021-08-25T16:17:31Zen
dc.description.abstractHepatitis E virus (HEV) is one of the most common causes of acute viral hepatitis, mainly transmitted by fecal-oral route but has also been linked to fulminant hepatic failure, chronic hepatitis, and extrahepatic neurological and renal diseases. HEV is an emerging zoonotic pathogen with a broad host range, and strains of HEV from numerous animal species are known to cross species barriers and infect humans. HEV is a single-stranded, positive-sense RNA virus in the family Hepeviridae. The genome typically contains three open reading frames (ORFs): ORF1 encodes a nonstructural polyprotein for virus replication and transcription, ORF2 encodes the capsid protein that elicits neutralizing antibodies, and ORF3, which partially overlaps ORF2, encodes a multifunctional protein involved in virion morphogenesis and pathogenesis. HEV virions are non-enveloped spherical particles in feces but exist as quasi-enveloped particles in circulating blood. Two types of HEV virus-like particles (VLPs), small T = 1 (270 Å) and native virion-sized T = 3 (320–340 Å) have been reported. There exist two distinct forms of capsid protein, the secreted form (ORF2S) inhibits antibody neutralization, whereas the capsid-associated form (ORF2C) self-assembles to VLPs. Four cis-reactive elements (CREs) containing stem-loops from secondary RNA structures have been identified in the non-coding regions and are critical for virus replication. This mini-review discusses the current knowledge and gaps regarding the structural and molecular biology of HEV with emphasis on the virion structure, genomic organization, secondary RNA structures, viral proteins and their functions, and life cycle of HEV.en
dc.description.versionPublished versionen
dc.format.extentPages 1907-1916en
dc.format.mimetypeapplication/pdfen
dc.identifier.doihttps://doi.org/10.1016/j.csbj.2021.03.038en
dc.identifier.eissn2001-0370en
dc.identifier.issn2001-0370en
dc.identifier.orcidMeng, Xiang-Jin [0000-0002-2739-1334]en
dc.identifier.otherPMC8079827en
dc.identifier.otherS2001-0370(21)00115-X (PII)en
dc.identifier.pmid33995894en
dc.identifier.urihttp://hdl.handle.net/10919/104708en
dc.identifier.volume19en
dc.language.isoenen
dc.publisherElsevieren
dc.relation.urihttps://www.ncbi.nlm.nih.gov/pubmed/33995894en
dc.rightsCreative Commons Attribution 4.0 Internationalen
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/en
dc.subjectGenetic Diversityen
dc.subjectGenomic organizationen
dc.subjectHepatitis E Virus (HEV)en
dc.subjectLife cycle of HEVen
dc.subjectProteins and functionsen
dc.subjectVirion structureen
dc.subject0103 Numerical and Computational Mathematicsen
dc.subject0802 Computation Theory and Mathematicsen
dc.titleStructural and molecular biology of hepatitis E virusen
dc.title.serialComputational and Structural Biotechnology Journalen
dc.typeArticle - Refereeden
dc.type.dcmitypeTexten
dc.type.otherJournalen
dcterms.dateAccepted2021-03-29en
pubs.organisational-group/Virginia Techen
pubs.organisational-group/Virginia Tech/Veterinary Medicineen
pubs.organisational-group/Virginia Tech/Veterinary Medicine/Biomedical Sciences and Pathobiologyen
pubs.organisational-group/Virginia Tech/University Distinguished Professorsen
pubs.organisational-group/Virginia Tech/University Research Institutesen
pubs.organisational-group/Virginia Tech/University Research Institutes/Fralin Life Sciencesen
pubs.organisational-group/Virginia Tech/Faculty of Health Sciencesen
pubs.organisational-group/Virginia Tech/All T&R Facultyen
pubs.organisational-group/Virginia Tech/Veterinary Medicine/CVM T&R Facultyen
pubs.organisational-group/Virginia Tech/University Research Institutes/Fralin Life Sciences/Durelle Scotten

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