Understanding Hepatitis E Viruses by exploring the structural and functional properties of ORF4

Hepatitis E virus (HEV) belongs to the family Hepeviridae and is the major cause of hepatitis E infections across the globe. Recently, a novel viral protein of HEV, named as open reading frame (ORF4), has been associated with its replication in genotype 1 isolates. However, much information regardin...

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Autores principales: Zoya Shafat, Ayesha Tazeen, Murshad Ahmed, et al.
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Publicado: International Academy of Ecology and Environmental Sciences 2021
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spelling oai:doaj.org-article:665096b3b9ff4a1b8dc275270a6282e22021-11-17T03:38:26ZUnderstanding Hepatitis E Viruses by exploring the structural and functional properties of ORF42220-8879https://doaj.org/article/665096b3b9ff4a1b8dc275270a6282e22021-12-01T00:00:00Zhttp://www.iaees.org/publications/journals/nb/articles/2021-11(4)/structural-and-functional-properties-of-ORF4-Hepatitis-virus.pdfhttps://doaj.org/toc/2220-8879Hepatitis E virus (HEV) belongs to the family Hepeviridae and is the major cause of hepatitis E infections across the globe. Recently, a novel viral protein of HEV, named as open reading frame (ORF4), has been associated with its replication in genotype 1 isolates. However, much information regarding ORF4 has not been explored. Thus, the study was conceptualized to explore the structural and functional features of HEV ORF4 protein to better understand the possible molecular mechanisms. The detailed investigation of the ORF4 was carried out in terms of its physicochemical properties, secondary and tertiary structure predictions and functional analysis using different bioinformatics tools. The in silico analyses revealed that ORF4 sequences were enriched in Serine, Proline and Glycine amino acid residues suggesting the prevalence of disordered residues. The protein was found to be thermostable, unstable and highly hydrophobic. The structural analysis showed the presence of cleft, tunnel and pore suggesting their participation in interaction with other molecules. Moreover, identification of several modified sites in ORF4 sequences such as glycosylation, phosphorylation and myristoylation sequences suggest their involvement in cellular signaling pathways and biological processes. Thus, taken together, it can be interpreted that HEV ORF4 possesses significant enormous flexibility due to the presence of Serine, Glycine and Proline amino acids, which suggest its involvement in protein-protein interaction. Furthermore, the presence of motifs, clefts and tunnels also strengthens our analysis, suggesting the commitment of ORF4 towards interaction with other target molecules. Thus, it could be potent drug-targets.Zoya ShafatAyesha TazeenMurshad Ahmed, et al.International Academy of Ecology and Environmental Sciencesarticlehepatitis e virusopen reading frame (orf4)physicochemical parametersstructural analysisfunctional analysisBiology (General)QH301-705.5ENNetwork Biology, Vol 11, Iss 4, Pp 277-294 (2021)
institution DOAJ
collection DOAJ
language EN
topic hepatitis e virus
open reading frame (orf4)
physicochemical parameters
structural analysis
functional analysis
Biology (General)
QH301-705.5
spellingShingle hepatitis e virus
open reading frame (orf4)
physicochemical parameters
structural analysis
functional analysis
Biology (General)
QH301-705.5
Zoya Shafat
Ayesha Tazeen
Murshad Ahmed, et al.
Understanding Hepatitis E Viruses by exploring the structural and functional properties of ORF4
description Hepatitis E virus (HEV) belongs to the family Hepeviridae and is the major cause of hepatitis E infections across the globe. Recently, a novel viral protein of HEV, named as open reading frame (ORF4), has been associated with its replication in genotype 1 isolates. However, much information regarding ORF4 has not been explored. Thus, the study was conceptualized to explore the structural and functional features of HEV ORF4 protein to better understand the possible molecular mechanisms. The detailed investigation of the ORF4 was carried out in terms of its physicochemical properties, secondary and tertiary structure predictions and functional analysis using different bioinformatics tools. The in silico analyses revealed that ORF4 sequences were enriched in Serine, Proline and Glycine amino acid residues suggesting the prevalence of disordered residues. The protein was found to be thermostable, unstable and highly hydrophobic. The structural analysis showed the presence of cleft, tunnel and pore suggesting their participation in interaction with other molecules. Moreover, identification of several modified sites in ORF4 sequences such as glycosylation, phosphorylation and myristoylation sequences suggest their involvement in cellular signaling pathways and biological processes. Thus, taken together, it can be interpreted that HEV ORF4 possesses significant enormous flexibility due to the presence of Serine, Glycine and Proline amino acids, which suggest its involvement in protein-protein interaction. Furthermore, the presence of motifs, clefts and tunnels also strengthens our analysis, suggesting the commitment of ORF4 towards interaction with other target molecules. Thus, it could be potent drug-targets.
format article
author Zoya Shafat
Ayesha Tazeen
Murshad Ahmed, et al.
author_facet Zoya Shafat
Ayesha Tazeen
Murshad Ahmed, et al.
author_sort Zoya Shafat
title Understanding Hepatitis E Viruses by exploring the structural and functional properties of ORF4
title_short Understanding Hepatitis E Viruses by exploring the structural and functional properties of ORF4
title_full Understanding Hepatitis E Viruses by exploring the structural and functional properties of ORF4
title_fullStr Understanding Hepatitis E Viruses by exploring the structural and functional properties of ORF4
title_full_unstemmed Understanding Hepatitis E Viruses by exploring the structural and functional properties of ORF4
title_sort understanding hepatitis e viruses by exploring the structural and functional properties of orf4
publisher International Academy of Ecology and Environmental Sciences
publishDate 2021
url https://doaj.org/article/665096b3b9ff4a1b8dc275270a6282e2
work_keys_str_mv AT zoyashafat understandinghepatitisevirusesbyexploringthestructuralandfunctionalpropertiesoforf4
AT ayeshatazeen understandinghepatitisevirusesbyexploringthestructuralandfunctionalpropertiesoforf4
AT murshadahmedetal understandinghepatitisevirusesbyexploringthestructuralandfunctionalpropertiesoforf4
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