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Structural and Functional Aspects of Ebola Virus Proteins
Ebola virus (EBOV), member of genus Ebolavirus, family Filoviridae, have a non-segmented, single-stranded RNA that contains seven genes: (a) nucleoprotein (NP), (b) viral protein 35 (VP35), (c) VP40, (d) glycoprotein (GP), (e) VP30, (f) VP24, and (g) RNA polymerase (L). All genes encode for one prot...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8538763/ https://www.ncbi.nlm.nih.gov/pubmed/34684279 http://dx.doi.org/10.3390/pathogens10101330 |
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author | Jain, Sahil Martynova, Ekaterina Rizvanov, Albert Khaiboullina, Svetlana Baranwal, Manoj |
author_facet | Jain, Sahil Martynova, Ekaterina Rizvanov, Albert Khaiboullina, Svetlana Baranwal, Manoj |
author_sort | Jain, Sahil |
collection | PubMed |
description | Ebola virus (EBOV), member of genus Ebolavirus, family Filoviridae, have a non-segmented, single-stranded RNA that contains seven genes: (a) nucleoprotein (NP), (b) viral protein 35 (VP35), (c) VP40, (d) glycoprotein (GP), (e) VP30, (f) VP24, and (g) RNA polymerase (L). All genes encode for one protein each except GP, producing three pre-proteins due to the transcriptional editing. These pre-proteins are translated into four products, namely: (a) soluble secreted glycoprotein (sGP), (b) Δ-peptide, (c) full-length transmembrane spike glycoprotein (GP), and (d) soluble small secreted glycoprotein (ssGP). Further, shed GP is released from infected cells due to cleavage of GP by tumor necrosis factor α-converting enzyme (TACE). This review presents a detailed discussion on various functional aspects of all EBOV proteins and their residues. An introduction to ebolaviruses and their life cycle is also provided for clarity of the available analysis. We believe that this review will help understand the roles played by different EBOV proteins in the pathogenesis of the disease. It will help in targeting significant protein residues for therapeutic and multi-protein/peptide vaccine development. |
format | Online Article Text |
id | pubmed-8538763 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-85387632021-10-24 Structural and Functional Aspects of Ebola Virus Proteins Jain, Sahil Martynova, Ekaterina Rizvanov, Albert Khaiboullina, Svetlana Baranwal, Manoj Pathogens Review Ebola virus (EBOV), member of genus Ebolavirus, family Filoviridae, have a non-segmented, single-stranded RNA that contains seven genes: (a) nucleoprotein (NP), (b) viral protein 35 (VP35), (c) VP40, (d) glycoprotein (GP), (e) VP30, (f) VP24, and (g) RNA polymerase (L). All genes encode for one protein each except GP, producing three pre-proteins due to the transcriptional editing. These pre-proteins are translated into four products, namely: (a) soluble secreted glycoprotein (sGP), (b) Δ-peptide, (c) full-length transmembrane spike glycoprotein (GP), and (d) soluble small secreted glycoprotein (ssGP). Further, shed GP is released from infected cells due to cleavage of GP by tumor necrosis factor α-converting enzyme (TACE). This review presents a detailed discussion on various functional aspects of all EBOV proteins and their residues. An introduction to ebolaviruses and their life cycle is also provided for clarity of the available analysis. We believe that this review will help understand the roles played by different EBOV proteins in the pathogenesis of the disease. It will help in targeting significant protein residues for therapeutic and multi-protein/peptide vaccine development. MDPI 2021-10-15 /pmc/articles/PMC8538763/ /pubmed/34684279 http://dx.doi.org/10.3390/pathogens10101330 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Jain, Sahil Martynova, Ekaterina Rizvanov, Albert Khaiboullina, Svetlana Baranwal, Manoj Structural and Functional Aspects of Ebola Virus Proteins |
title | Structural and Functional Aspects of Ebola Virus Proteins |
title_full | Structural and Functional Aspects of Ebola Virus Proteins |
title_fullStr | Structural and Functional Aspects of Ebola Virus Proteins |
title_full_unstemmed | Structural and Functional Aspects of Ebola Virus Proteins |
title_short | Structural and Functional Aspects of Ebola Virus Proteins |
title_sort | structural and functional aspects of ebola virus proteins |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8538763/ https://www.ncbi.nlm.nih.gov/pubmed/34684279 http://dx.doi.org/10.3390/pathogens10101330 |
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