Comparative Analysis of NS5 Protein for Tick Borne Encephalitis Virus Strains in three Virus Subtypes

Non-structural protein 5 (NS5) of tick-borne encephalitis virus is an enzyme which is responsible for a copying of viral RNA, and it has a strong structural similarity to RNA polymerases of another RNA virus families. The strains of the virus are separated into three subtypes, which differ by specif...

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Autores principales: U. V. Potapova, S. I. Feranchuk, S. I. Belikov, G. N. Leonova
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Lenguaje:RU
Publicado: Scientific Сentre for Family Health and Human Reproduction Problems 2019
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Acceso en línea:https://doaj.org/article/50ad1233e0ae4500a2a372cb2b8c952f
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spelling oai:doaj.org-article:50ad1233e0ae4500a2a372cb2b8c952f2021-11-23T06:14:41ZComparative Analysis of NS5 Protein for Tick Borne Encephalitis Virus Strains in three Virus Subtypes2541-94202587-959610.29413/ABS.2018-3.6.5https://doaj.org/article/50ad1233e0ae4500a2a372cb2b8c952f2019-01-01T00:00:00Zhttps://www.actabiomedica.ru/jour/article/view/1879https://doaj.org/toc/2541-9420https://doaj.org/toc/2587-9596Non-structural protein 5 (NS5) of tick-borne encephalitis virus is an enzyme which is responsible for a copying of viral RNA, and it has a strong structural similarity to RNA polymerases of another RNA virus families. The strains of the virus are separated into three subtypes, which differ by specific mutations in virus proteins, including NS5 protein. The methods of structural bioinformatics allow to construct a model of NS5 protein for several strains of the virus.The paper presents the comparative analysis of sequences and structures of NS5 protein, for three subtypes of the tick-borne encephalitis virus. The segments of protein were identified where the highest difference between subtypes and within subtypes is observed. These segments, where most of the mutations are accumulated, are located in methyltransferase domain, in the inter-domain interface, and in the three subdomains of polymerase domain. The association between the locations of mutations in NS5 protein and the flexibility of a protein backbone was observed using normal mode analysis. Namely, the most important mutations are located in the parts of protein where the amplitude of synchronous oscillations estimated using normal mode analysis is the highest: in the second zinc binding pocket within polymerase domain, in the N-terminal extension within inter-domain interface, and around an active site of methyltransferase domain.U. V. PotapovaS. I. FeranchukS. I. BelikovG. N. LeonovaScientific Сentre for Family Health and Human Reproduction Problemsarticlesubtypes of tick-borne encephalitis virusens5 proteinprotein structureScienceQRUActa Biomedica Scientifica, Vol 3, Iss 6, Pp 36-47 (2019)
institution DOAJ
collection DOAJ
language RU
topic subtypes of tick-borne encephalitis viruse
ns5 protein
protein structure
Science
Q
spellingShingle subtypes of tick-borne encephalitis viruse
ns5 protein
protein structure
Science
Q
U. V. Potapova
S. I. Feranchuk
S. I. Belikov
G. N. Leonova
Comparative Analysis of NS5 Protein for Tick Borne Encephalitis Virus Strains in three Virus Subtypes
description Non-structural protein 5 (NS5) of tick-borne encephalitis virus is an enzyme which is responsible for a copying of viral RNA, and it has a strong structural similarity to RNA polymerases of another RNA virus families. The strains of the virus are separated into three subtypes, which differ by specific mutations in virus proteins, including NS5 protein. The methods of structural bioinformatics allow to construct a model of NS5 protein for several strains of the virus.The paper presents the comparative analysis of sequences and structures of NS5 protein, for three subtypes of the tick-borne encephalitis virus. The segments of protein were identified where the highest difference between subtypes and within subtypes is observed. These segments, where most of the mutations are accumulated, are located in methyltransferase domain, in the inter-domain interface, and in the three subdomains of polymerase domain. The association between the locations of mutations in NS5 protein and the flexibility of a protein backbone was observed using normal mode analysis. Namely, the most important mutations are located in the parts of protein where the amplitude of synchronous oscillations estimated using normal mode analysis is the highest: in the second zinc binding pocket within polymerase domain, in the N-terminal extension within inter-domain interface, and around an active site of methyltransferase domain.
format article
author U. V. Potapova
S. I. Feranchuk
S. I. Belikov
G. N. Leonova
author_facet U. V. Potapova
S. I. Feranchuk
S. I. Belikov
G. N. Leonova
author_sort U. V. Potapova
title Comparative Analysis of NS5 Protein for Tick Borne Encephalitis Virus Strains in three Virus Subtypes
title_short Comparative Analysis of NS5 Protein for Tick Borne Encephalitis Virus Strains in three Virus Subtypes
title_full Comparative Analysis of NS5 Protein for Tick Borne Encephalitis Virus Strains in three Virus Subtypes
title_fullStr Comparative Analysis of NS5 Protein for Tick Borne Encephalitis Virus Strains in three Virus Subtypes
title_full_unstemmed Comparative Analysis of NS5 Protein for Tick Borne Encephalitis Virus Strains in three Virus Subtypes
title_sort comparative analysis of ns5 protein for tick borne encephalitis virus strains in three virus subtypes
publisher Scientific Сentre for Family Health and Human Reproduction Problems
publishDate 2019
url https://doaj.org/article/50ad1233e0ae4500a2a372cb2b8c952f
work_keys_str_mv AT uvpotapova comparativeanalysisofns5proteinfortickborneencephalitisvirusstrainsinthreevirussubtypes
AT siferanchuk comparativeanalysisofns5proteinfortickborneencephalitisvirusstrainsinthreevirussubtypes
AT sibelikov comparativeanalysisofns5proteinfortickborneencephalitisvirusstrainsinthreevirussubtypes
AT gnleonova comparativeanalysisofns5proteinfortickborneencephalitisvirusstrainsinthreevirussubtypes
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