Structure and flexibility of non-structural proteins 3 and -5 of Dengue- and Zika viruses in solution
Dengue- (DENV) and Zika viruses (ZIKV) rely on their non-structural protein 5 (NS5) including a methyl-transferase (MTase) and a RNA-dependent RNA polymerase (RdRp) for capping and synthesis of the viral RNA, and the non-structural protein 3 (NS3) with its protease and helicase domain for polyprotei...
| Main Authors: | , , , , |
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| Format: | Journal Article |
| Language: | English |
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2020
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| Online Access: | https://hdl.handle.net/10356/144510 |
| _version_ | 1811691033300303872 |
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| author | Saw, Wuan Geok Pan, Ankita Manimekalai, Malathy Sony Subramanian Grüber, Ardina Grüber, Gerhard |
| author2 | School of Biological Sciences |
| author_facet | School of Biological Sciences Saw, Wuan Geok Pan, Ankita Manimekalai, Malathy Sony Subramanian Grüber, Ardina Grüber, Gerhard |
| author_sort | Saw, Wuan Geok |
| collection | NTU |
| description | Dengue- (DENV) and Zika viruses (ZIKV) rely on their non-structural protein 5 (NS5) including a methyl-transferase (MTase) and a RNA-dependent RNA polymerase (RdRp) for capping and synthesis of the viral RNA, and the non-structural protein 3 (NS3) with its protease and helicase domain for polyprotein possessing, unwinding dsRNA proceeding replication, and NTPase/RTPase activities. Accumulation of data for DENV- and ZIKV NS3 and NS5 in solution during recent years provides information about their overall shape, substrate-induced alterations, oligomeric forms and flexibility, with the latter being essential for domain-domain crosstalk. The importance and differences of the linker regions that connect the two domains of NS3 or NS5 are highlighted in particular with respect to the different DENV serotypes (DENV-1 to −4) as well as to the sequence diversities between the DENV and ZIKV proteins. Novel mutants of the French Polynesia ZIKV NS3 linker presented, identify critical residues in protein stability and enzymatic activity. |
| first_indexed | 2024-10-01T06:13:27Z |
| format | Journal Article |
| id | ntu-10356/144510 |
| institution | Nanyang Technological University |
| language | English |
| last_indexed | 2024-10-01T06:13:27Z |
| publishDate | 2020 |
| record_format | dspace |
| spelling | ntu-10356/1445102023-02-28T17:00:11Z Structure and flexibility of non-structural proteins 3 and -5 of Dengue- and Zika viruses in solution Saw, Wuan Geok Pan, Ankita Manimekalai, Malathy Sony Subramanian Grüber, Ardina Grüber, Gerhard School of Biological Sciences Science::Biological sciences Flavivirus Dengue Dengue- (DENV) and Zika viruses (ZIKV) rely on their non-structural protein 5 (NS5) including a methyl-transferase (MTase) and a RNA-dependent RNA polymerase (RdRp) for capping and synthesis of the viral RNA, and the non-structural protein 3 (NS3) with its protease and helicase domain for polyprotein possessing, unwinding dsRNA proceeding replication, and NTPase/RTPase activities. Accumulation of data for DENV- and ZIKV NS3 and NS5 in solution during recent years provides information about their overall shape, substrate-induced alterations, oligomeric forms and flexibility, with the latter being essential for domain-domain crosstalk. The importance and differences of the linker regions that connect the two domains of NS3 or NS5 are highlighted in particular with respect to the different DENV serotypes (DENV-1 to −4) as well as to the sequence diversities between the DENV and ZIKV proteins. Novel mutants of the French Polynesia ZIKV NS3 linker presented, identify critical residues in protein stability and enzymatic activity. Ministry of Education (MOE) Accepted version This work as well as the research scholarship of Ankita Pan was supported by the Ministry of Education MOE Tier 3 (MOE2012-T3- 1-008), Singapore to G.G. 2020-11-10T06:57:56Z 2020-11-10T06:57:56Z 2018 Journal Article Saw, W. G., Pan, A., Manimekalai, M. S. S., Grüber, A., & Grüber, G. (2019). Structure and flexibility of non-structural proteins 3 and -5 of Dengue- and Zika viruses in solution. Progress in Biophysics and Molecular Biology, 143, 67-77. doi:10.1016/j.pbiomolbio.2018.08.008 0079-6107 https://hdl.handle.net/10356/144510 10.1016/j.pbiomolbio.2018.08.008 30171868 143 67 77 en Progress in Biophysics and Molecular Biology © 2018 Elsevier Ltd. All rights reserved. This paper was published in Progress in Biophysics and Molecular Biology and is made available with permission of Elsevier Ltd. application/pdf |
| spellingShingle | Science::Biological sciences Flavivirus Dengue Saw, Wuan Geok Pan, Ankita Manimekalai, Malathy Sony Subramanian Grüber, Ardina Grüber, Gerhard Structure and flexibility of non-structural proteins 3 and -5 of Dengue- and Zika viruses in solution |
| title | Structure and flexibility of non-structural proteins 3 and -5 of Dengue- and Zika viruses in solution |
| title_full | Structure and flexibility of non-structural proteins 3 and -5 of Dengue- and Zika viruses in solution |
| title_fullStr | Structure and flexibility of non-structural proteins 3 and -5 of Dengue- and Zika viruses in solution |
| title_full_unstemmed | Structure and flexibility of non-structural proteins 3 and -5 of Dengue- and Zika viruses in solution |
| title_short | Structure and flexibility of non-structural proteins 3 and -5 of Dengue- and Zika viruses in solution |
| title_sort | structure and flexibility of non structural proteins 3 and 5 of dengue and zika viruses in solution |
| topic | Science::Biological sciences Flavivirus Dengue |
| url | https://hdl.handle.net/10356/144510 |
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