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Rhinovirus RNA Polymerase: Structure, Function, and Inhibitors
Human rhinovirus is responsible for causing 50% of common cold infections in infants and adults. It belongs to the picornavirus family of nonenveloped positive-strand RNA viruses. The RNA synthesis of rhinovirus is carried out by RNA-dependent RNA polymerase, also known as 3D(Pol). It catalyzes the...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
2019
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7173612/ http://dx.doi.org/10.1016/B978-0-12-815422-9.00011-5 |
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author | Nirwan, Sonam Kakkar, Rita |
author_facet | Nirwan, Sonam Kakkar, Rita |
author_sort | Nirwan, Sonam |
collection | PubMed |
description | Human rhinovirus is responsible for causing 50% of common cold infections in infants and adults. It belongs to the picornavirus family of nonenveloped positive-strand RNA viruses. The RNA synthesis of rhinovirus is carried out by RNA-dependent RNA polymerase, also known as 3D(Pol). It catalyzes the synthesis of negative-strand RNA using a positive-strand template. The structure of the enzyme consists of three domains: palm, fingers, and thumb domains and Mg(2+) in the active site. These conserved structural features of the enzyme help in catalyzing phosphodiester bond formation between the two consecutive nucleotide units complimentary to the template RNA using a VPg primer. Owing to the presence of over 100 serotypes of the enzyme, designing specific inhibitors targeting the polymerase is a challenging task and until now no clinically approved antirhino viral drug is reported. In this review, we have given detailed information about the structure and function of the enzyme and also discussed some of the inhibitors and their in vivo activity against 3D(Pol). |
format | Online Article Text |
id | pubmed-7173612 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
record_format | MEDLINE/PubMed |
spelling | pubmed-71736122020-04-22 Rhinovirus RNA Polymerase: Structure, Function, and Inhibitors Nirwan, Sonam Kakkar, Rita Viral Polymerases Article Human rhinovirus is responsible for causing 50% of common cold infections in infants and adults. It belongs to the picornavirus family of nonenveloped positive-strand RNA viruses. The RNA synthesis of rhinovirus is carried out by RNA-dependent RNA polymerase, also known as 3D(Pol). It catalyzes the synthesis of negative-strand RNA using a positive-strand template. The structure of the enzyme consists of three domains: palm, fingers, and thumb domains and Mg(2+) in the active site. These conserved structural features of the enzyme help in catalyzing phosphodiester bond formation between the two consecutive nucleotide units complimentary to the template RNA using a VPg primer. Owing to the presence of over 100 serotypes of the enzyme, designing specific inhibitors targeting the polymerase is a challenging task and until now no clinically approved antirhino viral drug is reported. In this review, we have given detailed information about the structure and function of the enzyme and also discussed some of the inhibitors and their in vivo activity against 3D(Pol). 2019 2018-11-02 /pmc/articles/PMC7173612/ http://dx.doi.org/10.1016/B978-0-12-815422-9.00011-5 Text en Copyright © 2019 Elsevier Inc. All rights reserved. Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active. |
spellingShingle | Article Nirwan, Sonam Kakkar, Rita Rhinovirus RNA Polymerase: Structure, Function, and Inhibitors |
title | Rhinovirus RNA Polymerase: Structure, Function, and Inhibitors |
title_full | Rhinovirus RNA Polymerase: Structure, Function, and Inhibitors |
title_fullStr | Rhinovirus RNA Polymerase: Structure, Function, and Inhibitors |
title_full_unstemmed | Rhinovirus RNA Polymerase: Structure, Function, and Inhibitors |
title_short | Rhinovirus RNA Polymerase: Structure, Function, and Inhibitors |
title_sort | rhinovirus rna polymerase: structure, function, and inhibitors |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7173612/ http://dx.doi.org/10.1016/B978-0-12-815422-9.00011-5 |
work_keys_str_mv | AT nirwansonam rhinovirusrnapolymerasestructurefunctionandinhibitors AT kakkarrita rhinovirusrnapolymerasestructurefunctionandinhibitors |