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Plasmodium falciparum specific helicase 2 is a dual, bipolar helicase and is crucial for parasite growth
Human malaria infection is a major challenge across the globe and is responsible for millions of deaths annually. Rapidly emerging drug resistant strains against the new class of anti-malarial drugs are major threat to control the disease burden worldwide. Helicases are present in every organism and...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6365506/ https://www.ncbi.nlm.nih.gov/pubmed/30728406 http://dx.doi.org/10.1038/s41598-018-38032-1 |
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author | Chauhan, Manish Tuteja, Renu |
author_facet | Chauhan, Manish Tuteja, Renu |
author_sort | Chauhan, Manish |
collection | PubMed |
description | Human malaria infection is a major challenge across the globe and is responsible for millions of deaths annually. Rapidly emerging drug resistant strains against the new class of anti-malarial drugs are major threat to control the disease burden worldwide. Helicases are present in every organism and have important role in various nucleic acid metabolic processes. Previously we have reported the presence of three parasite specific helicases (PSH) in Plasmodium falciparum 3D7 strain. Here we present the detailed biochemical characterization of PfPSH2. PfPSH2 is DNA and RNA stimulated ATPase and is able to unwind partially duplex DNA and RNA substrates. It can translocate in both 3′ to 5′ and 5′ to 3′ directions. PfPSH2 is expressed in all the stages of intraerythrocytic development and it is localized in cytoplasm in P. falciparum 3D7 strain. The dsRNA mediated inhibition study suggests that PfPSH2 is important for the growth and survival of the parasite. This study presents the detailed characterization of PfPSH2 and lays the foundation for future development of PfPSH2 as drug target. |
format | Online Article Text |
id | pubmed-6365506 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-63655062019-02-08 Plasmodium falciparum specific helicase 2 is a dual, bipolar helicase and is crucial for parasite growth Chauhan, Manish Tuteja, Renu Sci Rep Article Human malaria infection is a major challenge across the globe and is responsible for millions of deaths annually. Rapidly emerging drug resistant strains against the new class of anti-malarial drugs are major threat to control the disease burden worldwide. Helicases are present in every organism and have important role in various nucleic acid metabolic processes. Previously we have reported the presence of three parasite specific helicases (PSH) in Plasmodium falciparum 3D7 strain. Here we present the detailed biochemical characterization of PfPSH2. PfPSH2 is DNA and RNA stimulated ATPase and is able to unwind partially duplex DNA and RNA substrates. It can translocate in both 3′ to 5′ and 5′ to 3′ directions. PfPSH2 is expressed in all the stages of intraerythrocytic development and it is localized in cytoplasm in P. falciparum 3D7 strain. The dsRNA mediated inhibition study suggests that PfPSH2 is important for the growth and survival of the parasite. This study presents the detailed characterization of PfPSH2 and lays the foundation for future development of PfPSH2 as drug target. Nature Publishing Group UK 2019-02-06 /pmc/articles/PMC6365506/ /pubmed/30728406 http://dx.doi.org/10.1038/s41598-018-38032-1 Text en © The Author(s) 2019 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Chauhan, Manish Tuteja, Renu Plasmodium falciparum specific helicase 2 is a dual, bipolar helicase and is crucial for parasite growth |
title | Plasmodium falciparum specific helicase 2 is a dual, bipolar helicase and is crucial for parasite growth |
title_full | Plasmodium falciparum specific helicase 2 is a dual, bipolar helicase and is crucial for parasite growth |
title_fullStr | Plasmodium falciparum specific helicase 2 is a dual, bipolar helicase and is crucial for parasite growth |
title_full_unstemmed | Plasmodium falciparum specific helicase 2 is a dual, bipolar helicase and is crucial for parasite growth |
title_short | Plasmodium falciparum specific helicase 2 is a dual, bipolar helicase and is crucial for parasite growth |
title_sort | plasmodium falciparum specific helicase 2 is a dual, bipolar helicase and is crucial for parasite growth |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6365506/ https://www.ncbi.nlm.nih.gov/pubmed/30728406 http://dx.doi.org/10.1038/s41598-018-38032-1 |
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