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Interaction of Plasmodium falciparum apicortin with α- and β-tubulin is critical for parasite growth and survival
Cytoskeletal structures of Apicomplexan parasites are important for parasite replication, motility, invasion to the host cell and survival. Apicortin, an Apicomplexan specific protein appears to be a crucial factor in maintaining stability of the parasite cytoskeletal assemblies. However, the functi...
Autores principales: | , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7907060/ https://www.ncbi.nlm.nih.gov/pubmed/33633135 http://dx.doi.org/10.1038/s41598-021-83513-5 |
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author | Chakrabarti, Malabika Joshi, Nishant Kumari, Geeta Singh, Preeti Shoaib, Rumaisha Munjal, Akshay Kumar, Vikash Behl, Ankita Abid, Mohammad Garg, Swati Gupta, Sonal Singh, Shailja |
author_facet | Chakrabarti, Malabika Joshi, Nishant Kumari, Geeta Singh, Preeti Shoaib, Rumaisha Munjal, Akshay Kumar, Vikash Behl, Ankita Abid, Mohammad Garg, Swati Gupta, Sonal Singh, Shailja |
author_sort | Chakrabarti, Malabika |
collection | PubMed |
description | Cytoskeletal structures of Apicomplexan parasites are important for parasite replication, motility, invasion to the host cell and survival. Apicortin, an Apicomplexan specific protein appears to be a crucial factor in maintaining stability of the parasite cytoskeletal assemblies. However, the function of apicortin, in terms of interaction with microtubules still remains elusive. Herein, we have attempted to elucidate the function of Plasmodium falciparum apicortin by monitoring its interaction with two main components of parasite microtubular structure, α-tubulin-I and β-tubulin through in silico and in vitro studies. Further, a p25 domain binding generic drug Tamoxifen (TMX), was used to disrupt PfApicortin-tubulin interactions which led to the inhibition in growth and progression of blood stage life cycle of P. falciparum. |
format | Online Article Text |
id | pubmed-7907060 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-79070602021-02-26 Interaction of Plasmodium falciparum apicortin with α- and β-tubulin is critical for parasite growth and survival Chakrabarti, Malabika Joshi, Nishant Kumari, Geeta Singh, Preeti Shoaib, Rumaisha Munjal, Akshay Kumar, Vikash Behl, Ankita Abid, Mohammad Garg, Swati Gupta, Sonal Singh, Shailja Sci Rep Article Cytoskeletal structures of Apicomplexan parasites are important for parasite replication, motility, invasion to the host cell and survival. Apicortin, an Apicomplexan specific protein appears to be a crucial factor in maintaining stability of the parasite cytoskeletal assemblies. However, the function of apicortin, in terms of interaction with microtubules still remains elusive. Herein, we have attempted to elucidate the function of Plasmodium falciparum apicortin by monitoring its interaction with two main components of parasite microtubular structure, α-tubulin-I and β-tubulin through in silico and in vitro studies. Further, a p25 domain binding generic drug Tamoxifen (TMX), was used to disrupt PfApicortin-tubulin interactions which led to the inhibition in growth and progression of blood stage life cycle of P. falciparum. Nature Publishing Group UK 2021-02-25 /pmc/articles/PMC7907060/ /pubmed/33633135 http://dx.doi.org/10.1038/s41598-021-83513-5 Text en © The Author(s) 2021 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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Chakrabarti, Malabika Joshi, Nishant Kumari, Geeta Singh, Preeti Shoaib, Rumaisha Munjal, Akshay Kumar, Vikash Behl, Ankita Abid, Mohammad Garg, Swati Gupta, Sonal Singh, Shailja Interaction of Plasmodium falciparum apicortin with α- and β-tubulin is critical for parasite growth and survival |
title | Interaction of Plasmodium falciparum apicortin with α- and β-tubulin is critical for parasite growth and survival |
title_full | Interaction of Plasmodium falciparum apicortin with α- and β-tubulin is critical for parasite growth and survival |
title_fullStr | Interaction of Plasmodium falciparum apicortin with α- and β-tubulin is critical for parasite growth and survival |
title_full_unstemmed | Interaction of Plasmodium falciparum apicortin with α- and β-tubulin is critical for parasite growth and survival |
title_short | Interaction of Plasmodium falciparum apicortin with α- and β-tubulin is critical for parasite growth and survival |
title_sort | interaction of plasmodium falciparum apicortin with α- and β-tubulin is critical for parasite growth and survival |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7907060/ https://www.ncbi.nlm.nih.gov/pubmed/33633135 http://dx.doi.org/10.1038/s41598-021-83513-5 |
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