Interaction of Plasmodium falciparum apicortin with α- and β-tubulin is critical for parasite growth and survival

Abstract 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, t...

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Autores principales:	Malabika Chakrabarti, Nishant Joshi, Geeta Kumari, Preeti Singh, Rumaisha Shoaib, Akshay Munjal, Vikash Kumar, Ankita Behl, Mohammad Abid, Swati Garg, Sonal Gupta, Shailja Singh
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/6315647a3e444a20b66d4a6609194ccf
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spelling	oai:doaj.org-article:6315647a3e444a20b66d4a6609194ccf2021-12-02T11:35:52ZInteraction of Plasmodium falciparum apicortin with α- and β-tubulin is critical for parasite growth and survival10.1038/s41598-021-83513-52045-2322https://doaj.org/article/6315647a3e444a20b66d4a6609194ccf2021-02-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-83513-5https://doaj.org/toc/2045-2322Abstract 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.Malabika ChakrabartiNishant JoshiGeeta KumariPreeti SinghRumaisha ShoaibAkshay MunjalVikash KumarAnkita BehlMohammad AbidSwati GargSonal GuptaShailja SinghNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-16 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Malabika Chakrabarti Nishant Joshi Geeta Kumari Preeti Singh Rumaisha Shoaib Akshay Munjal Vikash Kumar Ankita Behl Mohammad Abid Swati Garg Sonal Gupta Shailja Singh Interaction of Plasmodium falciparum apicortin with α- and β-tubulin is critical for parasite growth and survival
description	Abstract 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	article
author	Malabika Chakrabarti Nishant Joshi Geeta Kumari Preeti Singh Rumaisha Shoaib Akshay Munjal Vikash Kumar Ankita Behl Mohammad Abid Swati Garg Sonal Gupta Shailja Singh
author_facet	Malabika Chakrabarti Nishant Joshi Geeta Kumari Preeti Singh Rumaisha Shoaib Akshay Munjal Vikash Kumar Ankita Behl Mohammad Abid Swati Garg Sonal Gupta Shailja Singh
author_sort	Malabika Chakrabarti
title	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_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_sort	interaction of plasmodium falciparum apicortin with α- and β-tubulin is critical for parasite growth and survival
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/6315647a3e444a20b66d4a6609194ccf
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Interaction of Plasmodium falciparum apicortin with α- and β-tubulin is critical for parasite growth and survival

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