Photosensitized INA-Labelled protein 1 (PhIL1) is novel component of the inner membrane complex and is required for Plasmodium parasite development

Saini, Ekta and Zeeshan, Mohammad and Brady, Declan and Pandey, Rajan and Kaiser, Gesine and Koreny, Ludek and Kumar, Pradeep and Thakur, Vandana and Tatiya, Shreyansh and Katris, Nicholas J. and Limenitakis, Rebecca Stanway and Kaur, Inderjeet and Green, Judith L. and Bottrill, Andrew R. and Guttery, David S. and Waller, Ross F. and Heussler, Volker and Holder, Anthony A. and Mohmmed, Asif and Malhotra, Pawan and Tewari, Rita (2017) Photosensitized INA-Labelled protein 1 (PhIL1) is novel component of the inner membrane complex and is required for Plasmodium parasite development. Scientific Reports, 7 (1). 15577/1-15577/11. ISSN 2045-2322

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Abstract

Plasmodium parasites, the causative agents of malaria, possess a distinctive membranous structure of flattened alveolar vesicles supported by a proteinaceous network, and referred to as the inner membrane complex (IMC). The IMC has a role in actomyosin-mediated motility and host cell invasion. Here, we examine the location, protein interactome and function of PhIL1, an IMC-associated protein on the motile and invasive stages of both human and rodent parasites. We show that PhIL1 is located in the IMC in all three invasive (merozoite, ookinete-, and sporozoite) stages of development, as well as in the male gametocyte and locates both at the apical and basal ends of ookinete and sporozoite stages. Proteins interacting with PhIL1 were identified, showing that PhIL1 was bound to only some proteins present in the glideosome motor complex (GAP50, GAPM1–3) of both P. falciparum and P. berghei. Analysis of PhIL1 function using gene targeting approaches indicated that the protein is required for both asexual and sexual stages of development. In conclusion, we show that PhIL1 is required for development of all zoite stages of Plasmodium and it is part of a novel protein complex with an overall composition overlapping with but different to that of the glideosome.

Item Type: Article
Schools/Departments: University of Nottingham, UK > Faculty of Medicine and Health Sciences > School of Life Sciences
Identification Number: 10.1038/s41598-017-15781-z
Depositing User: Eprints, Support
Date Deposited: 20 Nov 2017 11:31
Last Modified: 20 Nov 2017 22:10
URI: http://eprints.nottingham.ac.uk/id/eprint/48240

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