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

Saini, Ekta; Zeeshan, Mohammad; Brady, Declan; Pandey, Rajan Kumar; Kaiser, Gesine; Kořený, Luděk; Kumar, Pradeep; Thakur, Vandana; Tatiya, Shreyansh; Katris, Nicholas J.; Limenitakis, Rebecca; Kaur, Inderjeet; Green, Judith L.; Bottrill, Andrew R.; Guttery, David S.; Waller, Ross F.; Heussler, Volker; Holder, Anthony A.; Mohmmed, Asif; Malhotra, Pawan; Tewari, Rita

doi:10.1038/s41598-017-15781-z

Cited by 49 publications

(69 citation statements)

References 45 publications

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“…Live cell imaging of transgenic parasite lines was performed at different proliferative stages during the parasite life cycle (Figure 1) as described previously (Roques et al, 2019;Saini et al, 2017) using a Zeiss AxioImager M2 microscope fitted with an AxioCam ICc1 digital camera (Carl Zeiss, Inc).…”

Section: Localization Of Ndc80-gfp Throughout the Parasite Life Cyclementioning

confidence: 99%

Real-time dynamics of Plasmodium NDC80 reveals unusual modes of chromosome segregation during parasite proliferation

Pandey

Zeeshan

Ferguson

et al. 2019

Preprint

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Eukaryotic cell proliferation requires chromosome replication and precise segregation, followed by cell division, to ensure daughter cells have identical genomic copies. The kinetochore is a multi-protein structure assembled on chromosome centromeres, which mediates attachment to spindle microtubules and chromosome segregation during mitosis. Plasmodium spp., the causative agent of malaria, undergoes closed mitosis with an intact nuclear membrane and intranuclear mitotic spindle. However, the regulation of the main events of mitosis and meiosis, including chromosome segregation, is poorly understood in this parasite. In part this is due to a distinct lack of markers for tracking kinetochore dynamics. Since NDC80 is the conserved component of the kinetochore complex, we labelled NDC80 with either a C-terminal GFP or mCherry tag by recombination at the endogenous locus to generate transgenic lines of the rodent malaria parasite Plasmodium berghei. We show that NDC80 is located at a single cluster of all kinetochores and examine its spatio-temporal dynamics throughout all proliferative stages of the parasite life cycle.We also compare the location of NDC80 with that of the kinetochore using electron microscopy. These transgenic parasite lines are a very useful resource to identify and study the kinetochore complex and follow chromosome dynamics during malaria parasite development.

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Section: Localization Of Ndc80-gfp Throughout the Parasite Life Cyclementioning

confidence: 99%

Real-time dynamics of Plasmodium NDC80 reveals unusual modes of chromosome segregation during parasite proliferation

Pandey

Zeeshan

Ferguson

et al. 2019

Preprint

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“…The genes can be classified into 3 major groups relating to motility, cytoadherence and erythrocyte invasion. Genes relating to the glideosome complex [ PF3D7_0918000 (GAP50) (13), PF3D7_1323700 (GAPM1) (14)], the inner membrane complex (15) [ PF3D7_0109000 (PHIL1) and PF3D7_1003600 (IMC1c)] and cytoskeleton (16, 17) [ PF3D7_1251200 (coronin), PF3D7_0932200 (Profilin) and PF3D7_1246200 (Actin 1)] are essential for the parasite to move towards a new red blood cell through gliding motility. Upon reaching the red blood cell, merozoite surface proteins such as PF3D7_1035400 (MSP3), PF3D7_1335100 (MSP7), PF3D7_1035500 (MSP6) (18) and PF3D7_1035700 (DBLMSP) facilitate the binding of the parasite to the red blood cell.…”

Section: Resultsmentioning

confidence: 99%

www.Malaria.tools - comparative genomic and transcriptomic database for Plasmodium species

Tan

Mutwil

2019

Preprint

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10Malaria is a tropical parasitic disease caused by the Plasmodium genus, which resulted in an estimated 11 219 million cases of malaria and 435,000 malaria-related deaths in 2017. Despite the availability of the P. 12 falciparum genome since 2002, almost 50% of the genes remain unannotated. To remedy this paucity of 13 functional information, we used transcriptomic data to build gene co-expression networks for two 14 Plasmodium species (P. falciparum and P. berghei), and included genomic data of four other Plasmodium 15 species, P. yoleii, P. knowlesi, P. vivax and P. cynomolgi, as well as two non-Plasmodium species from 16 the Apicomplexa, Toxoplasma gondii and Theileria parva. The database is preloaded with tools that allow 17 the identification and cross-species comparison of co-expressed gene neighborhoods, clusters, and life 18 stage-specific expression, thus providing sophisticated tools to predict gene function. Moreover, we 19 exemplify how the tools can be used to easily identify genes relevant for pathogenicity and various life 20 stages of the malaria parasite. The database is freely available at https://malaria.tools. 21 22 Orthogroups D Kinesin-8, putative Radial spoke protein 3 Kinesin, putative GAS8-like protein Dynein light chain, putative Kinesin-like protein, putative MORN repeat Dynein light chain, putative Kinesin-8, putative Kinesin-like protein, putative Kinesin, putative

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“…We have previously shown the expression and localization of PhIL1 in the IMC of the P. falciparum parasite and its interaction with some of the components of glideosomal complex (Saini et al, 2017). To investigate the existence of PhIL1-associated novel IMC protein complex in P. falciparum, we selected three proteins: a conserved protein of unknown function (PF3D7_1310700), referred here as PhIL1…”

Section: P Falciparum Alv5 Phip and Gapm2 Proteins Co-localise Withmentioning

confidence: 99%

Unravelling a PhIL1-glideosome associated complex in Plasmodium falciparum merozoite that is essential for invasion in host erythrocytes

Saini¹,

Sheokand²,

Sharma³

et al. 2020

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The human malaria parasite, Plasmodium falciparum possess a unique mechanism of gliding motility guided by glideosome that powers its entry into insect and vertebrate hosts to facilitate its invasion and internalization within the targeted host cell. Photosensitized INA-labelled protein 1 (PhIL1) forms a novel protein complex that is associated with glideosome motor complex in the inner membrane complex of invasive merozoite. To establish the role of PfPhIL1 associated novel complex at asexual blood stages, we characterized three proteins associated with PhIL1: a glideosome associated protein- PfGAPM2, an IMC structural protein- PfALV5 and a previously uncharacterised protein - referred here as PfPhIP (PhIL1 interacting protein). GFP targeting and co-immunoprecipitation analysis confirmed that these proteins are part of a PhIL1 associated novel complex, which co-exists with the glideosomal complex. To know the functional significance of PhIL1 associated complex, transgenic parasites were generated for glmS mediated conditional knock-down of each of the three proteins. Parasites lacking PfPhIP or PfGAPM2 were unable to invade the RBCs. PfPhIP deficient parasites also showed defects in merozoite segmentation. PfPhIP and PfGAPM2 depleted parasites revealed abrogation of reorientation/gliding, although initial attachment with human RBCs was not affected in these knock-down parasites. Together, the data presented here shows that proteins of the PhIL1 associated complex play an important role in orientation of P. falciparum merozoites post initial attachment, which is crucial for formation of tight junction and hence invasion of host erythrocytes.

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

Cited by 49 publications

References 45 publications

Real-time dynamics of Plasmodium NDC80 reveals unusual modes of chromosome segregation during parasite proliferation

Real-time dynamics of Plasmodium NDC80 reveals unusual modes of chromosome segregation during parasite proliferation

www.Malaria.tools - comparative genomic and transcriptomic database for Plasmodium species

Unravelling a PhIL1-glideosome associated complex in Plasmodium falciparum merozoite that is essential for invasion in host erythrocytes

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