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https://doi.org/10.1038/s41598-018-33358-2
Title: | Febrile Temperature Elevates the Expression of Phosphatidylserine on Plasmodium falciparum (FCR3CSA) Infected Red Blood Cell Surface Leading to Increased Cytoadhesion | Authors: | Zhang, R Chandramohanadas, R Lim, C.T Dao, M |
Keywords: | chondroitin sulfate phosphatidylserine animal biosynthesis blood cell adhesion CHO cell line Cricetulus erythrocyte fever genetics human malaria falciparum metabolism parasitology pathogenicity Plasmodium falciparum surface property temperature Animals Cell Adhesion CHO Cells Chondroitin Sulfates Cricetulus Erythrocytes Fever Humans Malaria, Falciparum Phosphatidylserines Plasmodium falciparum Surface Properties Temperature |
Issue Date: | 2018 | Citation: | Zhang, R, Chandramohanadas, R, Lim, C.T, Dao, M (2018). Febrile Temperature Elevates the Expression of Phosphatidylserine on Plasmodium falciparum (FCR3CSA) Infected Red Blood Cell Surface Leading to Increased Cytoadhesion. Scientific Reports 8 (1) : 15022. ScholarBank@NUS Repository. https://doi.org/10.1038/s41598-018-33358-2 | Abstract: | During the asexual intra-erythrocytic cycle, Plasmodium (P.) falciparum exports parasitic proteins to the surface of infected red blood cells (iRBCs) facilitating its cytoadhesion to various endothelial host receptors. This adhesive behavior is a critical contributor towards disease manifestation. However, little is known about the influence of recurring elevated temperature – a common symptom of the malaria infection – on the adhesive properties of iRBCs to endothelial receptors. To address this, we performed dual-micropipette step-pressure technique between P. falciparum (strain FCR3CSA) iRBCs and Chinese Hamster Ovary cells expressing Chondroitin sulfate A (CHO-CSA) after transient iRBCs incubation at febrile temperatures which revealed increase in adhesion parameters. Furthermore, flow cytometry analysis revealed an increase in phosphatidylserine (PS) expression on the iRBC surface following exposure to febrile temperature. The adhesion between iRBCs and CHO-CSA cells was remarkably reduced in presence of soluble Annexin V, indicating the mediation of PS on the adhesion events. Our results suggest that elevated PS recruitment on iRBC under thermally stressed conditions contributes to the increased adhesive behavior of iRBCs CSA-binding phenotype to CHO-CSA. © 2018, The Author(s). | Source Title: | Scientific Reports | URI: | https://scholarbank.nus.edu.sg/handle/10635/175015 | ISSN: | 20452322 | DOI: | 10.1038/s41598-018-33358-2 |
Appears in Collections: | Elements Staff Publications |
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