Pf155/RESA protein influences the dynamic microcirculatory behavior of ring-stage Plasmodium falciparum infected red blood cells
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Han_Pf155 RESA protein.pdf
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Author(s)
Diez Silva, Monica
Park, YongKeun
Huang, Sha
Bow, Hansen
Mercereau-Puijalon, Odile
Deplaine, Guillaume
Lavazec, Catherine
Perrot, Sylvie
Bonnefoy, Serge
Feld, Michael S.
Date Issued
August 2012
Journal
Scientific Reports
Publisher
Nature Publishing Group
Citation
Diez-Silva, Monica, YongKeun Park, Sha Huang, Hansen Bow, Odile Mercereau-Puijalon, Guillaume Deplaine, Catherine Lavazec, et al. “Pf155/RESA Protein Influences the Dynamic Microcirculatory Behavior of Ring-Stage Plasmodium Falciparum Infected Red Blood Cells.” Sci. Rep. 2 (August 30, 2012).
Version
Final published version
Abstract
Proteins exported by Plasmodium falciparum to the red blood cell (RBC) membrane modify the structural properties of the parasitized RBC (Pf-RBC). Although quasi-static single cell assays show reduced ring-stage Pf-RBCs deformability, the parameters influencing their microcirculatory behavior remain unexplored. Here, we study the dynamic properties of ring-stage Pf-RBCs and the role of the parasite protein Pf155/Ring-Infected Erythrocyte Surface Antigen (RESA). Diffraction phase microscopy revealed RESA-driven decreased Pf-RBCs membrane fluctuations. Microfluidic experiments showed a RESA-dependent reduction in the Pf-RBCs transit velocity, which was potentiated at febrile temperature. In a microspheres filtration system, incubation at febrile temperature impaired traversal of RESA-expressing Pf-RBCs. These results show that RESA influences ring-stage Pf-RBCs microcirculation, an effect that is fever-enhanced. This is the first identification of a parasite factor influencing the dynamic circulation of young asexual Pf-RBCs in physiologically relevant conditions, offering novel possibilities for interventions to reduce parasite survival and pathogenesis in its human host.
MIT Department
Massachusetts Institute of Technology. Department of Electrical Engineering and Computer Science
Massachusetts Institute of Technology. Department of Materials Science and Engineering
Massachusetts Institute of Technology. Spectroscopy Laboratory
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DOI of Published Version
https://doi.org/10.1038/srep00614
