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    Plasmodium falciparum ligand binding to erythrocytes induce alterations in deformability essential for invasion

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    24
    Author
    Sisquella, X; Nebr, T; Thompson, JK; Whitehead, L; Malpede, BM; Salinas, ND; Rogers, K; Tolia, NH; Fleig, A; O'Neill, J; ...
    Date
    2017-02-22
    Source Title
    eLife
    Publisher
    ELIFE SCIENCES PUBLICATIONS LTD
    University of Melbourne Author/s
    Whitehead, Lachlan; Cowman, Alan; Rogers, Kelly; Tham, Wai-Hong
    Affiliation
    Medical Biology (W.E.H.I.)
    Metadata
    Show full item record
    Document Type
    Journal Article
    Citations
    Sisquella, X., Nebr, T., Thompson, J. K., Whitehead, L., Malpede, B. M., Salinas, N. D., Rogers, K., Tolia, N. H., Fleig, A., O'Neill, J., Timm, W. -H., Horgen, F. D. & Cowman, A. F. (2017). Plasmodium falciparum ligand binding to erythrocytes induce alterations in deformability essential for invasion. ELIFE, 6, https://doi.org/10.7554/eLife.21083.
    Access Status
    Open Access
    URI
    http://hdl.handle.net/11343/258262
    DOI
    10.7554/eLife.21083
    Abstract
    The most lethal form of malaria in humans is caused by Plasmodium falciparum. These parasites invade erythrocytes, a complex process involving multiple ligand-receptor interactions. The parasite makes initial contact with the erythrocyte followed by dramatic deformations linked to the function of the Erythrocyte binding antigen family and P. falciparum reticulocyte binding-like families. We show EBA-175 mediates substantial changes in the deformability of erythrocytes by binding to glycophorin A and activating a phosphorylation cascade that includes erythrocyte cytoskeletal proteins resulting in changes in the viscoelastic properties of the host cell. TRPM7 kinase inhibitors FTY720 and waixenicin A block the changes in the deformability of erythrocytes and inhibit merozoite invasion by directly inhibiting the phosphorylation cascade. Therefore, binding of P. falciparum parasites to the erythrocyte directly activate a signaling pathway through a phosphorylation cascade and this alters the viscoelastic properties of the host membrane conditioning it for successful invasion.

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