1. Structural Biology and Molecular Biophysics
  2. Microbiology and Infectious Disease

Crystal structure of PfRh5, an essential P. falciparum ligand for invasion of human erythrocytes

  1. Lin Chen
  2. Yibin Xu
  3. Julie Healer
  4. Jenny K Thompson
  5. Brian J Smith
  6. Michael C Lawrence
  7. Alan F Cowman  Is a corresponding author
  1. Walter and Eliza Hall Institute of Medical Research, Australia
  2. La Trobe University, Australia
https://doi.org/10.7554/eLife.04187
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  1. Lin Chen
  2. Yibin Xu
  3. Julie Healer
  4. Jenny K Thompson
  5. Brian J Smith
  6. Michael C Lawrence
  7. Alan F Cowman
(2014)
Crystal structure of PfRh5, an essential P. falciparum ligand for invasion of human erythrocytes
eLife 3:e04187.
https://doi.org/10.7554/eLife.04187
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Abstract

Plasmodium falciparum causes the most severe form of malaria in humans and is responsible for over 700,000 deaths annually. It is an obligate intracellular parasite and invades erythrocytes where it grows in a relatively protected niche. Invasion of erythrocytes is essential for parasite survival and this involves interplay of multiple protein-protein interactions. One of the most important interactions is binding of parasite invasion ligand families EBLs and PfRhs to host receptors on the surface of erythrocytes. PfRh5 is the only essential invasion ligand within the PfRh family and is an important vaccine candidate. PfRh5 binds the host receptor basigin. Here we have determined the crystal structure of PfRh5 using diffraction data to 2.18 Å resolution. PfRh5 exhibits a novel fold comprising nine mostly-anti-parallel α-helices encasing a N-terminal β-hairpin, with the overall shape being an elliptical disk. This is the first three-dimensional structure determined for the PfRh family of proteins.

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Author details

  1. Lin Chen

    Walter and Eliza Hall Institute of Medical Research, Melbourne, Australia
    Competing interests
    The authors declare that no competing interests exist.

  2. Yibin Xu

    Walter and Eliza Hall Institute of Medical Research, Melbourne, Australia
    Competing interests
    The authors declare that no competing interests exist.

  3. Julie Healer

    Walter and Eliza Hall Institute of Medical Research, Melbourne, Australia
    Competing interests
    The authors declare that no competing interests exist.

  4. Jenny K Thompson

    Walter and Eliza Hall Institute of Medical Research, Melbourne, Australia
    Competing interests
    The authors declare that no competing interests exist.

  5. Brian J Smith

    La Trobe University, Melbourne, Australia
    Competing interests
    The authors declare that no competing interests exist.

  6. Michael C Lawrence

    Walter and Eliza Hall Institute of Medical Research, Melbourne, Australia
    Competing interests
    The authors declare that no competing interests exist.

  7. Alan F Cowman

    Walter and Eliza Hall Institute of Medical Research, Melbourne, Australia
    For correspondence
    cowman@wehi.edu.au
    Competing interests
    The authors declare that no competing interests exist.

Reviewing Editor

  1. Axel Brakhage, Leibniz Institute for Natural Product Research and Infection Biology - Hans Knöll Institute, Germany

Version history

  1. Received: July 29, 2014
  2. Accepted: October 7, 2014
  3. Accepted Manuscript published: October 8, 2014 (version 1)
  4. Version of Record published: November 3, 2014 (version 2)

Copyright

© 2014, Chen et al.

This article is distributed under the terms of the Creative Commons Attribution License permitting unrestricted use and redistribution provided that the original author and source are credited.

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  1. Lin Chen
  2. Yibin Xu
  3. Julie Healer
  4. Jenny K Thompson
  5. Brian J Smith
  6. Michael C Lawrence
  7. Alan F Cowman
(2014)
Crystal structure of PfRh5, an essential P. falciparum ligand for invasion of human erythrocytes
eLife 3:e04187.
https://doi.org/10.7554/eLife.04187

Share this article

https://doi.org/10.7554/eLife.04187

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