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Parasite biology

An anchor for Plasmodium invasion

Nature Reviews Microbiology volume 13, pages 128–129 (2015)Cite this article

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CyRPA ... tethers and secures the PfRH5–PfRipr–CyRPA complex to the surface of the parasite

By analysing lysates from schizonts using co-immunoprecipitation followed by mass spectrometry, the authors showed that CyRPA associates with PfRH5 and PfRipr in a native multiprotein complex of ∼200 kDa. In contrast to PfRH5, which is located in the rhoptry in schizont-stage parasites, CyRPA and PfRipr are located in different apical organelles called micronemes. However, PfRH5, CyRPA and PfRipr were found to colocalize at the surface of invading merozoites, which suggests that all three proteins are released from their respective organelles to form a complex at the surface during host cell invasion. Furthermore, whereas PfRH5 interacts with the host receptor basigin, CyRPA lacks erythrocyte-binding activity, which indicates that it does not have a direct function in attachment and might instead have a structural role. Indeed, the authors report that CyRPA has a GPI moiety that tethers and secures the PfRH5–PfRipr–CyRPA complex to the surface of the parasite, thus enabling PfRH5 to associate with basigin and facilitate erythrocyte invasion.

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References

  1. Reddy, K. S., Amlabu, E. et al. Multiprotein complex between the GPI-anchored CyRPA with PfRH5 and PfRipr is crucial for Plasmodium falciparum erythrocyte invasion. Proc. Natl Acad. Sci. USA http://dx.doi.org/10.1073/pnas.1415466112 (2015)

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Authors
  1. Andrea Du Toit
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Du Toit, A. An anchor for Plasmodium invasion. Nat Rev Microbiol 13, 128–129 (2015). https://doi.org/10.1038/nrmicro3436

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