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Biochem Biophys Res Commun. 2018 Jun 2;500(2):261-267. doi: 10.1016/j.bbrc.2018.04.056. Epub 2018 Apr 13.

The malaria parasite RhopH protein complex interacts with erythrocyte calmyrin identified from a comprehensive erythrocyte protein library.

Author information

1
Division of Malaria Research, Proteo-Science Center, Ehime University, Matsuyama, Ehime 790-8577, Japan.
2
Division of Medical Zoology, Department of Microbiology and Immunology, Faculty of Medicine, Tottori University, Yonago, Tottori 683-8503, Japan.
3
Division of Cell-Free Sciences, Proteo-Science Center, Ehime University, Matsuyama, Ehime 790-8577, Japan.
4
Division of Molecular Parasitology, Proteo-Science Center, Ehime University, Shitsukawa, Toon, Ehime 791-0295, Japan.
5
Division of Malaria Research, Proteo-Science Center, Ehime University, Matsuyama, Ehime 790-8577, Japan. Electronic address: tsuboi.takafumi.mb@ehime-u.ac.jp.

Abstract

Malaria merozoite apical organelles; microneme and rhoptry secreted proteins play functional roles during and following invasion of host erythrocytes. Among numerous proteins, the rhoptries discharge high molecular weight proteins known as RhopH complex. Recent reports suggest that the RhopH complex is essential for growth and survival of the malaria parasite within erythrocytes. However, an in-depth understanding of the host-parasite molecular interactions is indispensable. Here we utilized a comprehensive mouse erythrocyte protein library consisting of 443 proteins produced by a wheat germ cell-free system, combined with AlphaScreen technology to identify mouse erythrocyte calmyrin as an interacting molecule of the rodent malaria parasite Plasmodium yoelii RhopH complex (PyRhopH). The PyRhopH interaction was dependent on the calmyrin N-terminus and divalent cation capacity. The finding unveils a recommendable and invaluable usefulness of our comprehensive mouse erythrocyte protein library together with the AlphaScreen technology in investigating a wide-range of host-parasite molecular interactions.

KEYWORDS:

AlphaScreen; Calmyrin; Erythrocyte protein; Plasmodium yoelii; RhopH complex; Wheat germ cell-free system

PMID:
29653104
DOI:
10.1016/j.bbrc.2018.04.056
[Indexed for MEDLINE]

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