# Erythrocyte Membrane Protein 3 (EMAP3) Is Exposed on the Surface of the Plasmodium berghei Infected Red Blood Cell

**Authors:** Sophia Raine C. Hernandez, Ravish Rashpa, Thorey K. Jonsdottir, Martina S. Paoletta, Josy ter Beek, María Rayón Díaz, Jelte M. M. Krol, Severine Chevalley‐Maurel, Takahiro Ishizaki, Ronnie P.‐A. Berntsson, Chris J. Janse, Blandine Franke‐Fayard, Mathieu Brochet, Ellen S. C. Bushell

PMC · DOI: 10.1111/mmi.70050 · Molecular Microbiology · 2026-01-20

## TL;DR

A new protein called EMAP3 is found on the surface of malaria-infected red blood cells, offering a new way to study how the parasite sticks to blood vessels.

## Contribution

EMAP3 is a novel Plasmodium berghei protein exposed on the surface of infected red blood cells, providing a new platform for studying cytoadherence.

## Key findings

- EMAP3 is trafficked to the outer membrane surface of Plasmodium berghei infected red blood cells.
- EMAP3 is not essential for parasite growth or sequestration but can display Plasmodium falciparum proteins on infected red blood cells.

## Abstract

The human malaria parasite Plasmodium falciparum invades red blood cells (RBCs) and exports parasite proteins to transform the host cell for its survival. These exported proteins facilitate cytoadherence of the infected RBC (iRBC) to endothelial cells of small blood vessels, protecting iRBCs from splenic clearance. The parasite protein PfEMP1 and the host protein CD36 play a major role in P. falciparum iRBC cytoadherence. The murine parasite Plasmodium berghei is a widely used experimental model that combines high genetic tractability with access to in vivo studies. The P. berghei iRBC also sequesters by CD36‐binding via an unknown parasite ligand and few parasite proteins, including EMAP1 and EMAP2, have been localised to the iRBC membrane. We have identified a new protein named EMAP3 and demonstrated its export to the iRBC membrane where it likely interacts with EMAP1, with only EMAP3 exposed on the outer surface of the iRBC. Parasites lacking EMAP3 display no significant reduction in growth or sequestration, indicating that EMAP3 is not a major CD36‐binding protein. The outer‐surface location of EMAP3 offers a new scaffold for displaying P. falciparum proteins on the surface of the P. berghei iRBC, providing a platform to screen in vivo for putative inhibitors of P. falciparum cytoadherence.

Erythrocyte membrane protein 3 (EMAP3) is a novel Plasmodium berghei protein that is trafficked to the outer membrane surface of the infected red blood cell (iRBC). EMAP3 is not critical for parasite growth or sequestration but offers a new scaffold for displaying Plasmodium falciparum proteins on iRBCs.

## Linked entities

- **Proteins:** EML3 (EMAP like 3), CD36 (CD36 molecule (CD36 blood group)), EML1 (EMAP like 1), AIMP1 (aminoacyl tRNA synthetase complex interacting multifunctional protein 1)
- **Diseases:** malaria (MONDO:0005136)
- **Species:** Plasmodium falciparum (taxon 5833), Plasmodium berghei (taxon 5821)

## Full-text entities

- **Genes:** EML1 (EMAP like 1) [NCBI Gene 2009] {aka BH, ELP79, EMAP, EMAP-1, EMAPL}, EML2 (EMAP like 2) [NCBI Gene 24139] {aka ELP70, EMAP-2, EMAP2}, EML3 (EMAP like 3) [NCBI Gene 256364] {aka ELP95, EMAP3, EMAP95}
- **Diseases:** malaria (MESH:D008288)
- **Species:** Plasmodium falciparum (malaria parasite P. falciparum, species) [taxon 5833], Mus musculus (house mouse, species) [taxon 10090], Plasmodium berghei (species) [taxon 5821], Homo sapiens (human, species) [taxon 9606]

## Full text

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## Figures

5 figures with captions in the complete paper: https://tomesphere.com/paper/PMC12956039/full.md

## References

65 references — full list in the complete paper: https://tomesphere.com/paper/PMC12956039/full.md

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Source: https://tomesphere.com/paper/PMC12956039