| Title: |
Erythrocyte membrane protein 3 (EMAP3) is exposed on the surface of the plasmodium berghei infected red blood cell |
| Authors: |
Hernandez, Sophia Raine C.; Rashpa, Ravish; Jonsdottir, Thorey K.; Paoletta, Martina; ter Beek, Josy; Rayón Díaz, María; Krol, Jelte M. M.; Chevalley-Maurel, Severine; Ishizaki, Takahiro; Berntsson, Ronnie P.-A.; Janse, Chris J.; Franke-Fayard, Blandine; Brochet, Mathieu; Bushell, Ellen S.C. |
| Publisher Information: |
Umeå universitet, Molekylär Infektionsmedicin, Sverige (MIMS); Umeå universitet, Institutionen för molekylärbiologi (Medicinska fakulteten); Umeå universitet, Wallenberg centrum för molekylär medicin vid Umeå universitet (WCMM); Umeå universitet, Institutionen för medicinsk kemi och biofysik; Umeå universitet, Umeå Centre for Microbial Research (UCMR); Department of Microbiology and Molecular Medicine, Faculty of Medicine, University of Geneva, Geneva, Switzerland; Instituto de Agrobiotecnología y Biología Molecular (IABIMO), INTA-CONICET, Hurlingham, Argentina; Leiden University Center for Infectious Diseases (LUCID), Leiden University Medical Center (LUMC), Leiden, Netherlands; Parasitology and Zoology Unit, Department of Infection and Pathology, School of Veterinary Medicine, Rakuno Gakuen University, Hokkaido, Ebetsu, Japan |
| Publication Year: |
2026 |
| Collection: |
Umeå University: Publications (DiVA) |
| Subject Terms: |
cell adhesion; malaria; parasitic diseases; Plasmodium; protein trafficking; protein transport; vector-borne diseases; Cell and Molecular Biology; Cell- och molekylärbiologi |
| Description: |
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. |
| Document Type: |
article in journal/newspaper |
| File Description: |
application/pdf |
| Language: |
English |
| Relation: |
Molecular Microbiology, 0950-382X, 2026; PMID 41559880; ISI:001665675800001 |
| DOI: |
10.1111/mmi.70050 |
| Availability: |
http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-249485; https://doi.org/10.1111/mmi.70050 |
| Rights: |
info:eu-repo/semantics/openAccess |
| Accession Number: |
edsbas.8F8769A4 |
| Database: |
BASE |