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

Autores
Hernandez, Sophia Raine C.; Rashpa, Ravish; Jonsdottir, Thorey K.; Paoletta, Martina; Beek, Josy ter; 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.
Año de publicación
2026
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
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.
Instituto de Biotecnología
Fil: Hernandez, Sophia Raine C. Umeå University. The Laboratory for Molecular Infection Medicine Sweden (MIMS); Suecia
Fil: Hernandez, Sophia Raine C. Umeå University. Department of Molecular Biology; Suecia
Fil: Rashpa, Ravish. University of Geneva. Faculty of Medicine. Department of Microbiology and Molecular Medicine; Suiza
Fil: Jonsdottir, Thorey K. Umeå University. The Laboratory for Molecular Infection Medicine Sweden (MIMS); Suecia
Fil: Jonsdottir, Thorey K. Umeå University. Department of Molecular Biology; Suecia
Fil: Paoletta, Martina. Umeå University. The Laboratory for Molecular Infection Medicine Sweden (MIMS); Suecia
Fil: Paoletta, Martina. Umeå University. Department of Molecular Biology; Suecia
Fil: Paoletta, Martina. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Agrobiotecnología y Biología Molecular; Argentina
Fil: Paoletta, Martina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Beek, Josy ter. Umeå University. Wallenberg Centre for Molecular Medicine; Suecia
Fil: Beek, Josy ter. Umeå University. Department of Medical Biochemistry and Biophysics; Suecia
Fil: Rayón Díaz, María. Umeå University. The Laboratory for Molecular Infection Medicine Sweden (MIMS); Suecia
Fil: Rayón Díaz, María. Umeå University. Department of Molecular Biology; Suecia
Fil: Krol, Jelte M.M. Leiden University Medical Center. Leiden University Center for Infectious Diseases (LUCID); Países Bajos
Fil: Chevalley-Maurel, Severine. Leiden University Medical Center. Leiden University Center for Infectious Diseases (LUCID); Países Bajos
Fil: Ishizaki, Takahiro. Umeå University. The Laboratory for Molecular Infection Medicine Sweden (MIMS); Suecia
Fil: Ishizaki, Takahiro. Umeå University. Department of Molecular Biology; Suecia
Fil: Ishizaki, Takahiro. Rakuno Gakuen University. School of Veterinary Medicine. Department of Infection and Pathology. Parasitology and Zoology Unit; Japón
Fil: Berntsson, Ronnie P.-A. Umeå University. Wallenberg Centre for Molecular Medicine; Suecia
Fil: Berntsson, Ronnie P.-A. Umeå University. Department of Medical Biochemistry and Biophysics; Suecia
Fil: Berntsson, Ronnie P.-A. Umeå University. Umeå Center for Microbial Research (UCMR); Suecia
Fil: Janse, Chris J. Leiden University Medical Center. Leiden University Center for Infectious Diseases (LUCID); Países Bajos
Fil: Franke-Fayard, Blandine. Leiden University Medical Center. Leiden University Center for Infectious Diseases (LUCID); Países Bajos
Fil: Brochet, Mathieu. University of Geneva. Faculty of Medicine. Department of Microbiology and Molecular Medicine; Suiza
Fil: Bushell, Ellen S. C. Umeå University. The Laboratory for Molecular Infection Medicine Sweden (MIMS); Suecia
Fil: Bushell, Ellen S. C. Umeå University. Department of Molecular Biology; Suecia
Fil: Bushell, Ellen S. C. Umeå University. Umeå Center for Microbial Research (UCMR); Suecia
Fuente
Molecular Microbiology : 1-17. (First published: 20 January 2026)
Materia
Plasmodium berghei
Eritrocitos
Enfermedad Transmitida por Vectores
Enfermedades Parasitarias
Erythrocytes
Vector-borne Diseases
Malaria
Parasitoses
Glóbulos Rojos
Red Blood Cells
Protein Transport
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by-nc-sa/4.0/
Repositorio
INTA Digital (INTA)
Institución
Instituto Nacional de Tecnología Agropecuaria
OAI Identificador
oai:localhost:20.500.12123/25269

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spelling Erythrocyte Membrane Protein 3 (EMAP3) Is Exposed on the Surface of the Plasmodium berghei Infected Red Blood CellHernandez, Sophia Raine C.Rashpa, RavishJonsdottir, Thorey K.Paoletta, MartinaBeek, Josy terRayón Díaz, MaríaKrol, Jelte M.M.Chevalley-Maurel, SeverineIshizaki, TakahiroBerntsson, Ronnie P.-A.Janse, Chris J.Franke-Fayard, BlandineBrochet, MathieuBushell, Ellen S. C.Plasmodium bergheiEritrocitosEnfermedad Transmitida por VectoresEnfermedades ParasitariasErythrocytesVector-borne DiseasesMalariaParasitosesGlóbulos RojosRed Blood CellsProtein TransportThe 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.Instituto de BiotecnologíaFil: Hernandez, Sophia Raine C. Umeå University. The Laboratory for Molecular Infection Medicine Sweden (MIMS); SueciaFil: Hernandez, Sophia Raine C. Umeå University. Department of Molecular Biology; SueciaFil: Rashpa, Ravish. University of Geneva. Faculty of Medicine. Department of Microbiology and Molecular Medicine; SuizaFil: Jonsdottir, Thorey K. Umeå University. The Laboratory for Molecular Infection Medicine Sweden (MIMS); SueciaFil: Jonsdottir, Thorey K. Umeå University. Department of Molecular Biology; SueciaFil: Paoletta, Martina. Umeå University. The Laboratory for Molecular Infection Medicine Sweden (MIMS); SueciaFil: Paoletta, Martina. Umeå University. Department of Molecular Biology; SueciaFil: Paoletta, Martina. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Agrobiotecnología y Biología Molecular; ArgentinaFil: Paoletta, Martina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Beek, Josy ter. Umeå University. Wallenberg Centre for Molecular Medicine; SueciaFil: Beek, Josy ter. Umeå University. Department of Medical Biochemistry and Biophysics; SueciaFil: Rayón Díaz, María. Umeå University. The Laboratory for Molecular Infection Medicine Sweden (MIMS); SueciaFil: Rayón Díaz, María. Umeå University. Department of Molecular Biology; SueciaFil: Krol, Jelte M.M. Leiden University Medical Center. Leiden University Center for Infectious Diseases (LUCID); Países BajosFil: Chevalley-Maurel, Severine. Leiden University Medical Center. Leiden University Center for Infectious Diseases (LUCID); Países BajosFil: Ishizaki, Takahiro. Umeå University. The Laboratory for Molecular Infection Medicine Sweden (MIMS); SueciaFil: Ishizaki, Takahiro. Umeå University. Department of Molecular Biology; SueciaFil: Ishizaki, Takahiro. Rakuno Gakuen University. School of Veterinary Medicine. Department of Infection and Pathology. Parasitology and Zoology Unit; JapónFil: Berntsson, Ronnie P.-A. Umeå University. Wallenberg Centre for Molecular Medicine; SueciaFil: Berntsson, Ronnie P.-A. Umeå University. Department of Medical Biochemistry and Biophysics; SueciaFil: Berntsson, Ronnie P.-A. Umeå University. Umeå Center for Microbial Research (UCMR); SueciaFil: Janse, Chris J. Leiden University Medical Center. Leiden University Center for Infectious Diseases (LUCID); Países BajosFil: Franke-Fayard, Blandine. Leiden University Medical Center. Leiden University Center for Infectious Diseases (LUCID); Países BajosFil: Brochet, Mathieu. University of Geneva. Faculty of Medicine. Department of Microbiology and Molecular Medicine; SuizaFil: Bushell, Ellen S. C. Umeå University. The Laboratory for Molecular Infection Medicine Sweden (MIMS); SueciaFil: Bushell, Ellen S. C. Umeå University. Department of Molecular Biology; SueciaFil: Bushell, Ellen S. C. Umeå University. Umeå Center for Microbial Research (UCMR); SueciaWiley2026-02-23T13:22:40Z2026-02-23T13:22:40Z2026-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://hdl.handle.net/20.500.12123/25269https://onlinelibrary.wiley.com/doi/10.1111/mmi.700500950-382X1365-2958https://doi.org/10.1111/mmi.70050Molecular Microbiology : 1-17. (First published: 20 January 2026)reponame:INTA Digital (INTA)instname:Instituto Nacional de Tecnología Agropecuariaenginfo:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)2026-02-26T11:47:43Zoai:localhost:20.500.12123/25269instacron:INTAInstitucionalhttp://repositorio.inta.gob.ar/Organismo científico-tecnológicoNo correspondehttp://repositorio.inta.gob.ar/oai/requesttripaldi.nicolas@inta.gob.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:l2026-02-26 11:47:43.183INTA Digital (INTA) - Instituto Nacional de Tecnología Agropecuariafalse
dc.title.none.fl_str_mv Erythrocyte Membrane Protein 3 (EMAP3) Is Exposed on the Surface of the Plasmodium berghei Infected Red Blood Cell
title Erythrocyte Membrane Protein 3 (EMAP3) Is Exposed on the Surface of the Plasmodium berghei Infected Red Blood Cell
spellingShingle Erythrocyte Membrane Protein 3 (EMAP3) Is Exposed on the Surface of the Plasmodium berghei Infected Red Blood Cell
Hernandez, Sophia Raine C.
Plasmodium berghei
Eritrocitos
Enfermedad Transmitida por Vectores
Enfermedades Parasitarias
Erythrocytes
Vector-borne Diseases
Malaria
Parasitoses
Glóbulos Rojos
Red Blood Cells
Protein Transport
title_short Erythrocyte Membrane Protein 3 (EMAP3) Is Exposed on the Surface of the Plasmodium berghei Infected Red Blood Cell
title_full Erythrocyte Membrane Protein 3 (EMAP3) Is Exposed on the Surface of the Plasmodium berghei Infected Red Blood Cell
title_fullStr Erythrocyte Membrane Protein 3 (EMAP3) Is Exposed on the Surface of the Plasmodium berghei Infected Red Blood Cell
title_full_unstemmed Erythrocyte Membrane Protein 3 (EMAP3) Is Exposed on the Surface of the Plasmodium berghei Infected Red Blood Cell
title_sort Erythrocyte Membrane Protein 3 (EMAP3) Is Exposed on the Surface of the Plasmodium berghei Infected Red Blood Cell
dc.creator.none.fl_str_mv Hernandez, Sophia Raine C.
Rashpa, Ravish
Jonsdottir, Thorey K.
Paoletta, Martina
Beek, Josy ter
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.
author Hernandez, Sophia Raine C.
author_facet Hernandez, Sophia Raine C.
Rashpa, Ravish
Jonsdottir, Thorey K.
Paoletta, Martina
Beek, Josy ter
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.
author_role author
author2 Rashpa, Ravish
Jonsdottir, Thorey K.
Paoletta, Martina
Beek, Josy ter
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.
author2_role author
author
author
author
author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Plasmodium berghei
Eritrocitos
Enfermedad Transmitida por Vectores
Enfermedades Parasitarias
Erythrocytes
Vector-borne Diseases
Malaria
Parasitoses
Glóbulos Rojos
Red Blood Cells
Protein Transport
topic Plasmodium berghei
Eritrocitos
Enfermedad Transmitida por Vectores
Enfermedades Parasitarias
Erythrocytes
Vector-borne Diseases
Malaria
Parasitoses
Glóbulos Rojos
Red Blood Cells
Protein Transport
dc.description.none.fl_txt_mv 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.
Instituto de Biotecnología
Fil: Hernandez, Sophia Raine C. Umeå University. The Laboratory for Molecular Infection Medicine Sweden (MIMS); Suecia
Fil: Hernandez, Sophia Raine C. Umeå University. Department of Molecular Biology; Suecia
Fil: Rashpa, Ravish. University of Geneva. Faculty of Medicine. Department of Microbiology and Molecular Medicine; Suiza
Fil: Jonsdottir, Thorey K. Umeå University. The Laboratory for Molecular Infection Medicine Sweden (MIMS); Suecia
Fil: Jonsdottir, Thorey K. Umeå University. Department of Molecular Biology; Suecia
Fil: Paoletta, Martina. Umeå University. The Laboratory for Molecular Infection Medicine Sweden (MIMS); Suecia
Fil: Paoletta, Martina. Umeå University. Department of Molecular Biology; Suecia
Fil: Paoletta, Martina. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Agrobiotecnología y Biología Molecular; Argentina
Fil: Paoletta, Martina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Beek, Josy ter. Umeå University. Wallenberg Centre for Molecular Medicine; Suecia
Fil: Beek, Josy ter. Umeå University. Department of Medical Biochemistry and Biophysics; Suecia
Fil: Rayón Díaz, María. Umeå University. The Laboratory for Molecular Infection Medicine Sweden (MIMS); Suecia
Fil: Rayón Díaz, María. Umeå University. Department of Molecular Biology; Suecia
Fil: Krol, Jelte M.M. Leiden University Medical Center. Leiden University Center for Infectious Diseases (LUCID); Países Bajos
Fil: Chevalley-Maurel, Severine. Leiden University Medical Center. Leiden University Center for Infectious Diseases (LUCID); Países Bajos
Fil: Ishizaki, Takahiro. Umeå University. The Laboratory for Molecular Infection Medicine Sweden (MIMS); Suecia
Fil: Ishizaki, Takahiro. Umeå University. Department of Molecular Biology; Suecia
Fil: Ishizaki, Takahiro. Rakuno Gakuen University. School of Veterinary Medicine. Department of Infection and Pathology. Parasitology and Zoology Unit; Japón
Fil: Berntsson, Ronnie P.-A. Umeå University. Wallenberg Centre for Molecular Medicine; Suecia
Fil: Berntsson, Ronnie P.-A. Umeå University. Department of Medical Biochemistry and Biophysics; Suecia
Fil: Berntsson, Ronnie P.-A. Umeå University. Umeå Center for Microbial Research (UCMR); Suecia
Fil: Janse, Chris J. Leiden University Medical Center. Leiden University Center for Infectious Diseases (LUCID); Países Bajos
Fil: Franke-Fayard, Blandine. Leiden University Medical Center. Leiden University Center for Infectious Diseases (LUCID); Países Bajos
Fil: Brochet, Mathieu. University of Geneva. Faculty of Medicine. Department of Microbiology and Molecular Medicine; Suiza
Fil: Bushell, Ellen S. C. Umeå University. The Laboratory for Molecular Infection Medicine Sweden (MIMS); Suecia
Fil: Bushell, Ellen S. C. Umeå University. Department of Molecular Biology; Suecia
Fil: Bushell, Ellen S. C. Umeå University. Umeå Center for Microbial Research (UCMR); Suecia
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.
publishDate 2026
dc.date.none.fl_str_mv 2026-02-23T13:22:40Z
2026-02-23T13:22:40Z
2026-01
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status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/20.500.12123/25269
https://onlinelibrary.wiley.com/doi/10.1111/mmi.70050
0950-382X
1365-2958
https://doi.org/10.1111/mmi.70050
url http://hdl.handle.net/20.500.12123/25269
https://onlinelibrary.wiley.com/doi/10.1111/mmi.70050
https://doi.org/10.1111/mmi.70050
identifier_str_mv 0950-382X
1365-2958
dc.language.none.fl_str_mv eng
language eng
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
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Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Wiley
publisher.none.fl_str_mv Wiley
dc.source.none.fl_str_mv Molecular Microbiology : 1-17. (First published: 20 January 2026)
reponame:INTA Digital (INTA)
instname:Instituto Nacional de Tecnología Agropecuaria
reponame_str INTA Digital (INTA)
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repository.name.fl_str_mv INTA Digital (INTA) - Instituto Nacional de Tecnología Agropecuaria
repository.mail.fl_str_mv tripaldi.nicolas@inta.gob.ar
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