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
.jpg)
- Institución
- Instituto Nacional de Tecnología Agropecuaria
- OAI Identificador
- oai:localhost:20.500.12123/25269
Ver los metadatos del registro completo
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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 |
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2026-02-23T13:22:40Z 2026-02-23T13:22:40Z 2026-01 |
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info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
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article |
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http://hdl.handle.net/20.500.12123/25269 https://onlinelibrary.wiley.com/doi/10.1111/mmi.70050 https://doi.org/10.1111/mmi.70050 |
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0950-382X 1365-2958 |
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eng |
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eng |
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application/pdf |
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Wiley |
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Wiley |
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