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Publication Details
AFRICAN RESEARCH NEXUS
SHINING A SPOTLIGHT ON AFRICAN RESEARCH
medicine
A duffy binding-like domain is involved in the NKp30-mediated recognition of Plasmodium falciparum-parasitized erythrocytes by natural killer cells
Journal of Infectious Diseases, Volume 195, No. 10, Year 2007
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Description
The recent demonstration that purified natural killer (NK) cells lyse Plasmodium falciparum-parasitized red blood cells (Pf-pRBCs) suggests that innate immunity is important in malaria. NK cell killing - presumably an early host response to infection - requires intimate contact between NK natural cytotoxicity receptors (NCRs) and ligands expressed on the surface of Pf-pRBCs. We investigated whether the Duffy binding-like (DBL)-1α domain of P. falciparum erythrocyte membrane protein-1 (PfEMP-1) expressed on parasitized erythrocytes rendered Pf-pRBCs susceptible to NK cell lysis. We showed that with NKp30-immunoglobulin and NKp46-immunoglobulin fusion proteins and DBL-1α peptides NCRs are involved in the NK cell-Pf-pKBC interaction. This interaction was direct, specific, and functional, leading to perforin production and granzyme B release. The prior treatment of NK cells with DBL-1α peptides abolished both this interaction and killing activity, suggesting that DBL-1α-NCRs interaction is the key recognition mechanism leading to parasite killing by NK cells. © 2007 by the Infectious Diseases Society of America. All rights reserved.
Authors & Co-Authors
Mavoungou, Elie
Gabon, Lambarene
Unité de Recherche Médicale, Albert Schweitzer Hospital
Germany, Tubingen
Eberhard Karls Universität Tübingen
Held, Jana
Unknown Affiliation
Mewono, Ludovic
Unknown Affiliation
Kremsner, Peter G.
Unknown Affiliation
Statistics
Citations: 96
Authors: 4
Affiliations: 2
Identifiers
Doi:
10.1086/515579
ISSN:
00221899
Research Areas
Infectious Diseases