A duffy binding-like domain is involved in the NKp30-mediated recognition of Plasmodium falciparum-parasitized erythrocytes by natural killer cells
In: The Journal of infectious diseases, Jg. 195 (2007), Heft 10, S. 1521-1531
Online
academicJournal
- print, 37 ref
Zugriff:
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-pRBC 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-la-NCRs interaction is the key recognition mechanism leading to parasite killing by NK cells.
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A duffy binding-like domain is involved in the NKp30-mediated recognition of Plasmodium falciparum-parasitized erythrocytes by natural killer cells
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Autor/in / Beteiligte Person: | MAVOUNGOU, Elie ; HELD, Jana ; MEWONO, Ludovic ; KREMSNER, Peter G |
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Zeitschrift: | The Journal of infectious diseases, Jg. 195 (2007), Heft 10, S. 1521-1531 |
Veröffentlichung: | Chicago, IL: University of Chicago Press, 2007 |
Medientyp: | academicJournal |
Umfang: | print, 37 ref |
ISSN: | 0022-1899 (print) |
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