A Duffy Binding–Like Domain Is Involved in the NKp30‐Mediated Recognition ofPlasmodiumfalciparum–Parasitized Erythrocytes by Natural Killer Cells
In: The Journal of Infectious Diseases, Jg. 195 (2007-05-15), S. 1521-1531
Online
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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)-1 alpha 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-1alpha 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-1 alpha peptides abolished both this interaction and killing activity, suggesting that DBL-1 alpha -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 ofPlasmodiumfalciparum–Parasitized Erythrocytes by Natural Killer Cells
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Autor/in / Beteiligte Person: | Kremsner, Peter G. ; Mewono, Ludovic ; Held, Jana ; Mavoungou, Elie |
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Zeitschrift: | The Journal of Infectious Diseases, Jg. 195 (2007-05-15), S. 1521-1531 |
Veröffentlichung: | Oxford University Press (OUP), 2007 |
Medientyp: | unknown |
ISSN: | 1537-6613 (print) ; 0022-1899 (print) |
DOI: | 10.1086/515579 |
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