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Open conformers of HLA-F are high-affinity ligands of the activating NK-cell receptor KIR3DS1

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Garcia-Beltran, Wilfredo F | Hölzemer, Angelique | Martrus, Gloria | Chung, Amy W | Pacheco, Yovana | Simoneau, Camille R | Rucevic, Marijana | Lamothe-Molina, Pedro A | Pertel, Thomas | Kim, Tae-Eun | Dugan, Haley | Alter, Galit | Dechanet-Merville, Julie | Jost, Stephanie | Carrington, Mary | Altfeld, Marcus

Edité par CCSD ; Nature Publishing Group -

International audience. The activating natural killer (NK)-cell receptor KIR3DS1 has been linked to the outcome of various human diseases, including delayed progression of disease caused by human immunodeficiency virus type 1 (HIV-1), yet a ligand that would account for its biological effects has remained unknown. We screened 100 HLA class I proteins and found that KIR3DS1 bound to HLA-F, a result we confirmed biochemically and functionally. Primary human KIR3DS1(+) NK cells degranulated and produced antiviral cytokines after encountering HLA-F and inhibited HIV-1 replication in vitro. Activation of CD4(+) T cells triggered the transcription and surface expression of HLA-F mRNA and HLA-F protein, respectively, and induced binding of KIR3DS1. HIV-1 infection further increased the transcription of HLA-F mRNA but decreased the binding of KIR3DS1, indicative of a mechanism for evading recognition by KIR3DS1(+) NK cells. Thus, we have established HLA-F as a ligand of KIR3DS1 and have demonstrated cell-context-dependent expression of HLA-F that might explain the widespread influence of KIR3DS1 in human disease.

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