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Transfer of the human NKG 2D ligands UL 16 binding proteins (ULBP) 1–3 is related to lytic granule release and leads to ligand retransfer and killing of ULBP ‐recipient natural killer cells
Author(s) -
LópezCobo Sheila,
RomeraCárdenas Gema,
GarcíaCuesta Eva M.,
Reyburn Hugh T.,
ValésGómez Mar
Publication year - 2015
Publication title -
immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.297
H-Index - 133
eISSN - 1365-2567
pISSN - 0019-2805
DOI - 10.1111/imm.12482
Subject(s) - nkg2d , microbiology and biotechnology , immune system , degranulation , effector , chemistry , receptor , lytic cycle , natural killer cell , biology , immunology , cytotoxic t cell , biochemistry , in vitro , virus
Summary After immune interactions, membrane fragments can be transferred between cells. This fast transfer of molecules is transient and shows selectivity for certain proteins; however, the constraints underlying acquisition of a protein are unknown. To characterize the mechanism and functional consequences of this process in natural killer ( NK ) cells, we have compared the transfer of different NKG 2D ligands. We show that human NKG 2D ligands can be acquired by NK cells with different efficiencies. The main findings are that NKG 2D ligand transfer is related to immune activation and receptor–ligand interaction and that NK cells acquire these proteins during interactions with target cells that lead to degranulation. Our results further demonstrate that NK cells that have acquired NKG 2D ligands can stimulate activation of autologous NK cells. Surprisingly, NK cells can also re‐transfer the acquired molecule to autologous effector cells during this immune recognition that leads to their death. These data demonstrate that transfer of molecules occurs as a consequence of immune recognition and imply that this process might play a role in homeostatic tuning‐down of the immune response or be used as marker of interaction.