The use of trimeric isoleucine-zipper fusion proteins to study surface-receptor-ligand interactions in natural killer cells.
The ligands for several activating natural killer (NK) cell receptors have not been identified to date. Soluble receptor fusion proteins can be used to stain target cells for the presence of these unidentified ligands. Here, we describe the generation and use of soluble type I NK cell receptor isoleucine-zipper (ILZ) fusion proteins of the immunoglobulin (Ig) superfamily. ILZ-fusion proteins are easy to produce and purify. They form trimeric complexes in solution and display a higher binding avidity than classical immunoglobulin-fusion proteins. ILZ-fusion proteins do not interact with Fc-receptors and can therefore be used to block receptor-ligand interactions in cellular assays. This makes ILZ-fusion proteins a valuable tool to study receptor-ligand interactions in NK cells and other cellular systems.
Stark
Sebastian
S
Institute for Immunology, University Heidelberg, Im Neuenheimer Feld 305, 69120 Heidelberg, Germany.
Flaig
Ruediger M
RM
Sandusky
Mina
M
Watzl
Carsten
C
D020816:Amino Acid Motifs; D003601:Cytotoxicity Tests, Immunologic; D003602:Cytotoxicity, Immunologic / Q000187:drug effects* / Q000276:immunology; D006801:Humans; D007532:Isoleucine / Q000737:chemistry; D007694:Killer Cells, Natural / Q000276:immunology*; D008024:Ligands; D017452:Receptors, IgG / Q000235:genetics; D011971:Receptors, Immunologic / Q000037:antagonists & inhibitors* / Q000737:chemistry / Q000235:genetics*; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000276:immunology / Q000494:pharmacology
D008024:Ligands; D017452:Receptors, IgG; D011971:Receptors, Immunologic; D011993:Recombinant Fusion Proteins; D007532:Isoleucine