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Updated: Aug 10, 2026

qKAT: Quantitative Semi-automated Typing of Killer-cell Immunoglobulin-like Receptor Genes
Published on: March 6, 2019
Human natural killer cell inhibitory receptors bind to HLA class I molecules
Insights
Human natural killer cell (NK) inhibitory receptors were studied. A soluble NK-associated transcript-2 receptor specifically binds to HLA-C alleles, providing evidence of physical interaction.
Area of Science:
- Immunology
- Molecular Biology
- Cellular Biology
Background:
- Human natural killer (NK) cells play a crucial role in the innate immune system.
- NK cell inhibitory receptors mediate interactions with target cells.
- Major histocompatibility complex (MHC) class I molecules are key targets for NK cell recognition.
Purpose of the Study:
- To provide direct evidence of physical interaction between NK inhibitory receptors and polymorphic determinants of MHC class I molecules.
- To characterize the binding specificity of a novel NK receptor.
Main Methods:
- Production of a soluble fusion protein of NK-associated transcript-2 with the human IgG1 Fc portion.
- Utilizing cell adhesion assays to evaluate receptor binding.
Main Results:
- The soluble NK-associated transcript-2 receptor specifically bound to HLA-C alleles.
- Binding was observed for HLA-C alleles possessing serine at position 77 and asparagine at position 80.
Conclusions:
- Direct physical interaction between a specific NK receptor and MHC class I molecules has been demonstrated.
- The findings elucidate the molecular basis of NK cell recognition of specific HLA-C alleles.
Abstract:
To obtain direct evidence that human natural killer cell (NK) inhibitory receptors physically interact with polymorphic determinants of major histocompatibility complex class I molecules, a receptor termed NK-associated transcript-2 has been produced as a soluble fusion protein with the human IgG1 Fc portion. This soluble receptor binds specifically to HLA-C alleles with serine 77 and asparagine 80 in cell adhesion assays.
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