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Journal Article

HLA-G mediated immune regulation is impaired by a single amino acid exchange in the alpha 2 domain.


Huyton,  T.
Department of Cellular Logistics, MPI for Biophysical Chemistry, Max Planck Society;

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Celik, A. A., Simper, G. S., Huyton, T., Blasczyk, R., & Bade-Döding, C. (2018). HLA-G mediated immune regulation is impaired by a single amino acid exchange in the alpha 2 domain. Human Immunology, 79(6), 453-462. doi:10.1016/j.humimm.2018.03.010.

Cite as: http://hdl.handle.net/21.11116/0000-0001-5E4A-4
The trade-off from HLA class I expression to HLA-G expression support the immune evasion of malignant cells. The essential role of the virtually invariant HLA-G in immune tolerance, tumor immunology and its expression frequency in immune privileged tissues is known; however the specific importance of allelic subtypes in immune responses is still not well understood. HLA-G*01:01, *01:03 and *01:04 are the most prevalent allelic variants differing at residues 31 and 110, respectively. In cytotoxicity assays applying K562 cells transduced with the HLA-G variants as targets and NK cells as effectors the differential protective potential of HLA-G variants was analyzed. Their peptide profiles were determined utilizing soluble HLA technology. An increased protective potential of HLA-G*01:04 could be observed. All variants exhibit a unique peptide repertoire with marginal overlap, while G*01:04 differs in its peptide anchor profile substantially. The functional differences between HLA-G subtypes could be explained by the constraint of the bound peptides, modifying the pHLA-G accessible surface. For the first time a contribution of amino acid alterations within the HLA-G heavy chain for peptide selection and NK cell recognition could be observed. These results will be a step towards understanding immune tolerance and will guide towards personalized immune therapeutic strategies.