HS1 protein (160-168) – Immunology – Antigens/Epitotes/Pools/Librairies

Reactivity to human leukocyte antigens (HLAs) is a risen concern in clinical treatments such as organ transplant rejection. Understanding the epitopes causing reactivity and the signalling pathways could lead to better clinical therapies. The peptides presented by the non-classical HLA-G are important for a largely tolerogenic role and are considered part of an immune checkpoint. This, therefore, makes understanding ligand characteristics and HLA-G a target for cancer therapies. The HS1 fragment (160-168) has been identified as an epitope that human leukocyte antigen HLA-G naturally presents, determined by liquid chromatographic tandem mass spectrometry (LC-Ms/MS). This epitope has been used extensively in the literature to help understand the natural ligand presentation of HLA-G. For example, leukocyte immunoglobulin (Ig)-like receptors (LILRs) are key regulators of the immune response and therefore targets for therapeutics. Inhibitory LILRB1 and LILRB2 with HLA-G are pivotal for immunotolerance during pregnancy and autoimmune diseases plus cancer cell immune evasion. HS1 fragment (160-168) was used in binding affinity assays to clarify the conformational plasticity of the interaction between the receptor, the HLA antigen, and the various peptides HLA-G can accommodate.