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Evaluation of the Reactivity and Receptor Competition of HLA-G Isoforms toward Available Antibodies : Implications of Structural Characteristics of HLA-G Isoforms
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| Title: | Evaluation of the Reactivity and Receptor Competition of HLA-G Isoforms toward Available Antibodies : Implications of Structural Characteristics of HLA-G Isoforms |
| Authors: | Furukawa, Atsushi Browse this author | | Meguro, Manami Browse this author | | Yamazaki, Rika Browse this author | | Watanabe, Hiroshi Browse this author | | Takahashi, Ami Browse this author | | Kuroki, Kimiko Browse this author →KAKEN DB | | Maenaka, Katsumi Browse this author →KAKEN DB |
| Keywords: | immune checkpoint | | HLA-G | | antibody | | ELISA |
| Issue Date: | Dec-2019 |
| Publisher: | MDPI |
| Journal Title: | International Journal of Molecular Sciences |
| Volume: | 20 |
| Issue: | 23 |
| Start Page: | 5947 |
| Publisher DOI: | 10.3390/ijms20235947 |
| Abstract: | The human leucocyte antigen (HLA)-G, which consists of seven splice variants, is a tolerogenic immune checkpoint molecule. It plays an important role in the protection of the fetus from the maternal immune response by binding to inhibitory receptors, including leukocyte Ig-like receptors (LILRs). Recent studies have also revealed that HLA-G is involved in the progression of cancer cells and the protection from autoimmune diseases. In contrast to its well characterized isoform, HLA-G1, the binding activities of other major HLA-G isoforms, such as HLA-G2, toward available anti-HLA-G antibodies are only partially understood. Here, we investigate the binding specificities of anti-HLA-G antibodies by using surface plasmon resonance. MEM-G9 and G233 showed strong affinities to HLA-G1, with a nM range for their dissociation constants, but did not show affinities to HLA-G2. The disulfide-linker HLA-G1 dimer further exhibited significant avidity effects. On the other hand, 4H84 and MEM-G1, which can be used for the Western blotting of HLA-G isoforms, can bind to native HLA-G2, while MEM-G9 and G233 cannot. These results reveal that HLA-G2 has a partially intrinsically disordered structure. Furthermore, MEM-G1, but not 4H84, competes with the LILRB2 binding of HLA-G2. These results provide novel insight into the functional characterization of HLA-G isoforms and their detection systems. |
| Rights: | https://creativecommons.org/licenses/by/4.0/ |
| Type: | article |
| URI: | http://hdl.handle.net/2115/76612 |
| Appears in Collections: | 薬学研究院 (Faculty of Pharmaceutical Sciences) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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