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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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