2022 Fiscal Year Final Research Report
The ligand recognition mechanism of immune activation receptor, LILRA2
Project/Area Number |
20K06518
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Multi-year Fund |
Section | 一般 |
Review Section |
Basic Section 43020:Structural biochemistry-related
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Research Institution | Kanazawa University (2021-2022) Hokkaido University (2020) |
Principal Investigator |
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Project Period (FY) |
2020-04-01 – 2023-03-31
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Keywords | 免疫受容体 / 相互作用解析 / 感染症 / 構造解析 / タンパク質 / 抗体 / 免疫活性化 |
Outline of Final Research Achievements |
The LILR (Leukocyte Immunoglobulin-Like Receptor) group is a transmembrane receptor-type protein expressed in immune cells. Although they have similar extracellular structures, they are broadly classified into the LILRA group, which has an immunoreceptor tyrosine-based activation motif (ITAM), or the LILRB group, which has Immunoreceptor tyrosine-based inhibitory motif (ITIM). Recently, it was reported that LILRA2 recognizes antibodies that have lost their antigen-recognition sites (cleaved antibodies) after cleavage between VH and CH1 of antibodies by protease secreted by bacteria. Here, we uncovered the the recognition mechanism of LILRA2 for its truncated antibody and two newly discovered ligands (ligands A and B).
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Free Research Field |
分子免疫学
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Academic Significance and Societal Importance of the Research Achievements |
近年、免疫細胞の表面に発現する受容体は、病原体の認識に関わっているだけでなく、がん細胞の排除への関与に関わっている。一方で、受容体を介して、過剰な免疫応答も引き起こされることもわかっている。本研究では、LILRA2と呼ばれる分子がどのように病原体の侵入に関わっているか明らかにした。さらに、LILRA2は自分自身の分子に結合することも明らかになってきた。本研究によって、LILRA2タンパク質の病原体侵入に関わる部分と、自分自身の分子に結合する部分が違うことが明らかとなった。
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