期刊
JOURNAL OF IMMUNOLOGY
卷 198, 期 9, 页码 3399-3403出版社
AMER ASSOC IMMUNOLOGISTS
DOI: 10.4049/jimmunol.1601296
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资金
- Platform for Drug Discovery, Informatics, and Structural Life Science
- Japan Society for the Promotion of Science [23770102, 25870019, 16J05871, 22121007]
- Ministry of Education, Culture, Sports, Science and Technology of Japan
- Ministry of Health, Labour and Welfare of Japan
- Program for Advancing Strategic International Networks to Accelerate the Circulation of Talented Researchers
- CREST, Japan Science and Technology
- Naito Foundation Subsidy for Female Researchers after Maternity Leave
- Support Office for Female Researchers at Hokkaido University
- Grants-in-Aid for Scientific Research [16H01562, 25870019, 26440076, 22121007, 16J05871, 23770102] Funding Source: KAKEN
HLA-G is a natural tolerogenic molecule and has the following unique features: seven isoforms (HLA-G1 to HLA-G7), formation of disulfide-linked homodimers, and (beta 2-microglobulin (beta 2m)-free forms. Interestingly, individuals null for the major isoform, HLA-G1, are healthy and expressed the alpha 2 domain-deleted isoform, HLA-G2, which presumably compensates for HLA-G1 function. However, the molecular characteristics of HLA-G2 are largely unknown. In this study, we unexpectedly found that HLA-G2 naturally forms a beta 2m-free and nondisulfide-linked homodimer, which is in contrast to the disulfide-bonded beta 2m-associated HLA-G1 homodimer. Furthermore, single-particle analysis, using electron microscopy, revealed that the overall structure and domain organization of the HLA-G2 homodimer resemble those of the HLA class II heterodimer. The HLA-G2 homodimer binds to leukocyte Ig-like receptor B2 with slow dissociation and a significant avidity effect. These findings provide novel insights into leukocyte Ig-like receptor B2-mediated immune regulation by the HLA-G2 isoform, as well as the gene evolution of HLA classes.
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