期刊
CELL REPORTS
卷 19, 期 7, 页码 1394-1405出版社
CELL PRESS
DOI: 10.1016/j.celrep.2017.04.059
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资金
- NIH [R01 AI22039, K01CA175127, 5R01 AI103867, 1U1 AI057229]
- Stanford Developmental Biology and Genetics training grant [NIH 5 T32 GM007790]
- Stanford Immunology postdoctoral training grant [5 T32 AI07290]
- Emergent Technologies Innovation Fund
- Howard Hughes Medical Institute (HHMI)
HLA-B*46:01 was formed by an intergenic mini-conversion, between HLA-B*15:01 and HLA-C*01:02, in Southeast Asia during the last 50,000 years, and it has since become the most common HLA-B allele in the region. A functional effect of the mini-conversion was introduction of the C1 epitope into HLA-B*46:01, making it an exceptional HLA-B allotype that is recognized by the C1-specific natural killer (NK) cell receptor KIR2DL3. High-resolution mass spectrometry showed that HLA-B*46:01 has a low-diversity peptidome that is distinct from those of its parents. A minority (21%) of HLA-B*46:01 peptides, with common C-terminal characteristics, form ligands for KIR2DL3. The HLA-B*46:01 peptidome is predicted to be enriched for peptide antigens derived from Mycobacterium leprae. Overall, the results indicate that the distinctive peptidome and functions of HLA-B*46:01 provide carriers with resistance to leprosy, which drove its rapid rise in frequency in Southeast Asia.
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