@article{29992,
  keywords = {leprosy, HLA class I, KIR, Antigen Presentation, Genetic polymorphism, Host-Pathogen Interactions, Mass Spectrometry, Modern human migration, Peptidome},
  author = {Hilton HG and McMurtrey C and Han A and Djaoud Z and Guethlein L and Blokhuis JH and Pugh J and Goyos A and Horowitz A and Buchli R and Jackson KW and Bardet W and Bushnell D and Robinson PJ and Mendoza J and Birnbaum M and Nielsen M and Garcia CK and Hildebrand W and Parham P},
  title = {The Intergenic Recombinant HLA-B∗46:01 Has a Distinctive Peptidome that Includes KIR2DL3 Ligands.},
  abstract = {<p>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.</p>
},
  year = {2017},
  journal = {Cell reports},
  volume = {19},
  pages = {1394-1405},
  issn = {2211-1247},
  url = {http://www.cell.com/cell-reports/pdf/S2211-1247(17)30570-3.pdf},
  doi = {10.1016/j.celrep.2017.04.059},
  language = {eng},
}