The MHC-Ib Molecule HLA-F Presents Peptides and Regulates Immunity Through Interactions with NK-Cell Receptors /
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| Author / Creator: | Dulberger, Charles Lefco, author. |
|---|---|
| Imprint: | 2017. Ann Arbor : ProQuest Dissertations & Theses, 2017 |
| Description: | 1 electronic resource (111 pages) |
| Language: | English |
| Format: | E-Resource Dissertations |
| Local Note: | School code: 0330 |
| URL for this record: | http://pi.lib.uchicago.edu/1001/cat/bib/11715053 |
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| 100 | 1 | |a Dulberger, Charles Lefco, |e author. |0 (orcid)0000-0002-1334-5468 | |
| 245 | 1 | 4 | |a The MHC-Ib Molecule HLA-F Presents Peptides and Regulates Immunity Through Interactions with NK-Cell Receptors / |c Charles Lefco Dulberger. |
| 260 | |c 2017. | ||
| 264 | 1 | |a Ann Arbor : |b ProQuest Dissertations & Theses, |c 2017 | |
| 300 | |a 1 electronic resource (111 pages) | ||
| 336 | |a text |b txt |2 rdacontent |0 http://id.loc.gov/vocabulary/contentTypes/txt | ||
| 337 | |a computer |b c |2 rdamedia |0 http://id.loc.gov/vocabulary/mediaTypes/c | ||
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| 500 | |a Includes supplementary digital materials. | ||
| 500 | |a Advisors: Erin J. Adams Committee members: Sean Crosson; Bana Jabri; Vincent J. Lynch. | ||
| 502 | |b Ph.D. |c University of Chicago, Division of the Biological Sciences, Department of Biochemistry and Molecular Biology |d 2017. | ||
| 510 | 4 | |a Dissertation Abstracts International, |c Volume: 78-12(E), Section: B. | |
| 520 | |a Evidence is mounting that HLA-F regulates the immune system in pregnancy, infection, and autoimmunity by signaling through NK-cell receptors (NKRs). We present structural, biochemical and evolutionary analyses demonstrating that HLA-F presents peptides of unconventional length dictated by a newly arisen mutation in the antigen-binding cleft (R62W) that has produced an open-ended groove that accommodates particularly long peptides. Compared to empty HLA-F open conformers (OC), HLA-F tetramers bound with human-derived peptides differentially stain leukocytes suggesting peptide-dependent engagement. Our binding studies and functional assays confirm that NKRs differentiate between peptide-bound and peptide-free HLA-F OC. The complex structure of peptide-loaded β 2m-HLA-F bound to the inhibitory LIR1 reveals similarities to high-affinity UL18 recognition and a docking strategy that relies on contacts with the HLA-F heavy chain as well as β2m, precluding binding to HLA-F OC. These findings provide the biochemical framework for how HLA-F regulates immunity via interactions with NKRs. Supplementary Table 2.2, which contains the peptide sequences eluted from HLA-F produced in HEK293T cells, can be found online. | ||
| 546 | |a English | ||
| 590 | |a School code: 0330 | ||
| 690 | |a Biochemistry. | ||
| 690 | |a Immunology. | ||
| 710 | 2 | |a University of Chicago. |e degree granting institution. |0 http://id.loc.gov/authorities/names/n79058404 |1 http://viaf.org/viaf/143657677 | |
| 720 | 1 | |a Erin J. Adams |e degree supervisor. | |
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