Nature Communications (Aug 2018)
Pathogen-derived HLA-E bound epitopes reveal broad primary anchor pocket tolerability and conformationally malleable peptide binding
- Lucy C. Walters,
- Karl Harlos,
- Simon Brackenridge,
- Daniel Rozbesky,
- Jordan R. Barrett,
- Vitul Jain,
- Thomas S. Walter,
- Chris A. O’Callaghan,
- Persephone Borrow,
- Mireille Toebes,
- Scott G. Hansen,
- Jonah B Sacha,
- Shaheed Abdulhaqq,
- Justin M. Greene,
- Klaus Früh,
- Emily Marshall,
- Louis J. Picker,
- E. Yvonne Jones,
- Andrew J. McMichael,
- Geraldine M. Gillespie
Affiliations
- Lucy C. Walters
- Nuffield Department of Medicine Research Building, Roosevelt Drive, Nuffield Department of Medicine, University of Oxford
- Karl Harlos
- Division of Structural Biology, Wellcome Centre for Human Genetics, Roosevelt Drive, University of Oxford
- Simon Brackenridge
- Nuffield Department of Medicine Research Building, Roosevelt Drive, Nuffield Department of Medicine, University of Oxford
- Daniel Rozbesky
- Division of Structural Biology, Wellcome Centre for Human Genetics, Roosevelt Drive, University of Oxford
- Jordan R. Barrett
- Nuffield Department of Medicine Research Building, Roosevelt Drive, Nuffield Department of Medicine, University of Oxford
- Vitul Jain
- Division of Structural Biology, Wellcome Centre for Human Genetics, Roosevelt Drive, University of Oxford
- Thomas S. Walter
- Division of Structural Biology, Wellcome Centre for Human Genetics, Roosevelt Drive, University of Oxford
- Chris A. O’Callaghan
- Henry Wellcome Building for Molecular Physiology, University of Oxford
- Persephone Borrow
- Nuffield Department of Medicine Research Building, Roosevelt Drive, Nuffield Department of Medicine, University of Oxford
- Mireille Toebes
- Department Molecular Oncology and Immunology, B6 Plesmanlaan 121
- Scott G. Hansen
- Vaccine and Gene Therapy Institute and Oregon National Primate Research Center, Oregon Health & Science University
- Jonah B Sacha
- Vaccine and Gene Therapy Institute and Oregon National Primate Research Center, Oregon Health & Science University
- Shaheed Abdulhaqq
- Vaccine and Gene Therapy Institute and Oregon National Primate Research Center, Oregon Health & Science University
- Justin M. Greene
- Vaccine and Gene Therapy Institute and Oregon National Primate Research Center, Oregon Health & Science University
- Klaus Früh
- Vaccine and Gene Therapy Institute and Oregon National Primate Research Center, Oregon Health & Science University
- Emily Marshall
- Vaccine and Gene Therapy Institute and Oregon National Primate Research Center, Oregon Health & Science University
- Louis J. Picker
- Vaccine and Gene Therapy Institute and Oregon National Primate Research Center, Oregon Health & Science University
- E. Yvonne Jones
- Division of Structural Biology, Wellcome Centre for Human Genetics, Roosevelt Drive, University of Oxford
- Andrew J. McMichael
- Nuffield Department of Medicine Research Building, Roosevelt Drive, Nuffield Department of Medicine, University of Oxford
- Geraldine M. Gillespie
- Nuffield Department of Medicine Research Building, Roosevelt Drive, Nuffield Department of Medicine, University of Oxford
- DOI
- https://doi.org/10.1038/s41467-018-05459-z
- Journal volume & issue
-
Vol. 9,
no. 1
pp. 1 – 13
Abstract
Human leucocyte antigen E (HLA-E) directly engages NK cells but also presents antigen to CD8+ T cells. Here the authors show crystal structures of HLA-E in complex with peptides derived from HIV and Mycobacterium tuberculosis, and describe binding conformations, the positional impact of residues involved and discuss implications for functional presentation to CD8+ T cells.
