Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 113, Issue 8, Pages E1006-E1015Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1519894113
Keywords
antigen presentation; peptide loading; major histocompatibility complex; protein interactions; SAXS
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Funding
- DOE Office of Science [DE-AC02-06CH11357]
- National Institute of General Medical Sciences of the National Institutes of Health [9 P41 GM103622]
- National Institute of Allergy and Infectious Diseases [AI0000394]
- National Institute of Biomedical Imaging and Bioengineering/National Institutes of Health [EB000008]
- Center for Drug Evaluation and Review/Federal Drug Administration [1617]
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Peptide loading of major histocompatibility complex class I (MHC-I) molecules is central to antigen presentation, self-tolerance, and CD8(+) T-cell activation. TAP binding protein, related (TAPBPR), a widely expressed tapasin homolog, is not part of the classical MHC-I peptide-loading complex (PLC). Using recombinant MHC-I molecules, we show that TAPBPR binds HLA-A*02:01 and several other MHC-I molecules that are either peptide-free or loaded with low-affinity peptides. Fluorescence polarization experiments establish that TAPBPR augments peptide binding by MHC-I. The TAPBPR/MHC-I interaction is reversed by specific peptides, related to their affinity. Mutational and small-angle X-ray scattering (SAXS) studies confirm the structural similarities of TAPBPR with tapasin. These results support a role of TAPBPR in stabilizing peptide-receptive conformation(s) of MHC-I, permitting peptide editing.
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