Special Seminar: Dr. Andrew McShan

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Summaries

Summary Sentence: Finding Cinderella’s Slipper:​ How Immunological Chaperones Charm Antigens onto the MHC-I to Fight Disease

Full Summary: Immune chaperones tapasin and TAPBPR associate with class I major histocompatibility complex (MHC-I) molecules to promote loading, exchange, and editing of peptide antigen cargo. The resulting peptide/MHC-I complexes display antigens to cytotoxic T cells on the cell surface for immune surveillance. Insights into peptide/MHC-I antigen presentation are important given that it is the most critical pathway used by the immune system to sense and respond to cancer, pathogen infection, and autoimmune disease. While several recently solved peptide-deficient MHC-I/chaperone structures provide important insights through static snapshots, a complete understanding of how immune chaperones contribute to antigen selection and presentation remains elusive. Here, using solution NMR and complementary biophysical assays, we investigate the molecular mechanism of peptide loading, selection, and exchange on the 90 kDa MHC-I/TAPBPR complex. We further explore the role of protein dynamics in shaping chaperone specificity towards different human MHC allotypes, which vary from person to person in the population and determine disease susceptibility. In addition, we uncover a functional role for a TAPBPR loop that directly senses and traps peptides antigen on the MHC-I groove. Finally, we examine whether TAPBPR contributes to metabolite antigen presentation by the non-classical MHC-I related molecule MR1 and compare our results to the classical peptide/MHC-I system. Together, our findings enable us to define similarities and differences utilized by immune chaperones to dictate peptide and metabolite antigen presentation by the MHC-I versus MR1. 

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School of Chemistry and Biochemistry

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Faculty/Staff, Public, Undergraduate students
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Status
  • Created By: arcs-stuweb03
  • Workflow Status: Published
  • Created On: Mar 9, 2022 - 1:57pm
  • Last Updated: Mar 9, 2022 - 2:18pm