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TitleCryoEM structure of an MHC-I/TAPBPR peptide-bound intermediate reveals the mechanism of antigen proofreading.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 122, Issue 2, Page e2416992122, Year 2025
Publish dateJan 14, 2025
AuthorsYi Sun / Ruth A Pumroy / Leena Mallik / Apala Chaudhuri / Chloe Wang / Daniel Hwang / Julia N Danon / Kimia Dasteh Goli / Vera Y Moiseenkova-Bell / Nikolaos G Sgourakis /
PubMed AbstractClass I major histocompatibility complex (MHC-I) proteins play a pivotal role in adaptive immunity by displaying epitopic peptides to CD8+ T cells. The chaperones tapasin and TAPBPR promote the ...Class I major histocompatibility complex (MHC-I) proteins play a pivotal role in adaptive immunity by displaying epitopic peptides to CD8+ T cells. The chaperones tapasin and TAPBPR promote the selection of immunogenic antigens from a large pool of intracellular peptides. Interactions of chaperoned MHC-I molecules with incoming peptides are transient in nature, and as a result, the precise antigen proofreading mechanism remains elusive. Here, we leverage a high-fidelity TAPBPR variant and conformationally stabilized MHC-I, to determine the solution structure of the human antigen editing complex bound to a peptide decoy by cryogenic electron microscopy (cryo-EM) at an average resolution of 3.0 Å. Antigen proofreading is mediated by transient interactions formed between the nascent peptide binding groove with the P2/P3 peptide anchors, where conserved MHC-I residues stabilize incoming peptides through backbone-focused contacts. Finally, using our high-fidelity chaperone, we demonstrate robust peptide exchange on the cell surface across multiple clinically relevant human MHC-I allomorphs. Our work has important ramifications for understanding the selection of immunogenic epitopes for T cell screening and vaccine design applications.
External linksProc Natl Acad Sci U S A / PubMed:39786927 / PubMed Central
MethodsEM (single particle)
Resolution3.0 Å
Structure data

45360

9c96

EMDB-45360, PDB-9c96:
Cryo-EM structure of TAP binding protein related (TAPBPR) in complex with HLA-A*02:01 bound to a suboptimal peptide.
Method: EM (single particle) / Resolution: 3.0 Å

Source
  • homo sapiens (human)
KeywordsIMMUNE SYSTEM / Antigen processing and presentation / TAP binding protein related / MHC-I / Chaperone

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