ArticleProceedings of the National Academy of Sciences of the United States of America2024
Principles of peptide selection by the transporter associated with antigen processing.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Architectural principles of transporter-chaperone coupling within the native MHC I peptide-loading complex.Science advances · 2026Article
- Artificial intelligence in peptide cancer vaccine design: from neoantigen discovery to immunogenicity prediction.Frontiers in genetics · 2026Review
- Identification of novel HLA class I-restricted hepatitis B virus peptides and their modulation by peptide editor TAPBPR.Frontiers in immunology · 2026Article
- Harnessing alternative splicing for off-the-shelf mRNA neoantigen vaccines in hepatocellular carcinoma.Cell research · 2025Article
- Selective HLA knockdown and PD-L1 expression prevent allogeneic CAR-NK cell rejection and enhance safety and anti-tumor responses in xenograft mice.Nature communications · 2025Article
- TAP1 promotes immune escape by activating JNK/STAT1/PD-L1 signaling in EBV-associated gastric cancer.Molecular and cellular biochemistry · 2025Article
- Structurally diverse viral inhibitors converge on a shared mechanism to stall the antigen transporter TAP.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Article
- Nucleotide-dependent conformational changes direct peptide export by the transporter associated with antigen processing.Immunity · 2025Article
- Proteasome-derived peptides: separating the trash from the recycling.Trends in biochemical sciences · 2025Review
- Harnessing an integrated glyco-nanovaccine technology for enhanced cancer immunotherapy.Communications medicine · 2025Article
- The biophysical requirements that govern the efficient endosomal escape of designed mini-proteins.Nature chemistry · 2025Article
- Structural Basis for Oxidized Glutathione Recognition by Yeast Cadmium Factor 1.Journal of the American Chemical Society · 2025Article
- A Structural Atlas of TAP Inhibition by Herpesviruses and Poxviruses.bioRxiv : the preprint server for biology · 2025Article
- Neoantigens in cancer immunoediting: from mechanisms to personalized vaccines in breast cancer.Frontiers in cell and developmental biology · 2025Review
- Computational biology and artificial intelligence in mRNA vaccine design for cancer immunotherapy.Frontiers in cellular and infection microbiology · 2024Review
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Authors and funding
4 authors.
Funding
Abstract
Our ability to fight pathogens relies on major histocompatibility complex class I (MHC-I) molecules presenting diverse antigens on the surface of diseased cells. The transporter associated with antigen processing (TAP) transports nearly the entire repertoire of antigenic peptides into the endoplasmic reticulum for MHC-I loading. How TAP transports peptides specific for MHC-I is unclear. In this study, we used cryo-EM to determine a series of structures of human TAP, both in the absence and presence of peptides with various sequences and lengths. The structures revealed that peptides of eight or nine residues in length bind in a similarly extended conformation, despite having little sequence overlap. We also identified two peptide-anchoring pockets on either side of the transmembrane cavity, each engaging one end of a peptide with primarily main chain atoms. Occupation of both pockets results in a global conformational change in TAP, bringing the two halves of the transporter closer together to prime it for isomerization and ATP hydrolysis. Shorter peptides are able to bind to each pocket separately but are not long enough to bridge the cavity to bind to both simultaneously. Mutations that disrupt hydrogen bonds with the N and C termini of peptides almost abolish MHC-I surface expression. Our findings reveal that TAP functions as a molecular caliper that selects peptides according to length rather than sequence, providing antigen diversity for MHC-I presentation.
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