ArticleJournal of virology2014
The immunodominant influenza A virus M158-66 cytotoxic T lymphocyte epitope exhibits degenerate class I major histocompatibility complex restriction in humans.
Article in Journal of virology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
26 citing papers in PubMed, 39 citations in OpenAlex.
- The challenge and promise of studying human antigen-specific T cells.Nature reviews. Immunology · 2026Review
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- TRAP: a contrastive learning-enhanced framework for robust TCR-pMHC binding prediction with improved generalizability.Chemical science · 2025Article
- Influenza Virus-Derived CD8 T Cell Epitopes: Implications for the Development of Universal Influenza Vaccines.Immune network · 2024Review
- Polyanhydride nanovaccine against H3N2 influenza A virus generates mucosal resident and systemic immunity promoting protection.NPJ vaccines · 2024Article
- CD8Nature communications · 2024Article
- Validation of Multi-epitope Peptides Encapsulated in PLGA Nanoparticles Against Influenza A Virus.Pharmaceutical research · 2023Article
- Shared graft-versus-leukemia minor histocompatibility antigens in DISCOVeRY-BMT.Blood advances · 2023Article
- Review
- Article
- Article
- CAR-T cells targeting a nucleophosmin neoepitope exhibit potent specific activity in mouse models of acute myeloid leukaemia.Nature biomedical engineering · 2021Article
- High-affinity oligoclonal TCRs define effective adoptive T cell therapy targeting mutant KRAS-G12D.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Deep Mutational Scan of the Highly Conserved Influenza A Virus M1 Matrix Protein Reveals Substantial Intrinsic Mutational Tolerance.Journal of virology · 2019Article
- Article
- Article
- The molecular basis for peptide repertoire selection in the human leucocyte antigen (HLA) C*06:02 molecule.The Journal of biological chemistry · 2017Article
- TCR-like antibodies mediate complement and antibody-dependent cellular cytotoxicity against Epstein-Barr virus-transformed B lymphoblastoid cells expressing different HLA-A*02 microvariants.Scientific reports · 2017Article
- Structural and regulatory diversity shape HLA-C protein expression levels.Nature communications · 2017Article
- Broad TCR repertoire and diverse structural solutions for recognition of an immunodominant CD8Nature structural & molecular biology · 2017Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
unlabelledCytotoxic T lymphocytes recognizing conserved peptide epitopes are crucial for protection against influenza A virus (IAV) infection. The CD8 T cell response against the M158-66 (GILGFVFTL) matrix protein epitope is immunodominant when restricted by HLA-A*02, a major histocompatibility complex (MHC) molecule expressed by approximately half of the human population. Here we report that the GILGFVFTL peptide is restricted by multiple HLA-C*08 alleles as well. We observed that M158-66 was able to elicit cytotoxic T lymphocyte (CTL) responses in both HLA-A*02- and HLA-C*08-positive individuals and that GILGFVFTL-specific CTLs in individuals expressing both restriction elements were distinct and not cross-reactive. The crystal structure of GILGFVFTL-HLA-C*08:01 was solved at 1.84 Å, and comparison with the known GILGFVFTL-HLA-A*02:01 structure revealed that the antigen bound both complexes in near-identical conformations, accommodated by binding pockets shaped from shared as well as unique residues. This discovery of degenerate peptide presentation by both HLA-A and HLA-C allelic variants eliciting unique CTL responses to IAV infection contributes fundamental knowledge with important implications for vaccine development strategies. IMPORTANCE: The presentation of influenza A virus peptides to elicit immunity is thought to be narrowly restricted, with a single peptide presented by a specific HLA molecule. In this study, we show that the same influenza A virus peptide can be more broadly presented by both HLA-A and HLA-C molecules. This discovery may help to explain the differences in immunity to influenza A virus between individuals and populations and may also aid in the design of vaccines.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.