ArticleNature communications2012
Modification of the carboxy-terminal flanking region of a universal influenza epitope alters CD4⁺ T-cell repertoire selection.
Article in Nature communications, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
What it found
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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
23 citing papers in PubMed, 37 citations in OpenAlex.
- Whole-protein screening and multi-modal profiling of antigen-specific CD4Nature communications · 2026Article
- Contributions of the N-terminal flanking residues of an antigenic peptide from the Japanese cedar pollen allergen Cry j 1 to the T-cell activation by HLA-DP5.International immunology · 2023Article
- Blocking IAgLife sciences · 2022Article
- Molecular characterization of HLA class II binding to the LAG-3 T cell co-inhibitory receptor.European journal of immunology · 2021Article
- Immunoinformatic Analysis Reveals Antigenic Heterogeneity of Epstein-Barr Virus Is Immune-Driven.Frontiers in immunology · 2021Article
- CD4Cell reports · 2020Article
- Human leukocyte antigen (HLA) class II peptide flanking residues tune the immunogenicity of a human tumor-derived epitope.The Journal of biological chemistry · 2019Article
- Imprinting and Editing of the Human CD4 T Cell Response to Influenza Virus.Frontiers in immunology · 2019Article
- Epstein-Barr virus strain heterogeneity impairs human T-cell immunity.Cancer immunology, immunotherapy : CII · 2018Article
- Optimized Peptide-MHC Multimer Protocols for Detection and Isolation of Autoimmune T-Cells.Frontiers in immunology · 2018Article
- Quantification of HLA-DM-Dependent Major Histocompatibility Complex of Class II Immunopeptidomes by the Peptide Landscape Antigenic Epitope Alignment Utility.Frontiers in immunology · 2018Article
- Conserved Binding Regions Provide the Clue for Peptide-Based Vaccine Development: A Chemical Perspective.Molecules (Basel, Switzerland) · 2017Review
- Using X-ray Crystallography, Biophysics, and Functional Assays to Determine the Mechanisms Governing T-cell Receptor Recognition of Cancer Antigens.Journal of visualized experiments : JoVE · 2017Article
- Dual Molecular Mechanisms Govern Escape at Immunodominant HLA A2-Restricted HIV Epitope.Frontiers in immunology · 2017Article
- Peptide and Peptide-Dependent Motions in MHC Proteins: Immunological Implications and Biophysical Underpinnings.Frontiers in immunology · 2017Review
- Artificial antigen-presenting cells expressing HLA class II molecules as an effective tool for amplifying human specific memory CD4(+) T cells.Immunology and cell biology · 2016Article
- Enhanced Detection of Antigen-Specific CD4+ T Cells Using Altered Peptide Flanking Residue Peptide-MHC Class II Multimers.Journal of immunology (Baltimore, Md. : 1950) · 2015Article
- The versatility of the αβ T-cell antigen receptor.Protein science : a publication of the Protein Society · 2014Review
- T-cell receptor specificity maintained by altered thermodynamics.The Journal of biological chemistry · 2013Article
- CD4 T-cell memory responses to viral infections of humans show pronounced immunodominance independent of duration or viral persistence.Journal of virology · 2013Article
Corrections and comments
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Authors and funding
14 authors at 3 institutions in 2 countries.
Funding
Abstract
Human CD4(+) αβ T cells are activated via T-cell receptor recognition of peptide epitopes presented by major histocompatibility complex (MHC) class II (MHC-II). The open ends of the MHC-II binding groove allow peptide epitopes to extend beyond a central nonamer core region at both the amino- and carboxy-terminus. We have previously found that these non-bound C-terminal residues can alter T cell activation in an MHC allele-transcending fashion, although the mechanism for this effect remained unclear. Here we show that modification of the C-terminal peptide-flanking region of an influenza hemagglutinin (HA(305-320)) epitope can alter T-cell receptor binding affinity, T-cell activation and repertoire selection of influenza-specific CD4(+) T cells expanded from peripheral blood. These data provide the first demonstration that changes in the C-terminus of the peptide-flanking region can substantially alter T-cell receptor binding affinity, and indicate a mechanism through which peptide flanking residues could influence repertoire selection.
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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.