ArticleNature communications2014
Divergent paths for the selection of immunodominant epitopes from distinct antigenic sources.
Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed, 66 citations in OpenAlex.
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- Overview of multifunctional cysteinyl cathepsins in atherosclerosis-based cardiovascular disease: from insights into molecular functions to clinical implications.Cell & bioscience · 2023Review
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- Revisiting the Principles of Designing a Vaccine.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Role of Helical Structure in MBP Immunodominant Peptides for Efficient IgM Antibody Recognition in Multiple Sclerosis.Frontiers in chemistry · 2022Article
- Partnering for the major histocompatibility complex class II and antigenic determinant requires flexibility and chaperons.Current opinion in immunology · 2021Review
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- Lysosomal cathepsin creates chimeric epitopes for diabetogenic CD4 T cells via transpeptidation.The Journal of experimental medicine · 2021Article
- How Does B Cell Antigen Presentation Affect Memory CD4 T Cell Differentiation and Longevity?Frontiers in immunology · 2021Review
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- Article
- Multiple genetic programs contribute to CD4 T cell memory differentiation and longevity by maintaining T cell quiescence.Cellular immunology · 2020Article
- Formaldehyde treatment of proteins enhances proteolytic degradation by the endo-lysosomal protease cathepsin S.Scientific reports · 2020Article
- The love and hate relationship of HLA-DM/DO in the selection of immunodominant epitopes.Current opinion in immunology · 2020Review
- Cysteinyl cathepsins in cardiovascular diseases.Biochimica et biophysica acta. Proteins and proteomics · 2020Review
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
Abstract
Immunodominant epitopes are few selected epitopes from complex antigens that initiate T-cell responses. Here to provide further insights into this process, we use a reductionist cell-free antigen-processing system composed of defined components. We use the system to characterize steps in antigen processing of pathogen-derived proteins or autoantigens and we find distinct paths for peptide processing and selection. Autoantigen-derived immunodominant epitopes are resistant to digestion by cathepsins, whereas pathogen-derived epitopes are sensitive. Sensitivity to cathepsins enforces capture of pathogen-derived epitopes by major histocompatibility complex class II (MHC class II) before processing, and resistance to HLA-DM-mediated-dissociation preserves the longevity of those epitopes. We show that immunodominance is established by higher relative abundance of the selected epitopes, which survive cathepsin digestion either by binding to MHC class II and resisting DM-mediated-dissociation, or being chemically resistant to cathepsins degradation. Non-dominant epitopes are sensitive to both DM and cathepsins and are destroyed.
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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.