ArticleThe Journal of experimental medicine2006
Enhancing immunogenicity by limiting susceptibility to lysosomal proteolysis.
Article in The Journal of experimental medicine, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 105 papers.
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Who cites it
105 citing papers in PubMed.
- Rationally designed minimized TbpB confers broad protection against meningococcal infection.PLoS pathogens · 2026Article
- Proteomic Analysis of Paraffin-Embedded Intestines fromProteomes · 2026Article
- Mucosal vaccination with enzymatically activeFrontiers in microbiology · 2026Article
- The optimized endolysosomal degradation assay with standardized enzyme activity represents an orthogonal method for predicting protein immunogenicity and T cell epitopes.Frontiers in allergy · 2026Article
- Conformational bias in SARS-CoV-2 Spike CD4+ T-cell epitope dominance.Frontiers in immunology · 2026Article
- Modulating antigen processing through metal-organic frameworks to bias adaptive immunity.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Cell-Free Expression of Nipah Virus Transmembrane Proteins for Proteoliposome Vaccine Design.ACS nano · 2025Article
- Conformational stability of hemocyanins regulates their lysosomal and proteasomal degradation, influencing their pro-inflammatory effects on mammalian antigen-presenting cells.Frontiers in immunology · 2025Article
- Bioinformatics Analysis and Immunogenicity Assessment of the Novel Multi-Stage DNA Vaccine W541 Against Mycobacterium Tuberculosis.Immunity, inflammation and disease · 2024Article
- Development of a hydrogen peroxide-inactivated vaccine that protects against viscerotropic yellow fever in a non-human primate model.Cell reports. Medicine · 2024Article
- Efferocytosis in dendritic cells: an overlooked immunoregulatory process.Frontiers in immunology · 2024Review
- Article
- The transcription factor Zeb1 controls homeostasis and function of type 1 conventional dendritic cells.Nature communications · 2023Article
- Design and Characterization of a Multistage Peptide-Based Vaccine Platform to TargetBioconjugate chemistry · 2023Article
- Structural Framework for Analysis of CD4+ T-Cell Epitope Dominance in Viral Fusion Proteins.Biochemistry · 2023Review
- A Nanovaccine Based on Adjuvant Peptide FK-13 and l-Phenylalanine Poly(ester amide) Enhances CD8Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
- Review
- CD4+ T-Cell Epitope Prediction by Combined Analysis of Antigen Conformational Flexibility and Peptide-MHCII Binding Affinity.Biochemistry · 2022Article
- Development of a Liquid Chromatography and High-Resolution and -Accuracy Mass Spectrometry Method to Evaluate New Biotherapeutic Entity Processing in Human Liver Lysosomes.ImmunoHorizons · 2022Article
- Lysosomes and lysosome-related organelles in immune responses.FEBS open bio · 2022Review
45 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
T cells recognize protein antigens as short peptides processed and displayed by antigen-presenting cells. However, the mechanism of peptide selection is incompletely understood, and, consequently, the differences in the immunogenicity of protein antigens remain largely unpredictable and difficult to manipulate. In this paper we show that the susceptibility of protein antigens to lysosomal proteolysis plays an important role in determining immunogenicity in vivo. We compared the immunogenicity of proteins with the same sequence (same T cell epitopes) and structure (same B cell epitopes) but with different susceptibilities to lysosomal proteolysis. After immunizing mice with each of the proteins adsorbed onto aluminum hydroxide as adjuvant, we measured serum IgG responses as a physiological measure of the antigen's ability to be presented on major histocompatibility complex class II molecules and to prime CD4+ T cells in vivo. For two unrelated model antigens (RNase and horseradish peroxidase), we found that only the less digestible forms were immunogenic, inducing far more efficient T cell priming and antibody responses. These findings suggest that stability to lysosomal proteolysis may be an important factor in determining immunogenicity, with potential implications for vaccine design.
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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.