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Updated: Aug 9, 2026

A High Throughput MHC II Binding Assay for Quantitative Analysis of Peptide Epitopes
Published on: March 25, 2014
Efficiency of MHC class I antigen processing: a quantitative analysis
M S Villanueva1, P Fischer, K Feen
1Section of Infectious Diseases, Yale School of Medicine, New Haven, Connecticut 06520-8022.
Listeria monocytogenes antigen processing efficiency was studied. Approximately 35 p60 molecules degrade to yield one cytotoxic T lymphocyte epitope, revealing insights into the MHC class I pathway.
Area of Science:
- Immunology
- Microbiology
- Molecular Biology
Background:
- Listeria monocytogenes is an intracellular pathogen.
- p60 is a secreted murein hydrolase processed into a T cell epitope.
- The H-2Kd MHC class I molecule presents the p60 epitope to T cells.
Purpose of the Study:
- To quantify the efficiency of antigen processing for the L. monocytogenes p60 protein.
- To investigate the relationship between intracellular antigen quantity and epitope production.
- To understand the capacity of the MHC class I antigen processing pathway.
Main Methods:
- Utilized L. monocytogenes strains with varying p60 secretion levels.
- Monitored the production and degradation rates of p60 and its epitope.
- Calculated antigen processing efficiency based on secretion and degradation kinetics.
Main Results:
- p60 217-225 epitope production rate is directly proportional to intracellular antigen load.
- Epitope generation is linked to the degradation of newly synthesized p60.
- Estimated that ~35 p60 molecules degrade to produce one p60 217-225 epitope.
Conclusions:
- Provides an estimate for the efficiency of antigen processing in the MHC class I pathway.
- Suggests the MHC class I pathway can accommodate foreign antigens.
- Highlights the quantitative aspects of intracellular antigen processing for T cell recognition.
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