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Antigen Processing Pathways

Antigen Processing Pathways

MHC molecules are key players in the immune response, enabling T cells to recognize and respond to specific antigens. They are present on the surface of all nucleated cells in the body and are instrumental in presenting antigens to T cells and activating them. T cells recognize the MHC-antigen complex and initiate an immune response. MHC class I and MHC class II are two main types of MHC molecules, each associated with a distinct antigen processing pathway.
MHC Class I: Presenting Endogenous...

Antigens Involved in Adaptive Immunity

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An antigen is any substance the immune system identifies as foreign and potentially harmful to the body, prompting an immune response. Antigens have two functional properties: immunogenicity and reactivity. Immunogenicity is the ability of an antigen to stimulate a specific immune response. At the same time, reactivity describes the antigen's ability to react with the cells and antibodies produced in response to it.
Complete Antigens
Complete antigens possess both immunogenicity and reactivity.

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Related Experiment Video

Updated: May 28, 2026

Immunopeptidomics: Isolation of Mouse and Human MHC Class I- and II-Associated Peptides for Mass Spectrometry Analysis

Immunopeptidomics: Isolation of Mouse and Human MHC Class I- and II-Associated Peptides for Mass Spectrometry Analysis

Published on: October 15, 2021

A peptide filtering relation quantifies MHC class I peptide optimization.

Neil Dalchau¹, Andrew Phillips, Leonard D Goldstein

¹Biological Computation Group, Microsoft Research, Cambridge, United Kingdom. ndalchau@microsoft.com

Plos Computational Biology

|October 25, 2011

Summary

This summary is machine-generated.

This study models how Major Histocompatibility Complex (MHC) class I molecules optimize peptide presentation. The model reveals tapasin enhances this process by improving peptide unbinding, crucial for immune responses and vaccination strategies.

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Last Updated: May 28, 2026

Immunopeptidomics: Isolation of Mouse and Human MHC Class I- and II-Associated Peptides for Mass Spectrometry Analysis

Immunopeptidomics: Isolation of Mouse and Human MHC Class I- and II-Associated Peptides for Mass Spectrometry Analysis

Published on: October 15, 2021

A High Throughput MHC II Binding Assay for Quantitative Analysis of Peptide Epitopes

A High Throughput MHC II Binding Assay for Quantitative Analysis of Peptide Epitopes

Published on: March 25, 2014

Peptide:MHC Tetramer-based Enrichment of Epitope-specific T cells

Peptide:MHC Tetramer-based Enrichment of Epitope-specific T cells

Published on: October 22, 2012

Area of Science:

Immunology
Computational Biology
Molecular Biology

Background:

Major Histocompatibility Complex (MHC) class I molecules present intracellular peptides to cytotoxic T lymphocytes, crucial for immune surveillance.
Peptide optimization by MHC class I determines which peptides are presented, influencing immune response efficacy, immune evasion, and vaccine success.

Purpose of the Study:

To develop a dynamical systems model of peptide optimization by MHC class I.
To investigate the role of the chaperone molecule tapasin in enhancing peptide optimization.
To quantify peptide optimization and predict cell surface peptide abundance.

Main Methods:

Developed a dynamical systems model for MHC class I peptide optimization.
Incorporated the chaperone molecule tapasin into the model.
Parameterized the model using experimental data to derive a peptide filtering relation.

Main Results:

The peptide filtering relation quantifies optimization based on peptide supply and unbinding rates.
Tapasin enhances peptide optimization by increasing peptide unbinding without delaying MHC transit.
Allele-specific peptide binding differences explain variations in peptide optimization across MHC class I alleles.

Conclusions:

The model provides a quantitative basis for understanding and predicting peptide optimization by MHC class I.
This framework can be applied to investigate viral infections and diseases at the cellular level.
Simulations demonstrated optimization of peptides from Human Immunodeficiency Virus Gag-Pol polyprotein.