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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...

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Updated: Jan 2, 2026

Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope

Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope

Published on: March 24, 2017

Cutting antigenic peptides down to size.

Kannan Natarajan¹, David H Margulies¹

¹Molecular Biology Section, Laboratory of Immune System Biology, NIAID, National Institutes of Health, Bethesda, Maryland 20892-1892.

The Journal of Biological Chemistry

|December 8, 2019

Summary

Aminopeptidases in the endoplasmic reticulum process peptides for antigen presentation. A study reveals how Major Histocompatibility Complex (MHC)-I adjusts its structure to allow aminopeptidase access to bound peptides, influencing cell surface display.

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Area of Science:

Immunology
Molecular Biology
Biophysics

Background:

Peptide processing by aminopeptidases in the endoplasmic reticulum is crucial for antigen presentation.
The role of these enzymes on peptides bound to Major Histocompatibility Complex (MHC)-I molecules remains unclear.

Purpose of the Study:

To investigate the structural and biophysical interactions between N-terminally extended peptides and MHC-I.
To elucidate the mechanism of aminopeptidase access to peptides presented by MHC-I.

Main Methods:

Structural analysis of peptide-MHC-I complexes.
Biophysical characterization of peptide binding and N-terminal exposure.

Main Results:

Major Histocompatibility Complex (MHC)-I undergoes conformational changes to accommodate N-terminally extended peptides.
These structural adjustments allow for both core peptide binding and exposure of the peptide's N terminus.
This mechanism dictates aminopeptidase access to the bound peptide.

Conclusions:

The study provides a mechanism explaining how aminopeptidases interact with peptides presented by MHC-I.
Findings offer insights into how longer peptides can be displayed on the cell surface, impacting immune recognition.