Antigen degradation or presentation by MHC class I molecules via classical and non-classical pathways.

Mol Immunol

Division of Tumor Biology, The Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX, Amsterdam, The Netherlands.

Published: October 2002

AI Article Synopsis

  • MHC class I molecules typically present endogenous peptides on the cell surface, relying on proteins like TAP and tapasin for this process.
  • Alternative pathways for peptide loading, particularly in cross-priming, offer significant insights into immune response mechanisms.
  • A key distinction between these pathways lies in the different proteases used for peptide generation, which affects peptide availability for immune responses.

Article Abstract

Major histocompatibility complex (MHC) class I molecules usually present endogenous peptides at the cell surface. This is the result of a cascade of events involving various dedicated proteins like the peptide transporter associated with antigen processing (TAP) and the ER chaperone tapasin. However, alternative ways for class I peptide loading exist which may be highly relevant in a process called cross-priming. Both pathways are described here in detail. One major difference between these pathways is that the proteases involved in the generation of peptides are different. How proteases and peptidases influence peptide generation and degradation will be discussed. These processes determine the amount of peptides available for TAP translocation and class I binding and ultimately the immune response.

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Source
http://dx.doi.org/10.1016/s0161-5890(02)00101-3DOI Listing

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