MHC class I molecules can direct proteolytic cleavage of antigenic precursors in the endoplasmic reticulum

Nathalie Brouwenstijn, Thomas Serwold, Nilabh Shastri

Research output: Contribution to journalArticlepeer-review

Abstract

The large set of peptides presented by MHC (major histocompatibility complex) class I molecules are generated by proteolysis of diverse precursors in the cytoplasm and possibly in the endoplasmic reticulum (ER). To define the potential peptide trimming events in the ER, we analyzed proteolytic products generated in isolated microsomes. The residues flanking the N terminus of the final antigenic peptide were rapidly removed within the microsomes but only in the presence of appropriate MHC molecules. Remarkably, the precursor peptide was bound to the MHC molecules in a distinct conformation and required an aminopeptidase activity to generate the optimal peptide. The MHC molecules are therefore not only the final repositories of antigenic peptides, but they can also direct their excision from longer precursors.

Original languageEnglish (US)
Pages (from-to)95-104
Number of pages10
JournalImmunity
Volume15
Issue number1
DOIs
StatePublished - 2001
Externally publishedYes

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology
  • Infectious Diseases

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