Abstract

Peptides extracted from HLA-A2.1 class I major histocompatibility complex (MHC) molecules expressed on the antigen processing mutant CEMx721.174.T2 were characterized by electrospray ionization-tandem mass spectrometry. Only seven dominant peptides were found, in contrast to over 200 associated with HLA-A2.1 on normal cells. These peptides were derived from the signal peptide domains of normal cellular proteins, were usually larger than nine residues, and were also associated with HLA-A2.1 in normal cells. These results suggest that proteolysis of signal peptide domains in the endoplasmic reticulum is a second mechanism for processing and presentation of peptides for association with class I molecules.

Keywords

Antigen processingAntigen presentationMajor histocompatibility complexHuman leukocyte antigenPeptideEndoplasmic reticulumMHC class ISignal peptideAntigenBiologyProteolysisMutantChemistryCell biologyMolecular biologyPeptide sequenceBiochemistryT cellGeneticsImmune systemGeneEnzyme

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Publication Info

Year
1992
Type
article
Volume
255
Issue
5049
Pages
1264-1266
Citations
527
Access
Closed

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Cite This

Robert Henderson, Hanspeter Michel, Kazuyasu Sakaguchi et al. (1992). HLA-A2.1-Associated Peptides from a Mutant Cell Line: A Second Pathway of Antigen Presentation. Science , 255 (5049) , 1264-1266. https://doi.org/10.1126/science.1546329

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DOI
10.1126/science.1546329