Characterization of Peptides Bound to the Class I MHC Molecule HLA-A2.1 by Mass Spectrometry

Abstract

Antigens recognized by T cells are expressed as peptides bound to major histocompatibility complex (MHC) molecules. Microcapillary high-performance liquid chromatography-electrospray ionization-tandem mass spectrometry was used to fractionate and sequence subpicomolar amounts of peptides isolated from the MHC molecule HLA-A2.1. Of 200 different species quantitated, eight were sequenced and four were found in cellular proteins. All were nine residues long and shared a distinct structural motif. The sensitivity and speed of this approach should enhance the analysis of peptides from small quantities of virally infected and transformed cells as well as those associated with autoimmune disease states.

Keywords

Major histocompatibility complexElectrospray ionizationHuman leukocyte antigenTandem mass spectrometryChemistryMass spectrometryPeptideHistocompatibilityElectrosprayAntigenBiologyBiochemistryChromatographyGeneticsGene

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Publication Info

Year: 1992
Type: letter
Volume: 255
Issue: 5049
Pages: 1261-1263
Citations: 1194
Access: Closed

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APA Style

                            
                                
                                    Donald F. Hunt, 
                                
                                    Robert Henderson, 
                                
                                    Jeffrey Shabanowitz
                                
                                et al.
                            
                            (1992). 
                            Characterization of Peptides Bound to the Class I MHC Molecule HLA-A2.1 by Mass Spectrometry. 
                            Science
                            , 255
                            (5049)
                            , 1261-1263.
                            https://doi.org/10.1126/science.1546328
                        

Identifiers

DOI: 10.1126/science.1546328