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Analysis of naturally processed peptides eluted from HLA DRB1 *0402 and *0404
Author(s) -
Hayden J.B.,
McCormack A.L.,
Yates J.R.,
Davey M.P.
Publication year - 1996
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/(sici)1097-4547(19960915)45:6<795::aid-jnr16>3.0.co;2-v
Subject(s) - peptide , major histocompatibility complex , edman degradation , human leukocyte antigen , mhc class ii , biology , mhc class i , peptide sequence , chemistry , microbiology and biotechnology , antigen , biochemistry , genetics , gene
Understanding the structural features of naturally processed peptides found within the major histocompatibility complex (MHC) class II peptide binding groove from disease‐associated MHC molecules may provide insights into the nature of potential disease‐related antigens. Class II MHC/peptide complexes were purified by immunoaffinity from transformed B cell lines homozygous for DRB1*0404 (an allele associated with rheumatoid arthritis) and *0402 (a closely related allele not associated with this disease). Peptides were eluted at acidic pH, fractionated by reversed phase HPLC, and analyzed by capillary electrophoresis. Those fractions containing a single dominant peptide were sequenced by automated Edman degradation and tandem mass spectrometry. The predominant peptide species identified came from non‐polymorphic regions of the HLA class I molecules expressed by each cell line. Peptides from DRB1*0404 were found to be nested clusters derived from positions 26–43 of the HLA‐B and ‐C α‐chain. DRB1*0402 contained as the predominant peptide species a nested cluster from positions 129–145 of the HLA‐B α‐chain. The primary structure of the class I derived peptides was consistent with that seen by peptides exhibiting promiscuous DR binding behavior. Processing of MHC‐derived peptides by MHC class II molecules is a common occurrence in the transformed B cell lines analyzed. © 1996 Wiley‐Liss, Inc.