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pubmed-article:8892091pubmed:abstractTextUnderstanding 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 alpha-chain. DRB1*0402 contained as the predominant peptide species a nested cluster from positions 129-145 of the HLA-B alpha-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.lld:pubmed
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pubmed-article:8892091pubmed:authorpubmed-author:YatesJ RJR3rdlld:pubmed
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pubmed-article:8892091pubmed:pagination795-802lld:pubmed
pubmed-article:8892091pubmed:dateRevised2011-11-17lld:pubmed
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pubmed-article:8892091pubmed:articleTitleAnalysis of naturally processed peptides eluted from HLA DRB1*0402 and *0404.lld:pubmed
pubmed-article:8892091pubmed:affiliationDepartment of Veterans Affairs Medical Center, Portland, OR 97207, USA.lld:pubmed
pubmed-article:8892091pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:8892091pubmed:publicationTypeResearch Support, U.S. Gov't, Non-P.H.S.lld:pubmed
pubmed-article:8892091pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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