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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
1997-3-14
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pubmed:abstractText |
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 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.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/HLA-DR Antigens,
http://linkedlifedata.com/resource/pubmed/chemical/HLA-DRB1*04:02 antigen,
http://linkedlifedata.com/resource/pubmed/chemical/HLA-DRB1 Chains,
http://linkedlifedata.com/resource/pubmed/chemical/Histocompatibility Antigens Class I,
http://linkedlifedata.com/resource/pubmed/chemical/Histocompatibility Antigens Class II,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0360-4012
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
45
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
795-802
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:8892091-B-Lymphocytes,
pubmed-meshheading:8892091-Cell Line, Transformed,
pubmed-meshheading:8892091-Chromatography, High Pressure Liquid,
pubmed-meshheading:8892091-Electrophoresis,
pubmed-meshheading:8892091-HLA-DR Antigens,
pubmed-meshheading:8892091-HLA-DRB1 Chains,
pubmed-meshheading:8892091-Histocompatibility Antigens Class I,
pubmed-meshheading:8892091-Histocompatibility Antigens Class II,
pubmed-meshheading:8892091-Humans,
pubmed-meshheading:8892091-Mass Spectrometry,
pubmed-meshheading:8892091-Peptides
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pubmed:year |
1996
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pubmed:articleTitle |
Analysis of naturally processed peptides eluted from HLA DRB1*0402 and *0404.
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pubmed:affiliation |
Department of Veterans Affairs Medical Center, Portland, OR 97207, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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