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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1992-1-27
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pubmed:abstractText |
We have characterized immunogenic epitopes of the 31-kDa outer surface protein A (OspA) protein of Borrelia burgdorferi, which is a major surface Ag of the spirochete causing Lyme disease. Full length and truncated forms of rOspA proteins were expressed in Escherichia coli, and their reactivities with antibodies and human T cell clones isolated from patients with Lyme disease were determined. The epitopes recognized by three of four OspA-reactive T cell clones are contained within the 60 COOH-terminal amino acids. Each of the four OspA-reactive T cell clones has a different HLA class II molecule involved in Ag recognition and recognizes a distinct epitope. One T cell clone promiscuously recognized an epitope in the context of different HLA-DQ molecules. In addition, the binding of a murine monoclonal anti-OspA antibody, as well as antibodies in sera of three of five patients with Lyme disease, was dependent upon the amino acids in the carboxy-terminal protion of this protein. Taken together, our results indicate that the 60 COOH-terminal amino acids of OspA contain epitopes recognized by human antibodies and T cells.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Outer Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Vaccines,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/HLA-D Antigens,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Oligodeoxyribonucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/OspA protein,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0022-1767
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
148
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pubmed:geneSymbol |
ospA
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
218-24
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1370170-Antibodies, Bacterial,
pubmed-meshheading:1370170-Antigen-Presenting Cells,
pubmed-meshheading:1370170-Antigens, Bacterial,
pubmed-meshheading:1370170-Antigens, Surface,
pubmed-meshheading:1370170-Bacterial Outer Membrane Proteins,
pubmed-meshheading:1370170-Bacterial Proteins,
pubmed-meshheading:1370170-Bacterial Vaccines,
pubmed-meshheading:1370170-Base Sequence,
pubmed-meshheading:1370170-Borrelia burgdorferi Group,
pubmed-meshheading:1370170-Clone Cells,
pubmed-meshheading:1370170-Epitopes,
pubmed-meshheading:1370170-HLA-D Antigens,
pubmed-meshheading:1370170-Lipoproteins,
pubmed-meshheading:1370170-Lyme Disease,
pubmed-meshheading:1370170-Lymphocyte Activation,
pubmed-meshheading:1370170-Molecular Sequence Data,
pubmed-meshheading:1370170-Oligodeoxyribonucleotides,
pubmed-meshheading:1370170-Recombinant Proteins,
pubmed-meshheading:1370170-T-Lymphocytes
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pubmed:year |
1992
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pubmed:articleTitle |
Epitopes on the outer surface protein A of Borrelia burgdorferi recognized by antibodies and T cells of patients with Lyme disease.
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pubmed:affiliation |
Department of Inflammation Biology, Syntex Research, Palo Alto, CA 94303.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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