pubmed-article:1370170 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:1370170 | lifeskim:mentions | umls-concept:C0024198 | lld:lifeskim |
pubmed-article:1370170 | lifeskim:mentions | umls-concept:C0030705 | lld:lifeskim |
pubmed-article:1370170 | lifeskim:mentions | umls-concept:C0006034 | lld:lifeskim |
pubmed-article:1370170 | lifeskim:mentions | umls-concept:C0039194 | lld:lifeskim |
pubmed-article:1370170 | lifeskim:mentions | umls-concept:C0003241 | lld:lifeskim |
pubmed-article:1370170 | lifeskim:mentions | umls-concept:C0003316 | lld:lifeskim |
pubmed-article:1370170 | lifeskim:mentions | umls-concept:C0134235 | lld:lifeskim |
pubmed-article:1370170 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:1370170 | pubmed:dateCreated | 1992-1-27 | lld:pubmed |
pubmed-article:1370170 | 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. | lld:pubmed |
pubmed-article:1370170 | pubmed:language | eng | lld:pubmed |
pubmed-article:1370170 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1370170 | pubmed:citationSubset | AIM | lld:pubmed |
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pubmed-article:1370170 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:1370170 | pubmed:month | Jan | lld:pubmed |
pubmed-article:1370170 | pubmed:issn | 0022-1767 | lld:pubmed |
pubmed-article:1370170 | pubmed:author | pubmed-author:TurckC WCW | lld:pubmed |
pubmed-article:1370170 | pubmed:author | pubmed-author:YsselHH | lld:pubmed |
pubmed-article:1370170 | pubmed:author | pubmed-author:PeltzGG | lld:pubmed |
pubmed-article:1370170 | pubmed:author | pubmed-author:SoderbergCC | lld:pubmed |
pubmed-article:1370170 | pubmed:author | pubmed-author:ShanafeltM... | lld:pubmed |
pubmed-article:1370170 | pubmed:author | pubmed-author:AnzolaJJ | lld:pubmed |
pubmed-article:1370170 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:1370170 | pubmed:day | 1 | lld:pubmed |
pubmed-article:1370170 | pubmed:volume | 148 | lld:pubmed |
pubmed-article:1370170 | pubmed:geneSymbol | ospA | lld:pubmed |
pubmed-article:1370170 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:1370170 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:1370170 | pubmed:pagination | 218-24 | lld:pubmed |
pubmed-article:1370170 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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pubmed-article:1370170 | pubmed:year | 1992 | lld:pubmed |
pubmed-article:1370170 | pubmed:articleTitle | Epitopes on the outer surface protein A of Borrelia burgdorferi recognized by antibodies and T cells of patients with Lyme disease. | lld:pubmed |
pubmed-article:1370170 | pubmed:affiliation | Department of Inflammation Biology, Syntex Research, Palo Alto, CA 94303. | lld:pubmed |
pubmed-article:1370170 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:1370170 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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