pubmed-article:7678098 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:7678098 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
pubmed-article:7678098 | lifeskim:mentions | umls-concept:C0242632 | lld:lifeskim |
pubmed-article:7678098 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:7678098 | lifeskim:mentions | umls-concept:C0003316 | lld:lifeskim |
pubmed-article:7678098 | lifeskim:mentions | umls-concept:C0034857 | lld:lifeskim |
pubmed-article:7678098 | lifeskim:mentions | umls-concept:C0004572 | lld:lifeskim |
pubmed-article:7678098 | lifeskim:mentions | umls-concept:C0444659 | lld:lifeskim |
pubmed-article:7678098 | lifeskim:mentions | umls-concept:C1524063 | lld:lifeskim |
pubmed-article:7678098 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:7678098 | pubmed:dateCreated | 1993-1-29 | lld:pubmed |
pubmed-article:7678098 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7678098 | pubmed:abstractText | Previous studies have demonstrated the serologic and T-cell immunogenicity for cattle of a recombinant form of the apical complex-associated 77-kDa merozite protein of Babesia bovis, designated Bb-1. The present study characterizes the immunogenic epitopes of the Bb-1 protein. A series of recombinant truncated fusion proteins spanning the majority of the Bb-1 protein were expressed in Escherichia coli, and their reactivities with bovine peripheral blood mononuclear cells and T-cell clones derived from B. bovis-immune cattle and with rabbit antibodies were determined. Lymphocytes from two immune cattle were preferentially stimulated by the N-terminal half of the Bb-1 protein (amino acids 23 to 266, termed Bb-1A), localizing the T-cell epitopes to the Bb-1A portion of the molecule. CD4+ T-cell clones derived by stimulation with the intact Bb-1 fusion protein were used to identify two T-cell epitopes in the Bb-1A protein, consisting of amino acids SVVLLSAFSGN VWANEAEVSQVVK and FSDVDKTKSTEKT (residues 23 to 46 and 82 to 94). In contrast, rabbit antiserum raised against the intact fusion protein reacted only with the C-terminal half of the protein (amino acids 267 to 499, termed Bb-1B), which contained 28 tandem repeats of the tetrapeptide PAEK or PAET. Biological assays and Northern (RNA) blot analyses for cytokines revealed that following activation with concanavalin A, T-cell clones reactive against the two Bb-1A epitopes produced interleukin-2, gamma interferon, and tumor necrosis factors beta and alpha, but not interleukin-4, suggesting that the Bb-1 antigen preferentially stimulates the Th1 subset of CD4+ T cells in cattle. The studies described here report for the first time the characterization, by cytokine production, of the Th1 subset of bovine T cells and show that, as in mice, protozoal antigens can induce Th1 cells in ruminants. This first demonstration of B. bovis-encoded Th1 cell epitopes provides a rationale for incorporation of all or part of the Bb-1 protein into a recombinant vaccine. | lld:pubmed |
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pubmed-article:7678098 | pubmed:language | eng | lld:pubmed |
pubmed-article:7678098 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7678098 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:7678098 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7678098 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7678098 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7678098 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7678098 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7678098 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:7678098 | pubmed:month | Jan | lld:pubmed |
pubmed-article:7678098 | pubmed:issn | 0019-9567 | lld:pubmed |
pubmed-article:7678098 | pubmed:author | pubmed-author:BrownW CWC | lld:pubmed |
pubmed-article:7678098 | pubmed:author | pubmed-author:ZhaiYY | lld:pubmed |
pubmed-article:7678098 | pubmed:author | pubmed-author:Rice-FichtA... | lld:pubmed |
pubmed-article:7678098 | pubmed:author | pubmed-author:WoodsV MVM | lld:pubmed |
pubmed-article:7678098 | pubmed:author | pubmed-author:TrippC ACA | lld:pubmed |
pubmed-article:7678098 | pubmed:author | pubmed-author:DobbelaereD... | lld:pubmed |
pubmed-article:7678098 | pubmed:author | pubmed-author:HeusslerV TVT | lld:pubmed |
pubmed-article:7678098 | pubmed:author | pubmed-author:TetzlaffC LCL | lld:pubmed |
pubmed-article:7678098 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:7678098 | pubmed:volume | 61 | lld:pubmed |
pubmed-article:7678098 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:7678098 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:7678098 | pubmed:pagination | 236-44 | lld:pubmed |
pubmed-article:7678098 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:7678098 | pubmed:year | 1993 | lld:pubmed |
pubmed-article:7678098 | pubmed:articleTitle | Identification of two Th1 cell epitopes on the Babesia bovis-encoded 77-kilodalton merozoite protein (Bb-1) by use of truncated recombinant fusion proteins. | lld:pubmed |
pubmed-article:7678098 | pubmed:affiliation | Department of Veterinary Pathobiology, Texas A&M University, College Station 77843. | lld:pubmed |
pubmed-article:7678098 | pubmed:publicationType | Journal Article | lld:pubmed |