pubmed-article:11641259 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:11641259 | lifeskim:mentions | umls-concept:C0087111 | lld:lifeskim |
pubmed-article:11641259 | lifeskim:mentions | umls-concept:C0020517 | lld:lifeskim |
pubmed-article:11641259 | lifeskim:mentions | umls-concept:C0332307 | lld:lifeskim |
pubmed-article:11641259 | lifeskim:mentions | umls-concept:C0020846 | lld:lifeskim |
pubmed-article:11641259 | lifeskim:mentions | umls-concept:C0162768 | lld:lifeskim |
pubmed-article:11641259 | pubmed:issue | 13 | lld:pubmed |
pubmed-article:11641259 | pubmed:dateCreated | 2001-11-5 | lld:pubmed |
pubmed-article:11641259 | pubmed:abstractText | By screening phage display random peptide libraries with purified immunoglobulin E (IgE) from birch pollen-allergic patients, we previously defined peptides mimicking natural IgE epitopes (mimotopes) of the major birch pollen allergen Bet v 1. The present study aimed to define a monovalent carrier for the IgE mimotopes to induce protective antibodies directed to the IgE epitopes, suitable for mimotope-specific therapy. We expressed the selected mimotopes as fusion proteins together with streptococcal albumin binding protein (ABP). The fusion proteins were recognized specifically by anti-Bet v 1 human IgE, which demonstrated that the mimotopes fused to ABP resemble the natural IgE epitope. Bet v 1-specific IgG was induced by immunization of BALB/c mice with fusion proteins. These IgG antibodies could inhibit IgE binding to Bet v 1. Skin testing of Bet v 1 allergic mice showed that the ABP mimotope constructs did not elicit type I skin reactions, although they possess IgE binding structures. Our data suggest that IgE mimotopes are safe for epitope-specific immunotherapy of sensitized individuals, when presented in a monovalent form. Therefore, ABP-fused mimotopes are promising candidates for a new type of immunotherapy based on the precise induction of blocking antibodies. | lld:pubmed |
pubmed-article:11641259 | pubmed:language | eng | lld:pubmed |
pubmed-article:11641259 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11641259 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:11641259 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11641259 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11641259 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11641259 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11641259 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11641259 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11641259 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11641259 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11641259 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11641259 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11641259 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11641259 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11641259 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11641259 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:11641259 | pubmed:month | Nov | lld:pubmed |
pubmed-article:11641259 | pubmed:issn | 1530-6860 | lld:pubmed |
pubmed-article:11641259 | pubmed:author | pubmed-author:ScheinerOO | lld:pubmed |
pubmed-article:11641259 | pubmed:author | pubmed-author:Boltz-Nitules... | lld:pubmed |
pubmed-article:11641259 | pubmed:author | pubmed-author:SuterMM | lld:pubmed |
pubmed-article:11641259 | pubmed:author | pubmed-author:SchöllII | lld:pubmed |
pubmed-article:11641259 | pubmed:author | pubmed-author:BreitenederHH | lld:pubmed |
pubmed-article:11641259 | pubmed:author | pubmed-author:BaumannSS | lld:pubmed |
pubmed-article:11641259 | pubmed:author | pubmed-author:Jensen-Jaroli... | lld:pubmed |
pubmed-article:11641259 | pubmed:author | pubmed-author:WiedermannUU | lld:pubmed |
pubmed-article:11641259 | pubmed:author | pubmed-author:HafnerCC | lld:pubmed |
pubmed-article:11641259 | pubmed:author | pubmed-author:GanglbergerEE | lld:pubmed |
pubmed-article:11641259 | pubmed:author | pubmed-author:Barbara... | lld:pubmed |
pubmed-article:11641259 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:11641259 | pubmed:volume | 15 | lld:pubmed |
pubmed-article:11641259 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:11641259 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:11641259 | pubmed:pagination | 2524-6 | lld:pubmed |
pubmed-article:11641259 | pubmed:dateRevised | 2011-6-21 | lld:pubmed |
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pubmed-article:11641259 | pubmed:year | 2001 | lld:pubmed |
pubmed-article:11641259 | pubmed:articleTitle | Monovalent fusion proteins of IgE mimotopes are safe for therapy of type I allergy. | lld:pubmed |
pubmed-article:11641259 | pubmed:affiliation | Department of Pathophysiology, University of Vienna, A-1090 Vienna, Austria. | lld:pubmed |
pubmed-article:11641259 | pubmed:publicationType | Journal Article | lld:pubmed |
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