http://rdf.ncbi.nlm.nih.gov/pubchem/patent/JP-2002501748-A
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filingDate | 1999-01-29-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
publicationDate | 2002-01-22-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
publicationNumber | JP-2002501748-A |
titleOfInvention | Methods and reagents for reducing allergic reactions |
abstract | (57) [Summary]nIt has been determined that allergens characterized by both a humoral (IgE) binding site and a cellular (T cell) binding site can be modified to be less allergic by modifying the IgE binding site. . The IgE binding site may be created by masking the site with a compound that interferes with IgE binding, or by as few as a single amino acid in the protein (most typically a hydrophobic residue relative to the center of the IgE binding epitope). ) Can be converted to a non-IgE binding site to eliminate IgE binding. This method allows the protein to remain outside of the IgE binding site while retaining the ability of the protein to activate T cells and, in some embodiments, by not significantly altering or reducing the ability to bind IgG. And let it be changed to the smallest possible. This example uses a peanut allergen to demonstrate alterations in the IgE binding site. The key amino acids within each IgE binding epitope of the peanut protein that are important for immunoglobulin binding have been determined. Even a single amino acid substitution within each epitope leads to loss of IgE binding. Although this epitope did not share a common amino acid sequence motif, the centrally located hydrophobic residue of this epitope appeared to be the most important for IgE binding. |
isCitedBy | http://rdf.ncbi.nlm.nih.gov/pubchem/patent/JP-2011505410-A http://rdf.ncbi.nlm.nih.gov/pubchem/patent/JP-2022524757-A http://rdf.ncbi.nlm.nih.gov/pubchem/patent/JP-7266700-B2 |
priorityDate | 1998-01-31-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
type | http://data.epo.org/linked-data/def/patent/Publication |
Incoming Links
Total number of triples: 108.