Source:http://linkedlifedata.com/resource/pubmed/id/21820178
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
15-16
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pubmed:dateCreated |
2011-8-29
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pubmed:abstractText |
Der f 7 and Der p 7 are important house dust mite allergens with known structure and suggested biological function recently. However, their IgE-binding determinants remain unknown. The purpose of this study is to identify the IgE-reactive epitopes of Der f 7 and the determinants of IgE-mediated cross-reactivity between Der f 7 and Der p 7. IgE-reactive determinants were identified by immunodot blot inhibition using synthetic overlapping peptides, allergen mutants, and a Der f 7 structural model. Our results showed that synthetic peptides with sequence (156)SILDP(160) on Der f 7 bind IgE in two of the 30 asthmatic serum samples tested. Recombinant Der f 7 I157A, L158A, or D159A mutants have reduced IgE-binding activity. Inhibition experiments confirmed Asp159 as a critical core residue for IgE-binding. Among Der p 7, Der f 7 and Der f 7 mutants with single substitution between residues 156 and 160, only the D159A mutant cannot inhibit significantly IgE-binding against Der p 7. Therefore, Asp159 contributes to IgE-mediated cross-reactivity between Der f 7 and Der p 7. The structural model constructed for Der f 7 suggests that the IgE-binding epitope forms a loop-like structure on the surface of the molecule. In conclusion, Asp 159 is a critical core residue of an IgE-binding and IgE-mediated cross-reactive epitope (156)SILDP(160) of Der f 7. Results obtained from this study provide more information on molecular and structural features related to allergenicity, underlying basis of IgE cross-reactivity between allergens, and in designing safer immunotherapy.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Dermatophagoides,
http://linkedlifedata.com/resource/pubmed/chemical/Arthropod Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Aspartic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Dermatophagoides farinae antigen f 7,
http://linkedlifedata.com/resource/pubmed/chemical/Dermatophagoides pteronyssinus...,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes, B-Lymphocyte,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin E
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
1872-9142
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pubmed:author | |
pubmed:copyrightInfo |
Copyright © 2011 Elsevier Ltd. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:volume |
48
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2130-4
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:21820178-Antigens, Dermatophagoides,
pubmed-meshheading:21820178-Arthropod Proteins,
pubmed-meshheading:21820178-Aspartic Acid,
pubmed-meshheading:21820178-Base Sequence,
pubmed-meshheading:21820178-Cross Reactions,
pubmed-meshheading:21820178-Epitope Mapping,
pubmed-meshheading:21820178-Epitopes, B-Lymphocyte,
pubmed-meshheading:21820178-Humans,
pubmed-meshheading:21820178-Immunoblotting,
pubmed-meshheading:21820178-Immunoglobulin E,
pubmed-meshheading:21820178-Models, Molecular,
pubmed-meshheading:21820178-Molecular Sequence Data,
pubmed-meshheading:21820178-Mutagenesis, Site-Directed,
pubmed-meshheading:21820178-Mutation,
pubmed-meshheading:21820178-Protein Conformation
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pubmed:year |
2011
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pubmed:articleTitle |
Asp159 is a critical core amino acid of an IgE-binding and cross-reactive epitope of a dust mite allergen Der f 7.
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pubmed:affiliation |
Department of Medical Research and Education, Taipei Veterans General Hospital, Shih-Pai, Taipei 11217, Taiwan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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