Ontology type: schema:ScholarlyArticle Open Access: True
2019-12
AUTHORSSze Lei Pang, Kok Lian Ho, Jitka Waterman, Robert Paul Rambo, Aik-Hong Teh, Indran Mathavan, Gemma Harris, Konstantinos Beis, Yee-How Say, Matta Sri Anusha, Yang Yie Sio, Fook Tim Chew, Chyan Leong Ng
ABSTRACTGroup 21 and 5 allergens are homologous house dust mite proteins known as mid-tier allergens. To reveal the biological function of group 21 allergens and to understand better the allergenicity of the rDer f 21 allergen, we determined the 1.5 Å crystal structure of rDer f 21 allergen from Dermatophagoides farinae. The rDer f 21 protein consists of a three helical bundle, similar to available structures of group 21 and homologous group 5 allergens. The rDer f 21 dimer forms a hydrophobic binding pocket similar to the one in the Der p 5 allergen, which indicates that both of the homologous groups could share a similar function. By performing structure-guided mutagenesis, we mutated all 38 surface-exposed polar residues of the rDer f 21 allergen and carried out immuno-dot blot assays using 24 atopic sera. Six residues, K10, K26, K42, E43, K46, and K48, which are located in the region between the N-terminus and the loop 1 of rDer f 21 were identified as the major IgE epitopes of rDer f 21. Epitope mapping of all potential IgE epitopes on the surface of the rDer f 21 crystal structure revealed heterogeneity in the sIgE recognition of the allergen epitopes in atopic individuals. The higher the allergen-sIgE level of an individual, the higher the number of epitope residues that are found in the allergen. The results illustrate the clear correlation between the number of specific major epitope residues in an allergen and the sIgE level of the atopic population. More... »
PAGES4933
http://scigraph.springernature.com/pub.10.1038/s41598-019-40879-x
DOIhttp://dx.doi.org/10.1038/s41598-019-40879-x
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PUBMEDhttps://www.ncbi.nlm.nih.gov/pubmed/30894561
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"type": "PropertyValue",
"value": [
"10.1038/s41598-019-40879-x"
]
},
{
"name": "dimensions_id",
"type": "PropertyValue",
"value": [
"pub.1112874290"
]
}
],
"sameAs": [
"https://doi.org/10.1038/s41598-019-40879-x",
"https://app.dimensions.ai/details/publication/pub.1112874290"
],
"sdDataset": "articles",
"sdDatePublished": "2019-04-11T13:28",
"sdLicense": "https://scigraph.springernature.com/explorer/license/",
"sdPublisher": {
"name": "Springer Nature - SN SciGraph project",
"type": "Organization"
},
"sdSource": "s3://com-uberresearch-data-dimensions-target-20181106-alternative/cleanup/v134/2549eaecd7973599484d7c17b260dba0a4ecb94b/merge/v9/a6c9fde33151104705d4d7ff012ea9563521a3ce/jats-lookup/v90/0000000370_0000000370/records_46741_00000003.jsonl",
"type": "ScholarlyArticle",
"url": "https://www.nature.com/articles/s41598-019-40879-x"
}
]Download the RDF metadata as: json-ld nt turtle xml License info
JSON-LD is a popular format for linked data which is fully compatible with JSON.
curl -H 'Accept: application/ld+json' 'https://scigraph.springernature.com/pub.10.1038/s41598-019-40879-x'
N-Triples is a line-based linked data format ideal for batch operations.
curl -H 'Accept: application/n-triples' 'https://scigraph.springernature.com/pub.10.1038/s41598-019-40879-x'
Turtle is a human-readable linked data format.
curl -H 'Accept: text/turtle' 'https://scigraph.springernature.com/pub.10.1038/s41598-019-40879-x'
RDF/XML is a standard XML format for linked data.
curl -H 'Accept: application/rdf+xml' 'https://scigraph.springernature.com/pub.10.1038/s41598-019-40879-x'
This table displays all metadata directly associated to this object as RDF triples.
319 TRIPLES
21 PREDICATES
80 URIs
21 LITERALS
9 BLANK NODES