Source:http://linkedlifedata.com/resource/pubmed/id/11717185
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
12
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| pubmed:dateCreated |
2001-11-21
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| pubmed:abstractText |
Accurate diagnosis of mosquito allergy has been precluded by the difficulty of obtaining salivary allergens. In this study, we expressed, purified, characterized and investigated the clinical relevance of a recombinant Aedes aegypti salivary allergen, rAed a 1. Two cDNA segments were ligated together to form the full-length Aed a 1 gene. rAed a 1 was expressed using a baculovirus/insect cell system, and purified using a combination of anion-exchange and gel-filtration chromatography. The purified rAed a 1 bound to human IgE, as detected by ELISA, ELISA inhibition tests and immunoblot analyses. Epicutaneous tests with rAed a 1 and a commercial whole-body AE: aegypti extract, and AE: aegypti bite tests were performed in 48 subjects. Nine of 31 (29%) of the subjects with positive immediate bite tests also had a positive rAed a 1 immediate skin reaction and 32% had an positive immediate test to the commercial extract. Six of 33 (18%) of the subjects with positive delayed bite tests also had a positive rAed a 1 delayed skin reaction and 6% had a positive delayed test to the commercial extract. Furthermore, rAed a 1-induced flare sizes significantly correlated with mosquito bite-induced flare sizes. None of the subjects with negative bite tests had a positive skin test to rAed a 1 or to commercial extract. We conclude that the rAed a 1 has identical antigenicity and biological activity to native Aed a 1, can be used in the in vitro and in vivo diagnosis of mosquito allergy, and is more sensitive than mosquito whole-body extract for detecting delayed skin reactions.
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| pubmed:grant | |
| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Allergens,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Plant,
http://linkedlifedata.com/resource/pubmed/chemical/Insect Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Salivary Proteins and Peptides
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| pubmed:status |
MEDLINE
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| pubmed:month |
Dec
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| pubmed:issn |
0953-8178
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
13
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
1445-52
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| pubmed:dateRevised |
2011-11-17
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| pubmed:meshHeading |
pubmed-meshheading:11717185-Aedes,
pubmed-meshheading:11717185-Allergens,
pubmed-meshheading:11717185-Animals,
pubmed-meshheading:11717185-Antigens, Plant,
pubmed-meshheading:11717185-Baculoviridae,
pubmed-meshheading:11717185-Binding, Competitive,
pubmed-meshheading:11717185-Binding Sites, Antibody,
pubmed-meshheading:11717185-Bites and Stings,
pubmed-meshheading:11717185-Cells, Cultured,
pubmed-meshheading:11717185-Enzyme-Linked Immunosorbent Assay,
pubmed-meshheading:11717185-Humans,
pubmed-meshheading:11717185-Hypersensitivity, Delayed,
pubmed-meshheading:11717185-Hypersensitivity, Immediate,
pubmed-meshheading:11717185-Insect Proteins,
pubmed-meshheading:11717185-Isoelectric Point,
pubmed-meshheading:11717185-Molecular Weight,
pubmed-meshheading:11717185-Recombinant Proteins,
pubmed-meshheading:11717185-Salivary Proteins and Peptides,
pubmed-meshheading:11717185-Skin Tests,
pubmed-meshheading:11717185-Spodoptera,
pubmed-meshheading:11717185-Time Factors
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| pubmed:year |
2001
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| pubmed:articleTitle |
Expression, purification, characterization and clinical relevance of rAed a 1--a 68-kDa recombinant mosquito Aedes aegypti salivary allergen.
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| pubmed:affiliation |
Department of Pediatrics and Child Health, and Department of Immunology, University of Manitoba, Winnipeg, Manitoba R3E 3P5, Canada. zpeng@ms.umanitoba.ca
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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