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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
1994-12-9
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pubmed:databankReference | |
pubmed:abstractText |
Shrimp is a common cause of seafood hypersensitivity. To study the mechanism of seafood hypersensitivity at the molecular level, we have determined the primary structure of the major heat-stable allergen of shrimp by cloning, expression, nucleotide sequencing, and amino acid sequence determination of an IgE-reactive cDNA clone, Met e I, isolated from a Metapenaeus ensis expression library in lambda gt 11. We first constructed a cDNA library from the shrimp M. ensis in lambda gt 11. We then screened the library with sera from patients with hypersensitivity reactions to shrimp and identified a positive IgE-reactive clone, designated as Met e I. This cDNA was purified to homogeneity and subsequently expressed in the plasmid pGEX. Serum antibodies from patients with shrimp allergy demonstrated positive IgE reactivity by immunoblotting to a protein encoded by the clone Met e I; sera from nonallergic control subjects were not reactive. The nucleotide sequence of this cDNA clone revealed an open reading frame of 281 amino acid residues, coding for a protein of 34 kd. Comparison of the Met e I amino acid sequence with the Genbank database showed that Met e I is highly homologous to multiple isoforms of tropomyosin.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Allergens,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin E,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tropomyosin
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0091-6749
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
94
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
882-90
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:7963157-Allergens,
pubmed-meshheading:7963157-Amino Acid Sequence,
pubmed-meshheading:7963157-Animals,
pubmed-meshheading:7963157-Cloning, Molecular,
pubmed-meshheading:7963157-DNA, Complementary,
pubmed-meshheading:7963157-Drug Stability,
pubmed-meshheading:7963157-Food Hypersensitivity,
pubmed-meshheading:7963157-Gene Library,
pubmed-meshheading:7963157-Hot Temperature,
pubmed-meshheading:7963157-Humans,
pubmed-meshheading:7963157-Immunoglobulin E,
pubmed-meshheading:7963157-Molecular Sequence Data,
pubmed-meshheading:7963157-Penaeidae,
pubmed-meshheading:7963157-Recombinant Proteins,
pubmed-meshheading:7963157-Tropomyosin
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pubmed:year |
1994
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pubmed:articleTitle |
Cloning, expression, and primary structure of Metapenaeus ensis tropomyosin, the major heat-stable shrimp allergen.
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pubmed:affiliation |
Division of Rheumatology, Allergy and Clinical Immunology, School of Medicine, University of California Davis.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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