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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
|
| pubmed:dateCreated |
1996-11-26
|
| pubmed:databankReference | |
| pubmed:abstractText |
Three known allergens of yellow jacket (Vespula vulgaris) venom are antigen 5, hyaluronidase, and phospholipase. Yellow jacket antigen 5 has been previously cloned and expressed in bacteria; it contains 204 amino acid residues, and it has 69% and 60% sequence identities with the homologous proteins of white-faced hornet (Dolichovespula maculata) and wasp (Polistes annularis), respectively. These studies are now extended to yellow jacket hyaluronidase and phospholipase; they contain 331 and 300 amino acid residues, respectively, and they show 92% and 67% sequence identity with their homologs of white-faced hornet. Tests with the natural and the recombinant vespid allergens in mice indicate partial antigenic cross-reactivity of their homologous proteins at both B- and T-cell levels. There is greater cross-reactivity among hornet and yellow jacket allergens than that among hornet or yellow jacket and wasp allergens. The order of cross-reaction of the three vespid allergens is hyaluronidase > antigen 5 > phospholipase. The continuous (linear) B-cell epitopes of vespid allergens show greater cross-reactivity than their discontinuous epitopes do. The discontinuous B-cell epitopes are immunodominant for all vespid allergens. The low degree of cross-reactivity of the immunodominant discontinuous B-cell epitopes of vespid allergens should be taken into consideration in selection of venoms for immunotherapy of patients with sensitivity to multiple vespids.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
AIM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Allergens,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Plant,
http://linkedlifedata.com/resource/pubmed/chemical/Hyaluronoglucosaminidase,
http://linkedlifedata.com/resource/pubmed/chemical/Insect Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipases A,
http://linkedlifedata.com/resource/pubmed/chemical/Wasp Venoms
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Sep
|
| pubmed:issn |
0091-6749
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
98
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
588-600
|
| pubmed:dateRevised |
2010-11-18
|
| pubmed:meshHeading |
pubmed-meshheading:8828537-Allergens,
pubmed-meshheading:8828537-Amino Acid Sequence,
pubmed-meshheading:8828537-Animals,
pubmed-meshheading:8828537-Antigens, Plant,
pubmed-meshheading:8828537-Base Sequence,
pubmed-meshheading:8828537-Cloning, Molecular,
pubmed-meshheading:8828537-Cross Reactions,
pubmed-meshheading:8828537-Hyaluronoglucosaminidase,
pubmed-meshheading:8828537-Hypersensitivity,
pubmed-meshheading:8828537-Insect Proteins,
pubmed-meshheading:8828537-Lymphocyte Activation,
pubmed-meshheading:8828537-Mice,
pubmed-meshheading:8828537-Mice, Inbred BALB C,
pubmed-meshheading:8828537-Molecular Sequence Data,
pubmed-meshheading:8828537-Phospholipases A,
pubmed-meshheading:8828537-Sequence Homology, Amino Acid,
pubmed-meshheading:8828537-Spleen,
pubmed-meshheading:8828537-Wasp Venoms,
pubmed-meshheading:8828537-Wasps
|
| pubmed:year |
1996
|
| pubmed:articleTitle |
Yellow jacket venom allergens, hyaluronidase and phospholipase: sequence similarity and antigenic cross-reactivity with their hornet and wasp homologs and possible implications for clinical allergy.
|
| pubmed:affiliation |
Rockefeller University, New York 10021, USA.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|