Allergens in Hymenoptera venom XI. Isolation of protein allergens from (yellow jacket) venom

Hoffman, Donald R.; Wood, Catherine L.

doi:10.1016/0091-6749(84)90094-0

Cited by 55 publications

(30 citation statements)

References 25 publications

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“…This protein corresponds to Api m 5 regarding m.w., amino acid sequence, enzymatic function, IgE immunoreactivity using a broad range of YJV-sensitized individuals, and functional allergenic capability using basophils from venom-allergic patients. Although a protein of this size has been reported as a putative IgE-reactive protein in another Vespula species, no attribution of a name or function in V. vulgaris has been made so far (34).…”

Section: Discussionmentioning

confidence: 99%

Identification, Recombinant Expression, and Characterization of the 100 kDa High Molecular Weight Hymenoptera Venom Allergens Api m 5 and Ves v 3

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Seismann

Bockisch

et al. 2010

The Journal of Immunology

108

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Section: Discussionmentioning

confidence: 99%

Identification, Recombinant Expression, and Characterization of the 100 kDa High Molecular Weight Hymenoptera Venom Allergens Api m 5 and Ves v 3

Blank

Seismann

Bockisch

et al. 2010

The Journal of Immunology

108

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“…In honeybee venom, the glycosylated allergens currently known are phospholipase A2 (Api m 1), hyaluronidase (Api m 2) and acid phosphatase (Api m 3) [86, 87], whereof the glycan parts of phospholipase A2 and hyaluronidase were characterized as IgE-binding CCD [84, 88, 89]. In yellow jacket venom, solely the major allergen hyaluronidase (Ves m/v/f/g/p/s 2) has been shown to be a glycoprotein containing CCD [84, 90] but further, yet unidentified IgE-binding glycoproteins are present in yellow jacket as well as in honeybee venoms [84, 91]. The only homologous allergenic structure in honeybee venom and yellow jacket venom identified so far is hyaluronidase, with an amino acid sequence identity of 53% between Api m 2 (Swiss-Prot Q08169) and Ves v 2 of Vespula vulgaris (Swiss-Prot P49370; table 11) [92, 93].…”

Section: Insect Venomsmentioning

confidence: 99%

The Principle of Homologous Groups in Regulatory Affairs of Allergen Products – A Proposal

Lorenz

Lüttkopf

May

et al. 2008

Int Arch Allergy Immunol

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Among other legal regulations, the Note for Guidance on Allergen Products CPMP/BWP/243/96 released by the European Medicines Agency provides regulatory instructions regarding the quality of allergen extracts for diagnostic or therapeutic purposes. The current revision of this guideline intends to transform the so-called ‘principle of taxonomic families’ to the ‘principle of homologous groups’. According to this concept, the data of one allergen extract demonstrating stability, efficacy and safety can, to a limited extent, be extrapolated to other allergen extracts belonging to the same homologous groups. The present work proposes the formation of homologous groups for pollen species and animal-derived materials on the basis of similar biochemical composition and homology/cross-reactivity of allergens or allergen sources. Some tree pollen species could be assigned to three different homologous groups, some weed pollen species to one homologous group and numerous grass pollen species to one homologous group on condition that data rely on single defined representative species. A homologous group for mites is limited to the Dermatophagoides species and the grouping of vertebrate-derived materials such as dander could be possible under restrictions. The criteria for the formation of the proposed homologous groups are illustrated in detail to provide an opportunity for extending existing homologous groups by further species in case of new insights in allergens and cross-reactivity of allergen sources. In this way, the concept of homologous groups could serve as a dynamic tool in the regulation of allergen products.

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“…Hyaluronidase, phospholipase A and B and proteases were all measured using the methods we have previously described [ 14).…”

Section: Protein and Enzyme Analysismentioning

confidence: 99%

Allergens in Hymenoptera Venom

Hoffman

Jacobson

Zerboni

1987

Int Arch Allergy Immunol

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The European hornet, Vespa crabro, is a very large insect native to much of Europe and Asia and introduced into eastern North America. Four cases of allergic reactions to V. crabro stings are presented, one of which was fatal. V. crabro venom contains 2% protein and peptide. There are three major proteins: Phospholipase AB, antigen 5 and hyaluronidase. These proteins are structurally and antigenically related to those from other vespid wasps, especially Vespula yellow jackets. IgE antibodies from patients allergic to Vespula usually cross-react with V. crabro venom. In three of the four patients with known reactions to V. crabro venom antigen 5 appeared to be the most important allergen. Serum from one patient was most reactive with hyaluronidase. Phospholipase had relatively little IgE-binding activity, although it was the major protein in the venom. V. crabro venom is at least as closely related to Vespula venoms as Dolichovespula venoms are.

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Allergens in Hymenoptera venom XI. Isolation of protein allergens from (yellow jacket) venom

Cited by 55 publications

References 25 publications

Identification, Recombinant Expression, and Characterization of the 100 kDa High Molecular Weight Hymenoptera Venom Allergens Api m 5 and Ves v 3

Identification, Recombinant Expression, and Characterization of the 100 kDa High Molecular Weight Hymenoptera Venom Allergens Api m 5 and Ves v 3

The Principle of Homologous Groups in Regulatory Affairs of Allergen Products – A Proposal

Allergens in Hymenoptera Venom

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