Recombinant Hymenoptera venom allergens

Müller, Ulrich

doi:10.1034/j.1398-9995.2002.02157.x

Cited by 72 publications

(49 citation statements)

References 40 publications

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“…For example, cross-reactivity between yellow jacket and honeybee venom hyaluronidases has been considered to be responsible for double-positive diagnosis. The ability to produce and characterize recombinant forms of venom allergens (Muller, 2002) opens the possibility for an improvement of diagnosis and for a detailed understanding of cross-reactivity patterns and specificity. This could lead to modified allergens with increased efficacy in immunotherapy treatment of allergic patients.…”

Section: Introductionmentioning

confidence: 99%

Structure of recombinant Ves v 2 at 2.0 Å resolution: structural analysis of an allergenic hyaluronidase from wasp venom

Skov

Seppälä

Coen

et al. 2006

Acta Crystallogr D Biol Crystallogr

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Wasp venom from Vespula vulgaris contains three major allergens: Ves v 1, Ves v 2 and Ves v 5. Here, the cloning, expression, biochemical characterization and crystal structure determination of the hyaluronidase Ves v 2 from family 56 of the glycoside hydrolases are reported. The allergen was expressed in Escherichia coli as an insoluble protein and refolded and purified to obtain full enzymatic activity. Three N‐glycosylation sites at Asn79, Asn99 and Asn127 were identified in Ves v 2 from a natural source by enzymatic digestions combined with MALDI–TOF mass spectrometry. The crystal structure of recombinant Ves v 2 was determined at 2.0 Å resolution and reveals a central (β/α)7 core that is further stabilized by two disulfide bonds (Cys19–Cys308 and Cys185–Cys197). Based on sequence alignments and structural comparison with the honeybee allergen Api m 2, it is proposed that a conserved cavity near the active site is involved in binding of the substrate. Surface epitopes and putative glycosylation sites have been compared with those of two other major group 2 allergens from Apis mellifera (honeybee) and Dolichovespula maculata (white‐faced hornet). The analysis suggests that the harboured allergic IgE‐mediated cross‐reactivity between Ves v 2 and the allergen from D. maculata is much higher than that between Ves v 2 and the allergen from A. mellifera.

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Section: Introductionmentioning

confidence: 99%

Structure of recombinant Ves v 2 at 2.0 Å resolution: structural analysis of an allergenic hyaluronidase from wasp venom

Skov

Seppälä

Coen

et al. 2006

Acta Crystallogr D Biol Crystallogr

View full text Add to dashboard Cite

show abstract

“…Thus, there is considerable interest in improving safety and efficacy of diagnostic approaches and Hymenoptera venom immunotherapy. The use of recombinant allergens for the development of component-resolved IgE immunoassays and safer and more efficacious immunotherapeutic modalities may provide such an improvement (4), but only a limited number of Hymenoptera venom allergens are available as recombinant proteins (5,6).…”

mentioning

confidence: 99%