2atm

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2atm, resolution 2.000Å

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Crystal structure of the recombinant allergen Ves v 2

Overview

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 A resolution and reveals a central (beta/alpha)(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.

About this Structure

2ATM is a Single protein structure of sequence from Vespula vulgaris with SO4 and MES as ligands. Active as Hyalurononglucosaminidase, with EC number 3.2.1.35 Full crystallographic information is available from OCA.

Reference

Structure of recombinant Ves v 2 at 2.0 Angstrom resolution: structural analysis of an allergenic hyaluronidase from wasp venom., Skov LK, Seppala U, Coen JJ, Crickmore N, King TP, Monsalve R, Kastrup JS, Spangfort MD, Gajhede M, Acta Crystallogr D Biol Crystallogr. 2006 Jun;62(Pt 6):595-604. Epub 2006, May 12. PMID:16699186

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