Major venom allergen of yellow jackets, Ves v 5: Structural characterization of a pathogenesis‐related protein superfamily

Abstract

Ves v 5 is one of three major allergens found in yellow-jacket venom: phospholipase A(1) (Ves v 1), hyaluronidase (Ves v 2), and antigen 5 (Ves v 5). Ves v 5 is related by high amino acid sequence identity to pathogenesis-related proteins including proteins from mammals, reptiles, insects, fungi, and plants. The crystal structure of Ves v 5 has been solved and refined to a resolution of 1.9 A. The majority of residues conserved between the pathogenesis-related proteins can be rationalized in terms of hydrogen bonding patterns and hydrophobic interactions defining an alpha-beta-alpha sandwich core structure. A small number of consensus residues are solvent exposed (including two adjacent histidines) and located in an elongated cavity that forms a putative active site. The site has no structural resemblance to previously characterized enzymes. Homologous antigen 5's from a large number of different yellow jackets, hornets, and paper wasps are known and patients show varying extents of cross-reactivity to the related antigen 5's. The structure of Ves v 5 allows a detailed analysis of the epitopes that may participate in antigenic cross-reactivity, findings that are useful for the development of a vaccine for treatment of insect allergy.

Structure of Protein Having Inhibitory Disintegrin and Leukotriene Scavenging Functions Contained in Single Domain

“…The C-terminal segment of tablysin-15 is longer than that of Ves v 5 and is similar in conformation to the hinge region between the CAP domain and the CRISP domain of the calcium channel blocker triflin (3,31). CRISP domain proteins normally contain two disulfide bonds in the hinge region (28), and one of these disulfides (linking Cys-209 and Cys-220) is conserved in tablysin-15.…”

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

“…In yellow jacket (Vespula vulgaris) venom these allergens are denoted Ves v 1 (phospholipase), Ves v 2 (hyaluronidase) and Ves v 5 (antigen 5). The three-dimensional structure has been determined for Ves v 5 (Henriksen et al, 2001), revealing an active site with no structural resemblance to previously characterized enzymes. The structure determination of Ves v 5 also enabled analyses of conformational B-cell epitopes involved in allergic crossreactivity.…”

Proteome of Hydra Nematocyst

“…In addition, we cannot exclude evolutionary transitions from venom-related molecules to structural proteins. The SCP domain might serve as an example, as it forms a pathogenesis-related superfamily across the metazoan subkingdom (34) and is part of the major capsule structure protein NOWA.…”