Major venom allergen of yellow jackets, Ves v 5: Structural characterization of a pathogenesis-related protein superfamily
Article first published online: 26 OCT 2001
Copyright © 2001 Wiley-Liss, Inc.
Proteins: Structure, Function, and Bioinformatics
Volume 45, Issue 4, pages 438–448, 1 December 2001
How to Cite
Henriksen, A., King, T. P., Mirza, O., Monsalve, R. I., Meno, K., Ipsen, H., Larsen, J. N., Gajhede, M. and Spangfort, M. D. (2001), Major venom allergen of yellow jackets, Ves v 5: Structural characterization of a pathogenesis-related protein superfamily. Proteins, 45: 438–448. doi: 10.1002/prot.1160
- Issue published online: 26 OCT 2001
- Article first published online: 26 OCT 2001
- Manuscript Accepted: 17 JUL 2001
- Manuscript Received: 27 APR 2001
- NIH. Grant Number: AI-17021
- Danish Natural Science Research Council
Ves v 5 is one of three major allergens found in yellow-jacket venom: phospholipase A1 (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 Å. The majority of residues conserved between the pathogenesis-related proteins can be rationalized in terms of hydrogen bonding patterns and hydrophobic interactions defining an α-β-α 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. Proteins 2001;45:438–448. © 2001 Wiley-Liss, Inc.