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Major venom allergen of yellow jackets, Ves v 5: Structural characterization of a pathogenesis‐related protein superfamily
Author(s) -
Henriksen Anette,
King Te P.,
Mirza Osman,
Monsalve Rafaél I.,
Meno Kåre,
Ipsen Henrik,
Larsen Jørgen N.,
Gajhede Michael,
Spangfort Michael D.
Publication year - 2001
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.1160
Subject(s) - venom , epitope , antigen , pathogenesis , allergen , peptide sequence , biology , protein superfamily , protein structure , sequence alignment , structural similarity , cross reactivity , allergy , chemistry , biochemistry , immunology , cross reactions , gene
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 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.