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

TY - JOUR

T1 - Major venom allergen of yellow jackets, Ves v 5

T2 - structural characterization of a pathogenesis-related protein superfamily

AU - Henriksen, A

AU - King, T P

AU - Mirza, O

AU - Monsalve, R I

AU - Meno, K

AU - Ipsen, H

AU - Larsen, J N

AU - Gajhede, Michael

AU - Spangfort, M D

N1 - Copyright 2001 Wiley-Liss, Inc.

PY - 2001

Y1 - 2001

N2 - 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.

AB - 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.

KW - Allergens

KW - Amino Acid Sequence

KW - Animals

KW - Binding Sites

KW - Conserved Sequence

KW - Crystallography, X-Ray

KW - Epitopes, B-Lymphocyte

KW - Hydrogen Bonding

KW - Hydrophobic and Hydrophilic Interactions

KW - Models, Molecular

KW - Molecular Sequence Data

KW - Multigene Family

KW - Phylogeny

KW - Protein Conformation

KW - Sequence Alignment

KW - Wasp Venoms

KW - Wasps

M3 - Journal article

SN - 0887-3585

VL - 45

SP - 438

EP - 448

JO - Proteins: Structure, Function, and Bioinformatics

JF - Proteins: Structure, Function, and Bioinformatics

IS - 4

ER -