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

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Major venom allergen of yellow jackets, Ves v 5 : structural characterization of a pathogenesis-related protein superfamily. / Henriksen, A; King, T P; Mirza, O; Monsalve, R I; Meno, K; Ipsen, H; Larsen, J N; Gajhede, Michael; Spangfort, M D.

In: Proteins: Structure, Function, and Bioinformatics, Vol. 45, No. 4, 2001, p. 438-48.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Henriksen, A, King, TP, Mirza, O, Monsalve, RI, Meno, K, Ipsen, H, Larsen, JN, Gajhede, M & Spangfort, MD 2001, 'Major venom allergen of yellow jackets, Ves v 5: structural characterization of a pathogenesis-related protein superfamily', Proteins: Structure, Function, and Bioinformatics, vol. 45, no. 4, pp. 438-48.

APA

Henriksen, A., King, T. P., Mirza, O., Monsalve, R. I., Meno, K., Ipsen, H., Larsen, J. N., Gajhede, M., & Spangfort, M. D. (2001). Major venom allergen of yellow jackets, Ves v 5: structural characterization of a pathogenesis-related protein superfamily. Proteins: Structure, Function, and Bioinformatics, 45(4), 438-48.

Vancouver

Henriksen A, King TP, Mirza O, Monsalve RI, Meno K, Ipsen H et al. Major venom allergen of yellow jackets, Ves v 5: structural characterization of a pathogenesis-related protein superfamily. Proteins: Structure, Function, and Bioinformatics. 2001;45(4):438-48.

Author

Henriksen, A ; King, T P ; Mirza, O ; Monsalve, R I ; Meno, K ; Ipsen, H ; Larsen, J N ; Gajhede, Michael ; Spangfort, M D. / Major venom allergen of yellow jackets, Ves v 5 : structural characterization of a pathogenesis-related protein superfamily. In: Proteins: Structure, Function, and Bioinformatics. 2001 ; Vol. 45, No. 4. pp. 438-48.

Bibtex

@article{b5cfa91558734647a86e4549c0aa5175,
title = "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.",
keywords = "Allergens, Amino Acid Sequence, Animals, Binding Sites, Conserved Sequence, Crystallography, X-Ray, Epitopes, B-Lymphocyte, Hydrogen Bonding, Hydrophobic and Hydrophilic Interactions, Models, Molecular, Molecular Sequence Data, Multigene Family, Phylogeny, Protein Conformation, Sequence Alignment, Wasp Venoms, Wasps",
author = "A Henriksen and King, {T P} and O Mirza and Monsalve, {R I} and K Meno and H Ipsen and Larsen, {J N} and Michael Gajhede and Spangfort, {M D}",
note = "Copyright 2001 Wiley-Liss, Inc.",
year = "2001",
language = "English",
volume = "45",
pages = "438--48",
journal = "Proteins: Structure, Function, and Bioinformatics",
issn = "0887-3585",
publisher = "JohnWiley & Sons, Inc.",
number = "4",

}

RIS

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

VL - 45

SP - 438

EP - 448

JO - Proteins: Structure, Function, and Bioinformatics

JF - Proteins: Structure, Function, and Bioinformatics

SN - 0887-3585

IS - 4

ER -

ID: 47290555