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Title: Der p 5 Crystal Structure Provides Insight into the Group 5 Dust Mite Allergens

Abstract

Group 5 allergens from house dust mites elicit strong IgE antibody binding in mite-allergic patients. The structure of Der p 5 was determined by x-ray crystallography to better understand the IgE epitopes, to investigate the biologic function in mites, and to compare with the conflicting published Blo t 5 structures, designated 2JMH and 2JRK in the Protein Data Bank. Der p 5 is a three-helical bundle similar to Blo t 5, but the interactions of the helices are more similar to 2JMH than 2JRK. The crystallographic asymmetric unit contains three dimers of Der p 5 that are not exactly alike. Solution scattering techniques were used to assess the multimeric state of Der p 5 in vitro and showed that the predominant state was monomeric, similar to Blo t 5, but larger multimeric species are also present. In the crystal, the formation of the Der p 5 dimer creates a large hydrophobic cavity of {approx}3000 {angstrom}{sup 3} that could be a ligand-binding site. Many allergens are known to bind hydrophobic ligands, which are thought to stimulate the innate immune system and have adjuvant-like effects on IgE-mediated inflammatory responses.

Authors:
; ; ; ; ; ; ; ; ;
Publication Date:
Research Org.:
Brookhaven National Laboratory (BNL) National Synchrotron Light Source
Sponsoring Org.:
DOE - OFFICE OF SCIENCE
OSTI Identifier:
1019682
Report Number(s):
BNL-95528-2011-JA
Journal ID: ISSN 0021-9258; JBCHA3; TRN: US201115%%322
DOE Contract Number:
DE-AC02-98CH10886
Resource Type:
Journal Article
Resource Relation:
Journal Name: Journal of Biological Chemistry; Journal Volume: 285; Journal Issue: 33
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; 99 GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; DIMERS; DUSTS; IN VITRO; MITES; PATIENTS; PROTEINS; SCATTERING; national synchrotron light source

Citation Formats

Mueller, G., Gosavi, R, Krahn, J, Edwards, L, Cuneo, M, Glesner, J, Pomes, A, Chapman, M, London, R, and Pedersen, L. Der p 5 Crystal Structure Provides Insight into the Group 5 Dust Mite Allergens. United States: N. p., 2010. Web. doi:10.1074/jbc.M110.128306.
Mueller, G., Gosavi, R, Krahn, J, Edwards, L, Cuneo, M, Glesner, J, Pomes, A, Chapman, M, London, R, & Pedersen, L. Der p 5 Crystal Structure Provides Insight into the Group 5 Dust Mite Allergens. United States. doi:10.1074/jbc.M110.128306.
Mueller, G., Gosavi, R, Krahn, J, Edwards, L, Cuneo, M, Glesner, J, Pomes, A, Chapman, M, London, R, and Pedersen, L. 2010. "Der p 5 Crystal Structure Provides Insight into the Group 5 Dust Mite Allergens". United States. doi:10.1074/jbc.M110.128306.
@article{osti_1019682,
title = {Der p 5 Crystal Structure Provides Insight into the Group 5 Dust Mite Allergens},
author = {Mueller, G. and Gosavi, R and Krahn, J and Edwards, L and Cuneo, M and Glesner, J and Pomes, A and Chapman, M and London, R and Pedersen, L},
abstractNote = {Group 5 allergens from house dust mites elicit strong IgE antibody binding in mite-allergic patients. The structure of Der p 5 was determined by x-ray crystallography to better understand the IgE epitopes, to investigate the biologic function in mites, and to compare with the conflicting published Blo t 5 structures, designated 2JMH and 2JRK in the Protein Data Bank. Der p 5 is a three-helical bundle similar to Blo t 5, but the interactions of the helices are more similar to 2JMH than 2JRK. The crystallographic asymmetric unit contains three dimers of Der p 5 that are not exactly alike. Solution scattering techniques were used to assess the multimeric state of Der p 5 in vitro and showed that the predominant state was monomeric, similar to Blo t 5, but larger multimeric species are also present. In the crystal, the formation of the Der p 5 dimer creates a large hydrophobic cavity of {approx}3000 {angstrom}{sup 3} that could be a ligand-binding site. Many allergens are known to bind hydrophobic ligands, which are thought to stimulate the innate immune system and have adjuvant-like effects on IgE-mediated inflammatory responses.},
doi = {10.1074/jbc.M110.128306},
journal = {Journal of Biological Chemistry},
number = 33,
volume = 285,
place = {United States},
year = 2010,
month = 1
}