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Title: Crystal Structures of Mite Allergens Der f 1 and Der p 1 Reveal Differences in Surface-Exposed Residues that May Influence Antibody Binding

Abstract

The Group 1 mite allergens, Der f 1 and Der p 1, are potent allergens excreted by Dermatophagoides farinae and Dermatophagoides pteronyssinus, respectively. The human IgE antibody responses to the Group 1 allergens show more cross-reactivity than the murine IgG antibody responses which are largely species-specific. Here, we report the crystal structure of the mature form of Der f 1, which was isolated from its natural source, and a new, high-resolution structure of mature recombinant Der p 1. Unlike Der p 1, Der f 1 is monomeric both in the crystalline state and in solution. Moreover, no metal binding is observed in the structure of Der f 1, despite the fact that all amino acids involved in Ca{sup 2+} binding in Der p 1 are completely conserved in Der f 1. Although Der p 1 and Der f 1 share extensive sequence identity, comparison of the crystal structures of both allergens revealed structural features which could explain the differences in murine and human IgE antibody responses to these allergens. There are structural differences between Der f 1 and Der p 1 which are unevenly distributed on the allergens' surfaces. This uneven spatial arrangement of conserved versus altered residues could explainmore » both the specificity and cross-reactivity of antibodies against Der f 1 and Der p 1.« less

Authors:
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  1. (
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States)
Sponsoring Org.:
USDOE
OSTI Identifier:
1005687
Resource Type:
Journal Article
Journal Name:
J. Mol. Biol.
Additional Journal Information:
Journal Volume: 386; Journal Issue: (2) ; 02, 2009; Journal ID: ISSN 0022-2836
Country of Publication:
United States
Language:
ENGLISH
Subject:
36 MATERIALS SCIENCE; ALLERGY; AMINO ACIDS; ANTIBODIES; ANTIBODY FORMATION; ANTIGEN-ANTIBODY REACTIONS; CRYSTAL STRUCTURE; HUMAN POPULATIONS; METALS; MITES; RESIDUES; SPECIFICITY; SURFACES

Citation Formats

Chruszcz, Maksymilian, Chapman, Martin D., Vailes, Lisa D., Stura, Enrico A., Saint-Remy, Jean-Marie, Minor, Wladek, Pomés, Anna, INDOOR Bio.), CEAS), Leuven), and UV). Crystal Structures of Mite Allergens Der f 1 and Der p 1 Reveal Differences in Surface-Exposed Residues that May Influence Antibody Binding. United States: N. p., 2009. Web. doi:10.1016/j.jmb.2008.12.049.
Chruszcz, Maksymilian, Chapman, Martin D., Vailes, Lisa D., Stura, Enrico A., Saint-Remy, Jean-Marie, Minor, Wladek, Pomés, Anna, INDOOR Bio.), CEAS), Leuven), & UV). Crystal Structures of Mite Allergens Der f 1 and Der p 1 Reveal Differences in Surface-Exposed Residues that May Influence Antibody Binding. United States. doi:10.1016/j.jmb.2008.12.049.
Chruszcz, Maksymilian, Chapman, Martin D., Vailes, Lisa D., Stura, Enrico A., Saint-Remy, Jean-Marie, Minor, Wladek, Pomés, Anna, INDOOR Bio.), CEAS), Leuven), and UV). Tue . "Crystal Structures of Mite Allergens Der f 1 and Der p 1 Reveal Differences in Surface-Exposed Residues that May Influence Antibody Binding". United States. doi:10.1016/j.jmb.2008.12.049.
@article{osti_1005687,
title = {Crystal Structures of Mite Allergens Der f 1 and Der p 1 Reveal Differences in Surface-Exposed Residues that May Influence Antibody Binding},
author = {Chruszcz, Maksymilian and Chapman, Martin D. and Vailes, Lisa D. and Stura, Enrico A. and Saint-Remy, Jean-Marie and Minor, Wladek and Pomés, Anna and INDOOR Bio.) and CEAS) and Leuven) and UV)},
abstractNote = {The Group 1 mite allergens, Der f 1 and Der p 1, are potent allergens excreted by Dermatophagoides farinae and Dermatophagoides pteronyssinus, respectively. The human IgE antibody responses to the Group 1 allergens show more cross-reactivity than the murine IgG antibody responses which are largely species-specific. Here, we report the crystal structure of the mature form of Der f 1, which was isolated from its natural source, and a new, high-resolution structure of mature recombinant Der p 1. Unlike Der p 1, Der f 1 is monomeric both in the crystalline state and in solution. Moreover, no metal binding is observed in the structure of Der f 1, despite the fact that all amino acids involved in Ca{sup 2+} binding in Der p 1 are completely conserved in Der f 1. Although Der p 1 and Der f 1 share extensive sequence identity, comparison of the crystal structures of both allergens revealed structural features which could explain the differences in murine and human IgE antibody responses to these allergens. There are structural differences between Der f 1 and Der p 1 which are unevenly distributed on the allergens' surfaces. This uneven spatial arrangement of conserved versus altered residues could explain both the specificity and cross-reactivity of antibodies against Der f 1 and Der p 1.},
doi = {10.1016/j.jmb.2008.12.049},
journal = {J. Mol. Biol.},
issn = {0022-2836},
number = (2) ; 02, 2009,
volume = 386,
place = {United States},
year = {2009},
month = {12}
}