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

Journal Article · Tue Dec 01 04:00:00 EST 2009 · J. Mol. Biol.

DOI:https://doi.org/10.1016/j.jmb.2008.12.049· OSTI ID:1005687

Chruszcz, Maksymilian; Chapman, Martin D; Vailes, Lisa D; Stura, Enrico A; Saint-Remy, Jean-Marie; Minor, Wladek; Pomés, Anna

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.

• Research Organization: Argonne National Laboratory (ANL)
• Sponsoring Organization: USDOE
• OSTI ID: 1005687
• Journal Information: J. Mol. Biol., Journal Name: J. Mol. Biol. Journal Issue: (2) ; 02, 2009 Vol. 386; ISSN JMOBAK; ISSN 0022-2836
• Country of Publication: United States
• Language: ENGLISH

Related Subjects

36 MATERIALS SCIENCE
ALLERGY
AMINO ACIDS
ANTIBODIES
ANTIBODY FORMATION
ANTIGEN-ANTIBODY REACTIONS
CRYSTAL STRUCTURE
HUMAN POPULATIONS
METALS
MITES
RESIDUES
SPECIFICITY
SURFACES