Molecular Determinants for Antibody Binding on Group 1 House Dust Mite Allergens

Journal Article · Wed Jul 11 04:00:00 EDT 2012 · J. Biol. Chem.

DOI:https://doi.org/10.1074/jbc.M111.311159· OSTI ID:1038298

Chruszcz, Maksymilian; Pomés, Anna; Glesner, Jill; Vailes, Lisa D; Osinski, Tomasz; Porebski, Przemyslaw J; Majorek, Karolina A; Heymann, Peter W; Platts-Mills, Thomas A.E.; Minor, Wladek; Chapman, Martin D ^[1]

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1. INDOOR Bio.

House dust mites produce potent allergens, Der p 1 and Der f 1, that cause allergic sensitization and asthma. Der p 1 and Der f 1 are cysteine proteases that elicit IgE responses in 80% of mite-allergic subjects and have proinflammatory properties. Their antigenic structure is unknown. Here, we present crystal structures of natural Der p 1 and Der f 1 in complex with a monoclonal antibody, 4C1, which binds to a unique cross-reactive epitope on both allergens associated with IgE recognition. The 4C1 epitope is formed by almost identical amino acid sequences and contact residues. Mutations of the contact residues abrogate mAb 4C1 binding and reduce IgE antibody binding. These surface-exposed residues are molecular targets that can be exploited for development of recombinant allergen vaccines.

• Research Organization: Advanced Photon Source (APS), Argonne National Laboratory (ANL), Argonne, IL (US)
• Sponsoring Organization: NIH
• OSTI ID: 1038298
• Journal Information: J. Biol. Chem., Journal Name: J. Biol. Chem. Journal Issue: (10) ; 03, 2012 Vol. 287; ISSN JBCHA3; ISSN 0021-9258
• Country of Publication: United States
• Language: ENGLISH

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
60 APPLIED LIFE SCIENCES
ALLERGY
AMINO ACID SEQUENCE
ANTIBODIES
ASTHMA
BIOLOGY
CRYSTAL STRUCTURE
CYSTEINE
DUSTS
IMMUNOLOGY
MITES
MUTATIONS
RESIDUES
TARGETS
VACCINES