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J Biol Chem. 2014 Jan 3;289(1):540-51. doi: 10.1074/jbc.M113.518795. Epub 2013 Nov 19.

Stabilization of the dimeric birch pollen allergen Bet v 1 impacts its immunological properties.

Author information

1
From the Structural Biology Group, Department of Molecular Biology.

Abstract

Many allergens share several biophysical characteristics, including the capability to undergo oligomerization. The dimerization mechanism in Bet v 1 and its allergenic properties are so far poorly understood. Here, we report crystal structures of dimeric Bet v 1, revealing a noncanonical incorporation of cysteine at position 5 instead of genetically encoded tyrosine. Cysteine polysulfide bridging stabilized different dimeric assemblies, depending on the polysulfide linker length. These dimers represent quaternary arrangements that are frequently observed in related proteins, reflecting their prevalence in unmodified Bet v 1. These conclusions were corroborated by characteristic immunologic properties of monomeric and dimeric allergen variants. Hereby, residue 5 could be identified as an allergenic hot spot in Bet v 1. The presented results refine fundamental principles in protein chemistry and emphasize the importance of protein modifications in understanding the molecular basis of allergenicity.

KEYWORDS:

Allergen; Crystal Structure; Dimerization; Mass Spectrometry (MS); Noncanonical Amino Acid Incorporation; Polysulfide Linking; Position-specific Alteration of Genetic Code; Post-translational Modification; Protein Assembly

PMID:
24253036
PMCID:
PMC3879576
DOI:
10.1074/jbc.M113.518795
[Indexed for MEDLINE]
Free PMC Article

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