AI Article Synopsis

  • Many allergens, like Bet v 1, have similar biophysical traits, particularly the ability to form dimers, but the details of how this occurs are not well understood.
  • Researchers discovered that in the structure of dimeric Bet v 1, cysteine replaces the usual tyrosine at position 5, which helps stabilize different dimer configurations through polysulfide bridging.
  • These findings highlight residue 5 as a key area linked to allergenic activity in Bet v 1, advancing our knowledge of protein chemistry and the role of modifications in allergy mechanisms.

Article 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.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3879576PMC
http://dx.doi.org/10.1074/jbc.M113.518795DOI Listing

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