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Conformational Flexibility Differentiates Naturally Occurring Bet v 1 Isoforms.

Sarina Grutsch1, Julian E Fuchs2, Linda Ahammer3

  • 1Institute of Organic Chemistry & Center for Molecular Biosciences Innsbruck (CMBI), University of Innsbruck, Innrain 80/82, A-6020 Innsbruck, Austria. sarina.grutsch@uibk.ac.at.

International Journal of Molecular Sciences
|June 8, 2017
PubMed
Summary

Birch pollen protein Bet v 1 isoforms exhibit varying flexibility, influencing allergic sensitization. This conformational flexibility impacts proteolytic cleavage, offering a structural basis for differing immune responses in allergies.

Keywords:
allergen structureallergensallergic sensitizationflexibilityproteolytic processing

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Area of Science:

  • Allergen structure and function
  • Immunology and protein biochemistry

Background:

  • Bet v 1 protein is a primary allergen in birch pollen
  • Isoforms of Bet v 1 show varied allergic sensitization and Th2 polarization
  • Differential proteolytic cleavage susceptibility is a likely cause for isoform variation

Purpose of the Study:

  • To investigate the conformational flexibility of Bet v 1 isoforms
  • To understand the link between flexibility, proteolytic cleavage, and immune response

Main Methods:

  • Nuclear Magnetic Resonance (NMR) relaxation experiments
  • Molecular dynamics simulations
  • NMR hydrogen-deuterium exchange measurements

Main Results:

  • Proteolytic cleavage sites in Bet v 1 isoforms (Bet v 1.0101 and Bet v 1.0102) are conformationally flexible
  • Bet v 1.0102 exhibits greater flexibility and heterogeneity than Bet v 1.0101
  • Bet v 1.0102 has more solvent-exposed backbone amides, correlating with higher proteolytic susceptibility

Conclusions:

  • Differential conformational flexibility in Bet v 1 isoforms may explain variations in proteolytic susceptibility
  • This flexibility could provide a structure-based rationale for observed differences in Th2 polarization and allergic sensitization