Structural basis for cross-reactivity and conformation fluctuation of the major beech pollen allergen Fag s 1

Scientific Reports
A H MoraesA P Valente

Abstract

Fag s 1 is a member of the Pathogen Related protein family 10 (PR-10) and can elicit cross-reaction with IgE antibodies produced against the birch pollen allergen Bet v 1. The Nuclear Magnetic Resonance (NMR) structure of Fag s 1 is presented along with its dynamic properties. It shares 66% identity with Bet v 1 and exhibits the expected three α-helices and seven β-sheets arranged as a semi-beta barrel and exposing the residues mapped as the Bet v 1 IgE epitope. The structural dynamics of Fag s 1 were monitored on the fast and intermediate timescales, using relaxation rates. The complex dynamics of Fag s 1 are closely related to the internal cavity, and they modulate IgE and ligand binding.

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Citations

May 21, 2020·Current Allergy and Asthma Reports·Lorenz AglasFatima Ferreira
Jun 6, 2020·Scientific Reports·Emilia RomerWilfried Schwab
Mar 11, 2020·Frontiers in Molecular Biosciences·Anna S KamenikKlaus R Liedl
Feb 20, 2021·Scientific Reports·Sebastian FührerMartin Tollinger
Jun 5, 2021·Environmental Research·Chiara SuannoStefano Del Duca
Jun 18, 2021·Biochimica Et Biophysica Acta. General Subjects·Veronica S ValadaresAdolfo H Moraes

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Methods Mentioned

BETA
Nuclear
X-ray
NMR
and
size exclusion chromatography

Software Mentioned

CPMG
CCPN
CCPN analysis
Aria
Talos
fit
CNS Solve
Mole
Topspin

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