RAW DATA ON THERMAL STABILITY, LIGAND BINDING AND ALLERGENICITY OF Mus m 1.0102 ALLERGEN AND ITS SELECTED CYSTEINE MUTANTS

Published: 16 February 2020| Version 1 | DOI: 10.17632/yscyvryz8t.1
Contributors:
Elena Ferrari,
Romina Corsini,
Samuele E. Burastero,
Alberto Spisni

Description

The data refer to the allergen Mus m 1.0102 and its cysteine mutants MM-C138A, MM-C157A and MM-C138,157A. The data describes protein fold stability, ligand binding ability and allergenic potential. They were obtained by means of: 1) a Dynamic Light Scattering-based thermal stability assay, 2) a Fluorescence-based ligand-binding assay and 3) a basophil degranulation test. Analysis of the raw data produced the temperatures corresponding to the onset of the protein unfolding, the dissociation constants for N-Phenyl-1-naphthylamine ligand and the profiles of b-hexosaminidase release from RBL cells, sensitized with the serum of selected allergic patients and incubated with increasing protein concentrations. The data highlight the enhanced thermal stability of MM-C138A mutant, without a relevant modification of its binding function and in vitro allergenicity. The data contribute to the process of the recombinant allergen standardization, focused to its potential use in immunotherapy and diagnostics applications.

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Categories

Modified Allergen, Standardization of Allergen, Allergen Structure

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