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ABSTRACT: Background
Recombinant Bet v 1a (rBet v 1a) has been used in allergy research for more than three decades, including clinical application of so-called hypoallergens. Quantitative IgE binding to rBet v 1a depends on its native protein conformation, which might be compromised upon heterologous expression, purification, or mutational engineering of rBet v 1a.Objective
To correlate experimental/theoretical comparisons of IgE binding of defined molar ratios of folded/misfolded recombinant Bet v 1a variants and to determine accuracy and precision of immuno- and physicochemical assays routinely used to assess the quality of recombinant allergen preparations.Methods
rBet v 1a and its misfolded variant rBet v 1aS112P/R145P were heterologously expressed and purified from Esch
SUBMITTER: Husslik F
PROVIDER: S-EPMC4506129 | biostudies-literature | 2015
REPOSITORIES: biostudies-literature