Purification, crystallization and preliminary X-ray analysis of a deletion mutant of a major buckwheat allergen

Abstract

A 16 kDa buckwheat protein (BWp16) is a major allergen responsible for immediate hypersensitivity reactions including anaphylaxis. A deletion mutant of BWp16 (rBWp16ÁN) was overproduced and purified and was shown to be immunologically active. A three-wavelength MAD data set was collected from a crystal of selenomethionine-labelled rBWp16ÁN. The crystal belonged to the triclinic space group P1, with unit-cell parameters a = 28.39, b = 31.54, c = 32.20 Å , = 111.92, = 108.91, = 98.74 . One monomer was expected to be present in the asymmetric unit based on the calculated Matthews coefficient of 1.76 Å 3 Da À1 .

Identification and characterization of the antigenic site (epitope) on bovine β‐lactoglobulin: common residues in linear and conformational epitopes

“…Principally, allergenic epitopes are divided in two main classes, namely (1) conformational epitopes, which are expected to be more susceptible to processing‐induced changes; and (2) linear epitopes, which are likely to be more resistant to physical treatments and to be deactivated only by hydrolysis . The allergic reaction has two stages: sensitisation and challenge.…”

“…more susceptible to processing-induced changes; and (2) linear epitopes, which are likely to be more resistant to physical treatments and to be deactivated only by hydrolysis. 11,12 The allergic reaction has two stages: sensitisation and challenge. In the first stage, food allergens are digested into small peptides which make a person sensitised.…”