Stability of recombinant 2 S albumin allergens in vitro.
Two well known 2 S albumins, Ber e 1 from brazil nut and sunflower 2 S albumin 8 (SFA-8), have been expressed in a eukaryotic system and purified. Analysis of recombinant versions of Ber e 1 and SFA-8 revealed them to be significantly more resistant to digestion by pepsin than BSA, and to be stable for up to 30 min in simulated gastric fluid. Unfolding monitored by CD indicated that both proteins were also very resistant to denaturation induced by heat and low pH. These results suggest that, although the ability of 2 S albumins to reach the circulatory system may be a prerequisite for the allergenicity of this group of proteins, stability is just one of a number of characteristics that provoke a selective immune response.
Murtagh
G J
GJ
School of Life and Environmental Sciences, University of Nottingham, University Park, UK. gareth.murtagh@nottingham.ac.uk
Dumoulin
M
M
Archer
D B
DB
Alcocer
M J
MJ
D055516:2S Albumins, Plant; D052179:Antigens, Plant; D031383:Bertholletia / Q000378:metabolism; D002942:Circular Dichroism; D006368:Helianthus / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D066298:In Vitro Techniques; D010434:Pepsin A / Q000494:pharmacology; D010940:Plant Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry*; D012709:Serum Albumin / Q000494:pharmacology; D013997:Time Factors; D014466:Ultraviolet Rays
D055516:2S Albumins, Plant; D052179:Antigens, Plant; D010940:Plant Proteins; D011994:Recombinant Proteins; D012709:Serum Albumin; C067568:methionine-rich 2S protein, Helianthus; C103364:2S albumin, brazil nut; D010434:Pepsin A