Abstract
Background: Immunoglobulin E (IgE) epitopes of β-lactoglubulin (βLG) have been identified by ELISA inhibition methods using sera from allergic patients. However, the functional capacity of these epitopes to stimulate mast cells is unknown. It is the goal of the present study to identify bivalent IgE epitopes of βLG able to trigger target mast cells. Methods:Peptides were obtained either by purification from tryptic hydrolysates of βLG or by synthesis. They were examined for their triggering activity in vitro on peritoneal <sup>3</sup>H-serotonin-labeled rat mast cells passively sensitized with IgE anti-βLG antibodies. In vivo, rats immunized with βLG were administered peptides by gavage for intestinal rat mast cell protease II release. Results: Compared with intact βLG, purified or synthetic tryptic-like βLG peptides have a sharply decreased allergenicity. Peptide 149–162 retains the highest bivalent IgE epitope-mediated triggering capacity. Conclusion: A functional bivalent IgE epitope was identified at the C terminal end of βLG.
Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
