Bet v I allergen is a family of protein allergens. Allergies are hypersensitivity reactions of the immune system to specific substances called allergens that, in most people, result in no symptoms. Trees within the order Fagales possess particularly potent allergens, e.g. the prototypical Bet v 1, the major white birch pollen antigen. Bet v 1 is the main cause of type I allergies observed in early spring. Type I, or immunoglobulin E-mediated allergies affect 1 in 5 people in Europe and North America. Commonly observed symptoms are hay fever, dermatitis, asthma and, in severe cases, anaphylactic shock. First contact with these allergens results in sensitisation; subsequent contact produces a cross-linking reaction of IgE on mast cells and concomitant release of histamine. The inevitable symptoms of an allergic reaction ensue.
Categorization
A nomenclature system has been established for antigens that cause IgE-mediated atopic allergies in humans. This nomenclature system is defined by a designation that is composed of the first three letters of the genus; a space; the first letter of the species name; a space and an Arabic number. In the event that two species names have identical designations, they are discriminated from one another by adding one or more letters to each species designation. The allergens in this family include allergens with the following designations: Bet v 1, Dau c 1, and Pru a 1. Other proteins belonging to this family include the major pollen allergens:
Aln g I from Alnus glutinosa ;
Api G I from Apium graveolens ;
Car b I from Carpinus betulus ;
Cor a I from Corylus avellana ;
Mal d I from Malus domestica.
Structure
NMR analysis has confirmed earlier predictions of the protein structure and site of the major T-cell epitope. The Bet v 1 protein comprises 6 anti-parallel beta-strands and 3 alpha-helices. Four of the strands dominate the global fold, and 2 of the helices form a C-terminal amphipathic helical motif. This motif is believed to be the T-cell epitope. However, one very striking feature of the three-dimensional structure of Bet v 1 is the presence of a large hydrophobic cavity, which is open to the exterior and probably functions as a ligand binding site. The motif is also found in:
the disease resistance response proteins, STH-2 and STH-21, from Solanum tuberosum and pI49, pI176 and DRRG49-C from Pisum sativum ;
the P.sativum abscisic acid-responsive proteins ABR17 and ABR18;
and the stress-induced protein SAM22 from Glycine max.
Additionally, the core domain of Bet v 1 founds or is part of a superfamily of domains called SRPBCC that include the StAR-related lipid-transfer domain.
Function
The biological function of Bet v 1 is still under investigations. Bet v 1 harbors a large hydrophobic pocket and is able to bind a large spectra of ligands in it like hormones and siderophores like flavenols. It belongs to the pathogenesis-related proteins, which are usually expressed upon infections and stressful conditions, implicating a role in host defense. In vitro, Bet v 1 has been shown to be immune-suppressive, when its pocket was filled by a ligand, but was able to mount a Th2-response important in allergy development, when the pocket remained empty.
