The 159 residue Bet v 1 is the major allergen from birch tree pollen. Its natural function is
unknown although it is capable of binding several types of physiologically relevant ligands …

Background: Recently, a novel family of low–molecular–weight (8–9 kD), two–EF–hand
calcium–binding proteins has been described as allergens in plant pollens. Approximately …

Bet v 1 is a 17-kDa protein abundantly present in the pollen of the White birch tree and is the
primary cause of birch pollen allergy in humans. Its three-dimensional structure is …

The term allergy was coined in 1906 by the Austrian scientist and pediatrician Clemens
Freiherr von Pirquet. In 1976, Dietrich Kraft became the head of the Allergy and Immunology …

The ability of pathogenesis-related proteins of family 10 to bind a broad spectrum of ligands
is considered to play a key role for their physiological and pathological functions. In …

Pathogenesis-related plant proteins of class-10 (PR-10) are essential for storage and
transport of small molecules. A prominent member of the PR-10 family, the major birch …

We have isolated a cDNA clone coding for a birch pollen allergen, Bet v 4. The deduced
amino acid sequence of Bet v 4 contained two typical EF-hand calcium-binding domains …

Birch pollinosis is one of the prevailing allergic diseases. In all, 5–20% of birch pollinotics
mount IgE antibodies against the minor birch pollen allergen Bet v 4, a Ca2+-binding …

Many allergens share several biophysical characteristics, including the capability to undergo
oligomerization. The dimerization mechanism in Bet v 1 and its allergenic properties are so …

Bet v 1, the major allergen of birch pollen, displays a considerable degree of heterogeneity.
Several charge variants have been detected by two-dimensional IgE immunoblots and …