Molecular and structural analysis of a continuous birch profilin epitope defined by a monoclonal antibody
P Wiedemann, K Giehl, SC Almo, AA Fedorov… - Journal of Biological …, 1996 - ASBMB
The interaction of a mouse monoclonal antibody (4A6) and birch profilin, a structurally well
conserved actin-and phosphoinositide-binding protein and cross-reactive allergen, was
characterized. In contrast to serum IgE from allergic patients, which shows cross-reactivity
with most plants, monoclonal antibody 4A6 selectively reacted with tree pollen profilins.
Using synthetic overlapping peptides, a continuous hexapeptide epitope was identified. The
exchange of a single amino acid (Gln-47→ Glu) within the epitope was found to abolish the …
conserved actin-and phosphoinositide-binding protein and cross-reactive allergen, was
characterized. In contrast to serum IgE from allergic patients, which shows cross-reactivity
with most plants, monoclonal antibody 4A6 selectively reacted with tree pollen profilins.
Using synthetic overlapping peptides, a continuous hexapeptide epitope was identified. The
exchange of a single amino acid (Gln-47→ Glu) within the epitope was found to abolish the …
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