Identification of profilin as a novel pollen allergen; IgE autoreactivity in sensitized individuals.
A complementary DNA encoding a pollen allergen from white birch (Betula verrucosa) that was isolated from a pollen complementary DNA library with serum immunoglobulin E from a birch pollen-allergic individual revealed significant sequence homology to profilins. The recombinant protein showed high affinity to poly-L-proline. Immunoglobulin E antibodies from allergic individuals bound to natural and recombinant birch profilin and also to human profilin. In addition, birch and human profilin induced histamine release from blood basophils of profilin-allergic individuals, but not of individuals sensitized to other plant allergens. The structural similarity of conserved proteins might therefore be responsible for maintaining immunoglobulin E antibody titers in type I allergy.
Valenta
R
R
Institute of General and Experimental Pathology, University of Vienna, Austria.
Duchêne
M
M
Pettenburger
K
K
Sillaber
C
C
Valent
P
P
Bettelheim
P
P
Breitenbach
M
M
Rumpold
H
H
Kraft
D
D
Scheiner
O
O
D000595:Amino Acid Sequence; D003285:Contractile Proteins / Q000276:immunology; D015723:Gene Library; D006801:Humans; D006967:Hypersensitivity; D015151:Immunoblotting; D007073:Immunoglobulin E / Q000276:immunology*; D008840:Microfilament Proteins / Q000235:genetics / Q000276:immunology*; D008969:Molecular Sequence Data; D011058:Pollen / Q000276:immunology*; D051304:Profilins; D011994:Recombinant Proteins / Q000276:immunology; D012441:Saccharomyces cerevisiae / Q000235:genetics; D012689:Sequence Homology, Nucleic Acid
D003285:Contractile Proteins; D008840:Microfilament Proteins; D051304:Profilins; D011994:Recombinant Proteins; D007073:Immunoglobulin E