Abstract
Four recombinant (r) allergens (rAmb a 8.0101, rArt v 4.0101, rBet v 2.0101, and rPhl p 12.0101) were successfully produced and used for sensitization studies. The allergens belong to the profilin family which is one of the most numerous allergen families. These four proteins represent allergens originating from pollen of weeds (rAmb a 8.0101 and rArt v 4.0101), tree (rBet v 2.0101) and grass (rPhl p 12.0101). The recombinant allergens were characterized using various biochemical and biophysical methods and tested for their ability to bind patient-derived antibodies. One hundred patients aged 2 to 50 years sensitized to pollen and plant-derived food allergens (IgE > 0.35 kU/L) were included. Sensitization to individual allergen sources and components of birch and timothy pollens was evaluated using multiparameter immunoblots. The presence of IgE to pollen-derived recombinant profilins rAmb a 8.0101, rArt v 4.0101, rBet v 2.0101, and rPhl p 12.0101 in serum was evaluated using ELISA method. The presence of IgE against pollen profilins was detected in 20 out of 100 studied patients. High correlation was seen between IgE ELISA results with individual pollen profilins. In summary, it was shown that the recombinant versions of the four allergenic profilins can be used for sensitization studies and for component-resolved allergy diagnostics.
Highlights
Profilins are ubiquitous, small proteins ranging between 12–16 kDa that are expressed in all eukaryotic cells and certain viruses, with the exception of some protists [1,2]
The reaction was quantified by measuring color intensity at 405 nm and the results presented as optical density (OD)
Our study demonstrates that the presence of immunoglobulin E E (IgE) to profilins in patients with pollen-food syndrome is quite frequent
Summary
Small proteins ranging between 12–16 kDa that are expressed in all eukaryotic cells and certain viruses, with the exception of some protists [1,2]. The profilin family shares highly conserved amino acid sequences, even among distantly related sources [4]. This holds true for profilins derived from different plants that are highly similar to each other, sharing approximately 80% amino. Molecules 2020, 25, 369 derived from different plants that are highly similar to each other, sharing approximately 80% amino acid identity [4]. This renders them as panallergens, but minor allergens widespread in pollens and foods, and and responsible responsible for for immunoglobulin immunoglobulin E E (IgE). Structural structural and and foods, immunological analyses of profilins indicate that profilins present in pollens and plant-derived foods immunological analyses of profilins indicate that profilins present in pollens and plant-derived foods are highly highlycross-reactive cross-reactive
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