| Abstract [eng] |
In the diagnosis and immunotherapy of allergies, allergen extracts are commonly used, which allow the identification of allergy sources, but are not suitable for the identification of individual molecules. Many of the problems associated with natural allergen extracts can be solved by the use of genetically engineered recombinant allergens. Biomedical researchers need large amounts of high-quality purified protein, but only a small number of proteins in natural hosts are synthesized in sufficient abundance. It depends on the characteristics of the protein which system to choose for its synthesis, and sometimes you have to try several of them to get the required result. Escherichia coli expression and Nicotiana benthamiana transient expression systems were chosen for the synthesis of plant allergens in this work. Mugword (lot. Artemisia vulgaris) Art v 1 and Art v 5, birch (lot. Betula pendula) Bet v 1 and ragweed (lot. Ambrosia artemisiifolia) Amb a 3 recombinant proteins have been successfully synthesized in the bacterial expression system. Mugword Art v 6, black alder (lot. Alnus glutinosa) Aln g 4, ragweed Amb a 4, olive (lot. Olea europaea) Ole e 7, Ole e 9 and Ole e 10, pear (lot. Pyrus communis) Pyr c 1 and Pyr c 3, timothy grass (lot. Phleum pratense) Phl p 13, peach (lot. Prunus persica) Pru p 3 recombinant proteins were synthesized in the plant expression system. Aln g 4, Amb a 4, Ole e 9, Pyr c 1, Pru p 3 and Pyr c 3 proteins were detected on SDS-PAGE polyacrylamide gels. |
