Akram Amini, Mojtaba sankian, Mohammad Ali Assarehzadegan, Fatemeh Vahedi, AbdolReza Varasteh
Immunobiochemistry Lab., Immunology Research Center, Bu-Ali Research Institute, Mashhad, Iran. akaminiak@gmail.com
Molecular biology reports 2011 AprThe inhalation of Chenopodium album (C. album) pollen has been reported as an important cause of allergic respiratory symptoms. The aim of this study was to produce the recombinant profilin of C. album (rChe a 2) pollen and to investigate its cross-reactivity with other plant-derived profilins based on potential conformational epitopes and IgE reactivity analysis. Che a 2-coding sequence was cloned, expressed, and purified using one step metal affinity chromatography to recover high-purity target protein. We assessed cross-reactivity and predicted IgE potential epitopes among rChe a 2 and other plant-derived profilins. Immunodetection and inhibition assays using sixteen individual sera from C. album allergic patients demonstrated that purified rChe a 2 could be the same as that in the crude extract. The results of inhibition assays among rChe a 2 and other plant-derived profilins were in accordance with those of the homology of predicted conserved conformational regions. In this study, amino acid sequence homology analysis showed that a high degree of IgE cross-reactivity among plant-derived profilins may depend on predicted potential IgE epitopes.
Akram Amini, Mojtaba sankian, Mohammad Ali Assarehzadegan, Fatemeh Vahedi, AbdolReza Varasteh. Chenopodium album pollen profilin (Che a 2): homology modeling and evaluation of cross-reactivity with allergenic profilins based on predicted potential IgE epitopes and IgE reactivity analysis. Molecular biology reports. 2011 Apr;38(4):2579-87
PMID: 21086179
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