1. Sal k 4, a new allergen of Salsola kali, is profilin: a predictive value of conserved conformational regions in cross-reactivity with other plant-derived profilins.
- Author
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Assarehzadegan MA, Amini A, Sankian M, Tehrani M, Jabbari F, and Varasteh A
- Subjects
- Amino Acid Sequence, Cloning, Molecular, Enzyme-Linked Immunosorbent Assay, Escherichia coli genetics, Female, Humans, Immunoglobulin E immunology, Male, Models, Molecular, Molecular Sequence Data, Plant Proteins biosynthesis, Plant Proteins chemistry, Plant Proteins immunology, Plant Proteins isolation & purification, Profilins biosynthesis, Profilins isolation & purification, Protein Conformation, Sequence Analysis, DNA, Sequence Homology, Amino Acid, Skin immunology, Allergens, Conserved Sequence, Cross Reactions, Pollen, Profilins chemistry, Profilins immunology, Salsola immunology
- Abstract
The aim of this study was to investigate a new allergen of Salsola kali, Sal k 4, and to investigate the predictive value of the conserved conformational regions in cross-reactivity with other plant-derived profilins. The Sal k 4-coding sequence was cloned, expressed, and purified by one-step Ni2+ affinity chromatography to recover high-purity target protein. We assessed cross-reactivity and predicted conserved conformational regions among rSal k 4 and other plant-derived profilins. Immunodetection and inhibition assays using 30 individual sera from S. kali allergic patients indicated that purified rSal k 4 might be the same as that in the crude extract. The results of inhibition assays among rSal k 4 and other plant-derived profilins were in accordance with the homology of the predicted conserved conformational regions. Amino acid sequence homology analysis showed that a high degree of IgE cross-reactivity among plant-derived profilins might depend on the predicted conserved conformational regions.
- Published
- 2010
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