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'); Reports of Biochemistry and Molecular Biology rbmb.net Basic Sciences http://rbmb.net 1 admin 2322-3480 2322-3480 10.61882/rbmb en jalali 1392 2 1 gregorian 2013 5 1 1 2 online 1 fulltext
en Molecular Cloning, Characterization, and Expression of Cuc m 2, a Major Allergen in Cucumis melo ایمنی شناسی Immunology <p style="text-align: justify;"><em><strong>Background:</strong></em> Several studies reported the clinical features of IgE-mediated hypersensitivity after ingestion of melon. Melon allergy is a common IgE-mediated fruit allergy in Iran. This prompted us to investigate immunochemical and molecular properties of the major allergen in melon fruit, to compare the IgE-binding capacity of the natural protein with the recombinant allergen, and to determine cross-reactivity of the major allergen with closely-related allergens from other plants displaying clinical cross-reactivity with melon.</p> <p style="text-align: justify;"><em><strong>Methods:</strong></em> Identification and molecular characterization of the major melon allergen were performed using IgE immunoblotting, allergen-specific ELISA, affinity-based purifications, cross-inhibition assays, cloning, and expression of the allergen in Escherichia coli.</p> <p style="text-align: justify;"><em><strong>Results:</strong></em> Melon profilin was identified and isolated as a major IgE-binding component and designated as Cuc m 2. Sequencing corresponding cDNA revealed an open reading frame of 363 bp coding for 131 amino acid residues and two fragments of 171 bp and 383 bps for the 5&rsquo;and 3&rsquo; UTRs, respectively. Significant cross-reactivity was found between melon profilin and Cynodon dactylon, tomato, peach, and grape profilins in cross-inhibition assays. Although the highest degree of amino acid identity was revealed with watermelon profilin, there was no significant cross-reactivity between melon and watermelon profilins.</p> <p style="text-align: justify;"><em><strong>Conclusion:</strong></em> Melon profilin is the major IgE-binding component in melon extract, and the recombinant and natural forms exhibited similar IgE-binding capacities. A part of the fruit-fruit and pollen-fruit cross-reactions could be explained by the presence of this conserved protein; however, sequence homology provides insufficient information to predict IgE cross-reactivity of profilins.</p> Cross-reactivity, Fruit allergy, Melon, Profilin, Recombinant allergen 49 63 http://rbmb.net/browse.php?a_code=A-10-1-9&slc_lang=en&sid=1 Mojtaba Sankian 10031947532846005923 10031947532846005923 No Immunology Research Center, School of Medicine, Mashhad University of Medical Sciences, Mashhad, Iran Mahmoud Mahmoudi 10031947532846005924 10031947532846005924 No Immunology Research Center, School of Medicine, Mashhad University of Medical Sciences, Mashhad, Iran Abdol-Reza Varasteh varasteha@mums.ac.ir 10031947532846005925 10031947532846005925 Yes Allergy Research Center, School of Medicine, Mashhad University of Medical Sciences, Mashhad, Iran