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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’and 3’ 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