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Sankian M.,Bu Ali Research Institute | Talebi F.,Bu Ali Research Institute | Moghadam M.,Bu Ali Research Institute | Vahedi F.,Razi Vaccine and Serum Research Institute | And 3 more authors.
Allergology International | Year: 2011

Background: Oral allergy syndrome resulted from plant-derived foods is frequent among adults. Allergy to melon (cucumis melo) is one of the most frequent fruit allergies in Iran. Three different major allergens have been found in Cucumis melo that Cuc m 1 (cucumisin) has been identified as the major allergen of melon. Cucumisin is an alkaline serine protease that it is found as a 78 kDa protein in precursor form. The aim of this study was production of recombinant Cuc m 1 in Escherichia coli (E. coli) cells and characterization of its allergenicity property. Methods: Production of recombinant Cuc m 1 was carried out by cDNA cloning technique into the pET32b(+) vector using specific primers designed based on cucumisin nucleotide sequence available in Genebank database, cucumisin encoding gene and directional cloning method. Cloned plasmid into E. coli TOP10 was transformed into E. coli BL21 and expression of the protein was induced by IPTG. The recombinant protein was purified via Ni-NTA affinity chromatography using histidine tag in recombinant protein. IgE binding of this protein was assessed by IgE-immunoblotting, ELISA and inhibition ELISA. Results: The directional cloning was resulted in expression of a fusion Cuc m 1. Immunoblotting with sera of patients allergic to melon showed strong reactivity with purified protein band. Inhibition assays demonstrated that purified rCuc m 1 could be the same with natural form of Cuc m 1 in total extract. Conclusions: In the present study, we have provided a functional recombinant cucumisin allergen, rCuc m 1 with 86 kDa, which may be used as a standard allergen for clinical diagnosis and study of allergy to melon. © 2011 Japanese Society of Allergology. Source


Assarehzadegan M.A.,Ahvaz Jundis hapur University of Medical science | Assarehzadegan M.A.,Bu Ali Research Institute | Sankian M.,Ahvaz Jundis hapur University of Medical science | Sankian M.,Bu Ali Research Institute | And 6 more authors.
Allergology International | Year: 2010

Background: The inhalation of Salsola kali pollen is an important cause of pollinosis during summer and early fall throughout desert and semi-desert areas. Sal k 1 has been previously reported as a major allergen of S. kali pollen. In this study, we produced the recombinant Sal k 1 and also its low IgE-binding mutant form. We further compared the IgE binding ability of these two recombinant molecules. Methods: The recombinant Sal k 1 and its low IgE-binding variant, obtained by three amino acid exchanges (R142→S, P143→A, D144→V), were cloned and expressed in E. coli, as proteins fused with thioredoxin and His-tags, and then purified by Ni2+ affinity chromatography. The IgE-binding capacity of the wild-type and mutated rSal k 1 was compared using immunoblotting, ELISA and inhibition assays by ten sera from S. kali allergic patients. Moreover, in vivo IgE-reactivity was investigated by the skin prick test. Results: Both the recombinant and the mutated form of Sal k 1 were expressed in E. coli at a relatively high amount and soluble form. All sera recognized rSal k 1 via immunoassay analysis. In addition, inhibition assays demonstrated that the purified rSal k 1 was similar to its counterpart in the crude extract. The mutated rSal k 1 exhibited a reduced IgE-binding capacity against wild-type rSal k 1. Conclusions: This study demonstrates that purified rSal k 1 is comprised of IgE-epitopes similar to that of its natural counterpart and that the mutated variant showed a reduced IgE-binding capacity based on in vitro assays and in vivo provocation testing. © 2010 Japanese Society of Allergology. Source


Fazaeli S.M.,Ferdowsi University of Mashhad | Mahdie R.,Varastegan Institute for Medical Science | Shafaghati Y.,University of Social Welfare and Rehabilitation Sciences
Journal of Mazandaran University of Medical Sciences | Year: 2016

Branchio-oculo-facial (BOF) is a rare genetic disorder inherited as an autosomal dominant trait resulting from maldevelopment in the branchial arches. This paper presents a case of sporadic BOF for the first time in Iran. He was 2 years and 9 months old that was born in the first pregnancy (normal birth). His parents were healthy and they were 3rd degree relatives. The patient had normal intelligence. His obvious symptoms were holes in both sides of the neck (he had surgery at 6 months of age), broad nasal bridge, nasal duct obstruction, pseudocleft of the upper lip, submucos cleft palate, microphthalmia, and squint eye (more dropping in right eye). He also had hypernasal speech. This rare syndrome is accompanied with different anomalies, and physical and mental disorders, therefore, a team of specialists is needed in treatment of such patients. © 2016, Mazandaran University of Medical Sciences. All rights reserved. Source


Noorbakhsh R.,Ferdowsi University of Mashhad | Mortazavi S.A.,Ferdowsi University of Mashhad | Sankian M.,Mashhad University of Medical Sciences | Shahidi F.,Ferdowsi University of Mashhad | And 8 more authors.
Journal of Agricultural and Food Chemistry | Year: 2010

Pistachio (Pistacia vera) is a tree nut that has been reported to cause IgE-mediated allergic reactions. This study was undertaken to investigate the distinctions between different cultivars of pistachio nut and the influence of different processing on the IgE-binding capacity of whole pistachio protein extracts. The influence of different processes on allergenicity was investigated using competitive inhibition ELISA and Western blotting assays. The Western blotting results of extracts from pistachio cultivars showed no marked difference among them. The IgE-binding capacity was significantly lower for the protein extract prepared from steam-roasted than from raw and dry-roasted pistachio nuts. The results of sensory evaluation analysis and hedonic rating proved no significant differences in color, taste, flavor, and overall quality of raw, roasted, and steam-roasted pistachio nut treatments. The most significant finding of the present study was the successful reduction of IgE-binding by pistachio extracts using steam-roast processing without any significant changes in sensory quality of product. © 2010 American Chemical Society. Source


Noorbakhsh R.,Ferdowsi University of Mashhad | Noorbakhsh R.,Mashhad University of Medical Sciences | Mortazavi S.A.,Ferdowsi University of Mashhad | Sankian M.,Mashhad University of Medical Sciences | And 4 more authors.
Allergology International | Year: 2010

Background: Tree nut allergy is one of the common potentially life-threatening food allergies in children and adults. Recombinant food allergens offer new perspectives to solve problems of clinical and molecular allergology in diagnosis, research, and therapy of food allergies. So far, superoxide dismutase (s) has been identified as a panallergen and studied in different allergenic sources. Manganese Superoxide Dismutase (MnSOD) has also been reported in pistachio that may cause allergic reactions in atopic subjects. The aim of this study was to describe the cloning, expression, and purification of MnSOD from pistachio nut. Methods: The pistachio MnSOD was cloned and expressed in E. coli BL21 (DE3) using a vector pET-32b (+). A recombinant protein was purified by metal precipitation. The protein immunoreactivity was evaluated using patients' IgE binding by means of ELISA and immunoblotting assays. Results: The MnSOD gene from pistachio was successfully cloned and expressed in E. coli. The purified pistachio MnSOD was recognized by IgE in 10 (40%) out of the 25 sera tested. Our results also showed that this protein might trigger some cross-reactions toward IgE antibodies and thus could be considered as a panallergen. Conclusions: For the first time recombinant manganese superoxide dismutase from nut source was expressed as a possible allergen. This pistachio allergen could be a possible basis for cross-reactivity with MnSOD from other sources. © 2010 Japanese Society of Allergology. Source

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