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1.
Allergol Int ; 60(4): 425-32, 2011 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-21593580

RESUMO

BACKGROUND: Tree nut allergy is characterized by a high frequency of life-threatening reactions and is typically lifelong persistent. Some people with a pistachio nut allergy, which is common in the pistachio rich area of Iran, develop a hypersensitivity to other tree nuts as well. The aim of this study was to investigate the prevalence of pistachio nut allergy in Iran, the major pistachio cultivation region in the world. The study also addressed the presence of allergenic cross-reactivity between pistachio and other nuts, including almond, peanut, and cashew in pistachio allergic patients. METHODS: A survey was conducted to determine whether the prevalence of pistachio allergy is affected by exposure to this nut in pistachio cultivation regions, as well as possible cross-reactivity between pistachio and other nuts including cashew, almond, and peanut. Inhibition Western blot and inhibition ELISA studies were conducted to assess the presence of allergenic cross-reactivity between pistachio and the other tree nuts. RESULTS: Our results revealed that the prevalence of pistachio allergy is twice as much in pistachio cultivation regions than other areas. Western blotting and inhibition ELISA presented high percentages of inhibition with pistachio and cashew, followed by almond and, to some degree, peanut which indicates different levels of allergenic cross-reactivity. CONCLUSIONS: The results indicate that exposure of people to pistachio significantly affects the prevalence of its allergic reactions. In addition, it was observed that, among pistachio allergic subjects, such exposure may affect the co-sensitivities with other nuts, including cashew and almond. The plant taxonomic classification of pistachio and other tree nuts does appear to predict allergenic cross-reactivity.


Assuntos
Alérgenos/imunologia , Hipersensibilidade a Noz/epidemiologia , Hipersensibilidade a Noz/imunologia , Pistacia/imunologia , Adolescente , Adulto , Criança , Reações Cruzadas , Ensaio de Imunoadsorção Enzimática , Feminino , Humanos , Imunoglobulina E/imunologia , Irã (Geográfico)/epidemiologia , Masculino , Prevalência , Adulto Jovem
2.
Allergol Int ; 60(3): 309-16, 2011 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-21430432

RESUMO

BACKGROUND: Pollinosis from Amaranthus retroflexus pollen is a common cause of respiratory allergy in Iran with a high positive rate (68.8%) among Iranian allergic patients. The aim of the present study was to evaluate the allergenicity of the A. retroflexus pollen profilin. METHODS: Using sera from twelve patients allergic to A. retroflexus pollen, IgE-binding proteins from the A. retroflexus pollen extract was identified by immunoblotting. The cDNA of A. retroflexus pollen profilin was amplified, then cloned into the pET-21b (+) vector, expressed in Escherichia coli, and finally purified by metal affinity chromatography. The IgE-binding capacity of the recombinant protein was then analyzed by the ELISA, immunoblotting, and inhibition assays, as well as by the skin prick test (SPT). RESULTS: Immunoblotting results indicated a 14.6kDa protein with IgE-reactivity to 33% (4/12) among A. retroflexus pollen-allergic patients. Nucleotide sequencing of the cDNA revealed an open reading frame of 399 bp encoding for 133 amino acid residues which was belonged to the profilin family and designated as Ama r 2. A recombinant Ama r 2 (rAma r 2) was then produced in E. coli as a soluble protein which showed a strong IgE-reactivity via ELISA confirmed by the SPT. Inhibition experiments revealed high IgE cross-reactivities with the profilins from other plants. CONCLUSIONS: The profilin from the A. retroflexus pollen, Ama r 2, was firstly identified as an allergen. Moreover, rAma r 2 was produced in E. coli as a soluble immunoreactive protein with an IgE-reactivity similar to that of its natural counterpart.


Assuntos
Alérgenos/imunologia , Amaranthus/imunologia , Pólen/imunologia , Profilinas/imunologia , Adulto , Alérgenos/genética , Alérgenos/metabolismo , Amaranthus/genética , Sequência de Aminoácidos , Reações Antígeno-Anticorpo/imunologia , Escherichia coli/genética , Escherichia coli/metabolismo , Feminino , Humanos , Hipersensibilidade/etiologia , Hipersensibilidade/imunologia , Hipersensibilidade/metabolismo , Imunoglobulina E/sangue , Imunoglobulina E/imunologia , Masculino , Pessoa de Meia-Idade , Dados de Sequência Molecular , Pólen/genética , Pólen/metabolismo , Profilinas/genética , Profilinas/metabolismo , Alinhamento de Sequência , Homologia de Sequência de Aminoácidos , Adulto Jovem
3.
J Agric Food Chem ; 58(18): 10231-5, 2010 Sep 22.
Artigo em Inglês | MEDLINE | ID: mdl-20735130

RESUMO

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.


Assuntos
Alérgenos/imunologia , Manipulação de Alimentos/métodos , Hipersensibilidade a Noz/imunologia , Nozes/imunologia , Pistacia/imunologia , Adulto , Feminino , Humanos , Imunoglobulina E/imunologia , Imunoglobulina E/metabolismo , Masculino , Hipersensibilidade a Noz/sangue , Nozes/metabolismo , Pistacia/metabolismo , Proteínas de Plantas/imunologia , Proteínas de Plantas/metabolismo , Controle de Qualidade , Especificidade da Espécie , Adulto Jovem
4.
Allergol Int ; 59(3): 295-304, 2010 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-20567132

RESUMO

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.


Assuntos
Alérgenos/imunologia , Hipersensibilidade a Noz/imunologia , Proteínas de Vegetais Comestíveis/imunologia , Proteínas Recombinantes/imunologia , Superóxido Dismutase/imunologia , Adolescente , Adulto , Alérgenos/biossíntese , Alérgenos/química , Alérgenos/genética , Criança , Biologia Computacional , Reações Cruzadas , Feminino , Humanos , Imunoglobulina E/metabolismo , Masculino , Pessoa de Meia-Idade , Hipersensibilidade a Noz/diagnóstico , Hipersensibilidade a Noz/terapia , Pistacia/efeitos adversos , Proteínas de Vegetais Comestíveis/biossíntese , Proteínas de Vegetais Comestíveis/química , Proteínas de Vegetais Comestíveis/genética , Conformação Proteica , Proteínas Recombinantes/biossíntese , Proteínas Recombinantes/química , Proteínas Recombinantes/genética , Superóxido Dismutase/biossíntese , Superóxido Dismutase/química , Superóxido Dismutase/genética , Adulto Jovem
5.
Allergol Int ; 58(2): 261-6, 2009 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-19307776

RESUMO

BACKGROUND: Pollens from the Salsola spp. are an important source of respiratory allergy in tropical countries. Our aim was to characterize the IgE binding proteins of S. incanescens pollen extract and study its cross-reactivity with S. kali pollen allergens. METHODS: Prick tests with S. kali and S. incanescens pollen extracts were performed on eight respiratory allergy patients from Mashhad, Northeast Iran. The antigenic profiles and IgE-binding patterns of S. kali and S. incanescens pollen extracts were compared by SDS-PAGE and Western blotting, using individual sera from the salsola pollen-sensitive patients. Cross-reactivity of proteins in the two weeds was assessed by IgE- immunoblotting inhibition. RESULTS: S. kali and S. incanescens pollen extracts showed similar IgE-binding profiles in Western blotting. The IgE binding components of 39, 45, 66 and 85 kDa were detected in both pollen extracts. Furthermore, inhibition of the immunoblots revealed extensive inhibition of IgE binding to proteins and a close relationship between these two weeds allergens. CONCLUSIONS: S. incanescens pollen is a potent allergen source with several IgE binding components that shows a close allergenic relationship with S. kali. Our results suggest that in S. incanescens-rich areas, S. kali pollen extracts could be used as a diagnostic reagent for allergic patients to S. incanescens pollen.


Assuntos
Reações Cruzadas/imunologia , Rinite Alérgica Sazonal/imunologia , Salsola/imunologia , Adulto , Antígenos de Plantas/análise , Antígenos de Plantas/imunologia , Ligação Competitiva/imunologia , Western Blotting , Feminino , Humanos , Imunoglobulina E/imunologia , Irã (Geográfico) , Masculino , Proteínas de Plantas/análise , Proteínas de Plantas/imunologia , Pólen/química , Pólen/imunologia , Rinite Alérgica Sazonal/diagnóstico , Salsola/anatomia & histologia , Testes Cutâneos , Adulto Jovem
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