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1.
Food Chem ; 302: 125350, 2020 Jan 01.
Artigo em Inglês | MEDLINE | ID: mdl-31415999

RESUMO

The aim of the study was to investigate the use of serine protease from Yarrowia lipolytica yeast for reduction of milk proteins allergenicity. Whey protein concentrate (WPC-80), αs-casein and their hydrolysates were analyzed for the capacity to bind IgE and IgG antibodies present in sera from patients with cow milk protein allergy using a competitive ELISA. The hydrolysis of αs-casein and whey protein concentrate contributed to a significant reduction of their immunoreactive epitopes. In case of IgE antibodies, the lowest binding capacity was detected in the 24 h hydrolysates of both proteins in which the inhibition of the reaction was ≤20 and ≤68% for αs-casein and whey protein concentrate respectively. One hour hydrolysis of WPC-80 reduced the protein antigenicity, while the longer time (5 h) might lead to the exposure of new IgE - reactive epitopes.


Assuntos
Hipersensibilidade a Leite/imunologia , Proteínas do Leite/imunologia , Hidrolisados de Proteína/imunologia , Serina Proteases/metabolismo , Alérgenos/imunologia , Alérgenos/metabolismo , Animais , Caseínas/imunologia , Caseínas/metabolismo , Pré-Escolar , Ensaio de Imunoadsorção Enzimática , Epitopos , Feminino , Cabras/imunologia , Humanos , Imunoglobulina E/imunologia , Imunoglobulina E/metabolismo , Imunoglobulina G/imunologia , Imunoglobulina G/metabolismo , Proteínas do Leite/metabolismo , Hidrolisados de Proteína/metabolismo , Proteínas do Soro do Leite/imunologia , Proteínas do Soro do Leite/metabolismo , Yarrowia/enzimologia
2.
Food Chem ; 302: 125333, 2020 Jan 01.
Artigo em Inglês | MEDLINE | ID: mdl-31416005

RESUMO

This study was performed to determine Parvalbumin (PV), a well-known fish allergenic protein, digestion kinetics and immunoreactivity of digestion products with Immunoglobulin G/Immunoglobulin E recognition to understand its allergic potential with or without lipid emulsion process. PV was subjected to simulated gastrointestinal digestion in emulsified condition. Digestion kinetics of the protein was analysed by electrophoresis, IgG/IgE binding ability by immunoblotting and indirect ELISA. Lipid emulsion significantly (p < 0.01) reduced the degree of PV hydrolysis by 52.10% for gastric digestion. Immune fragments of gastric digestion were detectable for 90-120 min longer in emulsified condition showing resistance. Consequently, lipid emulsion decreased the digestive ability of PV in stomach, increasing resistance to gastrointestinal digestion by pepsin proteases. It also altered IgG/IgE binding ability of digestion products, thereby indicating that PV with lipid emulsion was resistant to digestion and possessed increased IgE binding ability resulting in higher risk of allergy among sensitized individuals.


Assuntos
Alérgenos/farmacocinética , Emulsões/farmacocinética , Proteínas de Peixes da Dieta/farmacocinética , Hipersensibilidade Alimentar/imunologia , Parvalbuminas/farmacocinética , Alérgenos/imunologia , Alérgenos/metabolismo , Animais , Digestão , Emulsões/química , Ensaio de Imunoadsorção Enzimática , Feminino , Proteínas de Peixes da Dieta/imunologia , Linguados , Hipersensibilidade Alimentar/etiologia , Immunoblotting , Imunoglobulina E/imunologia , Imunoglobulina E/metabolismo , Imunoglobulina G/imunologia , Imunoglobulina G/metabolismo , Lipídeos/química , Lipídeos/farmacocinética , Camundongos Endogâmicos BALB C , Parvalbuminas/imunologia , Parvalbuminas/metabolismo , Pepsina A/metabolismo
3.
Zhonghua Nei Ke Za Zhi ; 58(11): 826-828, 2019 Nov 01.
Artigo em Chinês | MEDLINE | ID: mdl-31665859

RESUMO

This study aims to explore the diagnostic value of specific immunoglobulin E (sIgE) and specific immunoglobulin G (sIgG) of Aspergillus fumigatus in the diagnosis of allergic broncho-pulmonary aspergillosis (ABPA) and severe asthma with fungal sensitization (SAFS). A total of 17 ABPA patients and 14 SAFS patients were enrolled. The levels of sIgG [2 294.00 (1 527.00, 14 170.00) U/ml vs. 972.60 (650.90, 1 792.00) U/ml] and sIgE [8.77 (1.64, 16.85) kU/L vs. 1.04 (0.70, 2.05) kU/L] in ABPA patients were significantly higher than those in SAFS patients (P<0.05). Aspergillus fumigatus sIgG was strongly correlated with Aspergillus fumigatus sIgE (r(s)=0.797, P<0.001) in ABPA patients. When combined with Aspergillus fumigatus sIgG (>1 000.00 U/mL) and Aspergillus fumigatus sIgE (>1.00 kU/L), the sensitivity was 82.3% and specificity 78.6% for the differential diagnosis of ABPA and SAFS. It demonstrates the diagnostic value of Aspergillus fumigatus sIgG and sIgE.


Assuntos
Aspergilose Broncopulmonar Alérgica/diagnóstico , Aspergillus fumigatus/isolamento & purificação , Asma/complicações , Imunoglobulina E/sangue , Imunoglobulina G/sangue , Anticorpos Antifúngicos/imunologia , Aspergilose Broncopulmonar Alérgica/sangue , Aspergilose Broncopulmonar Alérgica/imunologia , Aspergilose Broncopulmonar Alérgica/microbiologia , Aspergillus fumigatus/imunologia , Asma/sangue , Asma/diagnóstico , Humanos , Imunoglobulina E/imunologia , Imunoglobulina G/imunologia , Índice de Gravidade de Doença
4.
J Agric Food Chem ; 67(46): 12918-12926, 2019 Nov 20.
Artigo em Inglês | MEDLINE | ID: mdl-31668066

RESUMO

The triosephosphate isomerase (TIM), Scy p 8, is a crab allergen and shows cross-reactivity in the shellfish. Here, recombinant Scy p 8 was expressed, and its crystal structure was determined at a resolution of 1.8 Å. The three-dimensional structure of Scy p 8 is primarily composed of a (ß/α)8-barrel motif prototype. Additionally, Scy p 8 showed cross-reactivity with high sequential and secondary structural identity among TIMs from shellfish species. The site-directed mutagenesis of critical amino acids of conformational epitopes was carried out, and the mutants of Trp 168 and Lys 237 to Ala reduced immunoglobulin E (IgE)-binding activity by approximately 30%, compared with wild-type TIM in an inhibition ELISA; however, it still induced basophil activation despite the interpatient variability between patients. These results can help to provide an accurate template for the analysis of the IgE binding and establish meaningful relationships between structure and allergenicity.


Assuntos
Braquiúros/enzimologia , Epitopos/química , Triose-Fosfato Isomerase/imunologia , Sequência de Aminoácidos , Animais , Braquiúros/química , Braquiúros/genética , Braquiúros/imunologia , Reações Cruzadas , Cristalização , Epitopos/genética , Epitopos/imunologia , Humanos , Imunoglobulina E/imunologia , Conformação Molecular , Conformação Proteica , Alinhamento de Sequência , Frutos do Mar/análise , Hipersensibilidade a Frutos do Mar/imunologia , Triose-Fosfato Isomerase/química , Triose-Fosfato Isomerase/genética
5.
Toxicol Lett ; 317: 59-67, 2019 Dec 15.
Artigo em Inglês | MEDLINE | ID: mdl-31577921

RESUMO

Toluene-diisocyanate (TDI) is mainly used in the manufacturing process of polyurethane foams, and is a potent inducer of occupational asthma characterized by airway inflammation and airway hyperreactivity. Thymic stromal lymphopoietin (TSLP) plays an important role in the development of asthma, and correlating with the differentiation of Th2 and Th17 cells. However, the role of TSLP in TDI-induced asthma remains unclear. In this study, 96 TDI-exposed workers as well as a mouse model of TDI-induced asthma were investigated. The air exposure assessment result of TDI in the workplace showed that workers were exposed to inhalation of a very high concentration of TDI, approximately 8 times the recommended level, leading to a decrease in pulmonary function and an increase in inflammatory cells, as well as TSLP and IgE levels in the supernatant of sputum obtained from exposed workers. In order to further investigate the role of TSLP in the pathogenesis of TDI-induced asthma, a mouse model of TDI-induced asthma was also employed. Histopathological analysis of mouse lung and bronchus showed an obvious infiltration of inflammatory cells around the bronchus. The levels of inflammatory cells, IFN-γ, IL-4 and IL-17 in bronchoalveolar lavage fluid (BALF), the expression levels of TSLP protein and ROR-γt and IL-17 mRNA in mouse lung tissues were also significantly increased. However, after treatment with TSLP neutralizing antibody (TSLP-Ab), the degree of pulmonary and bronchial inflammation in mice was significantly alleviated, and the levels of inflammatory cells, IFN-γ, IL-4 and IL-17 in BALF, and the expression levels of ROR-γt and IL-17 mRNA in lung tissue were significantly decreased. Our data shows that TSLP plays an important role in the pathogenesis of TDI-induced asthma, and that TSLP-Ab can effectively alleviate TDI-induced airway inflammation of asthma.


Assuntos
Anti-Inflamatórios/farmacologia , Anticorpos Neutralizantes/farmacologia , Asma/prevenção & controle , Citocinas/antagonistas & inibidores , Mediadores da Inflamação/antagonistas & inibidores , Pulmão/efeitos dos fármacos , Pneumonia/prevenção & controle , Tolueno 2,4-Di-Isocianato/efeitos adversos , Adulto , Animais , Asma/induzido quimicamente , Asma/imunologia , Asma/metabolismo , Estudos de Casos e Controles , Estudos Transversais , Citocinas/imunologia , Citocinas/metabolismo , Humanos , Imunoglobulina E/imunologia , Mediadores da Inflamação/imunologia , Mediadores da Inflamação/metabolismo , Exposição por Inalação/efeitos adversos , Interleucina-17/imunologia , Pulmão/imunologia , Pulmão/metabolismo , Masculino , Camundongos Endogâmicos BALB C , Pessoa de Meia-Idade , Exposição Ocupacional/efeitos adversos , Pneumonia/induzido quimicamente , Pneumonia/imunologia , Pneumonia/metabolismo , Transdução de Sinais/efeitos dos fármacos
6.
N Engl J Med ; 381(14): 1321-1332, 2019 10 03.
Artigo em Inglês | MEDLINE | ID: mdl-31577874

RESUMO

BACKGROUND: In the majority of patients with chronic spontaneous urticaria, most currently available therapies do not result in complete symptom control. Ligelizumab is a next-generation high-affinity humanized monoclonal anti-IgE antibody. Data are limited regarding the dose-response relationship of ligelizumab and the efficacy and safety of ligelizumab as compared with omalizumab and placebo in patients who have moderate-to-severe chronic spontaneous urticaria that is inadequately controlled with H1-antihistamines at approved or increased doses, alone or in combination with H2-antihistamines or leukotriene-receptor antagonists. METHODS: In a phase 2b dose-finding trial, we randomly assigned patients to receive ligelizumab at a dose of 24 mg, 72 mg, or 240 mg, omalizumab at a dose of 300 mg, or placebo, administered subcutaneously every 4 weeks for a period of 20 weeks, or a single 120-mg dose of ligelizumab. Disease symptoms of hives, itch, and angioedema were monitored by means of weekly activity scores. The main objective was to determine a dose-response relationship for the complete control of hives (indicated by a weekly hives-severity score of 0, on a scale from 0 to 21, with higher scores indicating greater severity); the primary end point of this response was assessed at week 12. Complete symptom control was indicated by a weekly urticaria activity score of 0 (on a scale from 0 to 42, with higher scores indicating greater severity). Safety was analyzed throughout the trial. RESULTS: A total of 382 patients underwent randomization. At week 12, a total of 30%, 51%, and 42% of the patients treated with 24 mg, 72 mg, and 240 mg, respectively, of ligelizumab had complete control of hives, as compared with 26% of the patients in the omalizumab group and no patients in the placebo group. A dose-response relationship was established. At week 12, a total of 30%, 44%, and 40% of the patients treated with 24 mg, 72 mg, and 240 mg, respectively, of ligelizumab had complete control of symptoms, as compared with 26% of the patients in the omalizumab group and no patients in the placebo group. In this small and short trial, no safety concerns regarding ligelizumab or omalizumab emerged. CONCLUSIONS: A higher percentage of patients had complete control of symptoms of chronic spontaneous urticaria with ligelizumab therapy of 72 mg or 240 mg than with omalizumab or placebo. (Funded by Novartis Pharma; ClinicalTrials.gov number, NCT02477332.).


Assuntos
Antialérgicos/administração & dosagem , Anticorpos Anti-Idiotípicos/administração & dosagem , Anticorpos Monoclonais Humanizados/administração & dosagem , Omalizumab/administração & dosagem , Urticária/tratamento farmacológico , Adulto , Idoso , Antialérgicos/efeitos adversos , Anticorpos Anti-Idiotípicos/efeitos adversos , Anticorpos Monoclonais Humanizados/efeitos adversos , Doença Crônica , Relação Dose-Resposta a Droga , Método Duplo-Cego , Esquema de Medicação , Feminino , Humanos , Imunoglobulina E/sangue , Imunoglobulina E/imunologia , Masculino , Pessoa de Meia-Idade , Omalizumab/efeitos adversos , Gravidade do Paciente , Indução de Remissão , Urticária/imunologia , Adulto Jovem
7.
Exp Appl Acarol ; 78(4): 555-564, 2019 Aug.
Artigo em Inglês | MEDLINE | ID: mdl-31367978

RESUMO

Blood-feeding ectoparasites constitute a growing burden for human and animal health, and animal production worldwide. In particular, mites (Acari: Gamasida) of the genera Dermanyssus (Dermanyssidae) and Ornithonyssus (Macronyssidae) infest birds and cause gamasoidosis in humans. The tropical fowl mite, Ornithonyssus bursa, is commonly found in tropical and subtropical countries but rarely reported in Europe. In this research we characterized the first two cases in Spain of clinical gamasoidosis diagnosed in patients infested with O. bursa, and investigated the IgE, IgM and IgG antibody response to mite proteins and the carbohydrate Galα1-3Galß1-(3)4GlcNAc-R (α-Gal) involved in the tick-bite associated alpha-Gal syndrome (AGS). The results suggested that O. bursa is establishing across Mediterranean countries, and may increase the risk for gamasoidosis. The immune antibody response to mite proteins was higher for IgM and similar for IgE and IgG antibodies between patients and non-allergic control individuals exposed to mite or tick bites. The anti-α-Gal antibody levels were similar between patients and controls, a result supported by the absence of this carbohydrate in mites. These results suggested that mite bites do not correlate with antibody response to acarine proteins or α-Gal, and are not associated with the AGS.


Assuntos
Proteínas de Artrópodes/imunologia , Infestações por Ácaros/diagnóstico , Infestações por Ácaros/imunologia , Ácaros/fisiologia , Oligossacarídeos/imunologia , Idoso , Animais , Feminino , Humanos , Imunoglobulina E/imunologia , Imunoglobulina G/imunologia , Imunoglobulina M/imunologia , Masculino , Infestações por Ácaros/parasitologia , Ácaros/classificação , Espanha
8.
Anticancer Res ; 39(8): 4511-4516, 2019 Aug.
Artigo em Inglês | MEDLINE | ID: mdl-31366553

RESUMO

BACKGROUND/AIM: Gluconacetobacter hansenii (G. hansenii) is an acetic acid bacterium of vinegar production. Its anti-allergic effect on mice upon oral administration was examined. MATERIALS AND METHODS: The amount of LPS was measured by the Limulus reaction. Mice were sensitized by peritoneal and intranasal administration of cedar pollen and alum followed by oral administration of 30 or 150 mg/kg of heated G. hansenii cells. Pollen was administered intranasally to evaluate nasal symptoms, and at 8 weeks, IgE and IL-10 levels in blood were measured by ELISA. RESULTS: The amount of LPS in dried bacterial cells was 10.4±3.3 mg/g. In the cedar pollinosis model of mice, a significant reduction was observed in nose scratching of both groups administered with the bacterial cells (30, 150 mg/kg). CONCLUSION: G. hansenii contains LPS, and its oral administration showed an anti-allergic effect by a significant mitigation of the symptoms in a pollen allergy mouse model.


Assuntos
Antialérgicos/administração & dosagem , Gluconacetobacter/imunologia , Pólen/efeitos adversos , Rinite Alérgica Sazonal/prevenção & controle , Ácido Acético/química , Administração Oral , Alérgenos/efeitos adversos , Animais , Antialérgicos/imunologia , Modelos Animais de Doenças , Humanos , Imunoglobulina E/imunologia , Camundongos , Rinite Alérgica Sazonal/microbiologia , Rinite Alérgica Sazonal/patologia
9.
Orv Hetil ; 160(33): 1311-1318, 2019 Aug.
Artigo em Húngaro | MEDLINE | ID: mdl-31401863

RESUMO

Introduction and aim: The aim of our research is to evaluate and compare commonly performed diagnostic tests, and to examine the psychological disorders induced by this food allergy. Children with symptoms suggesting cow's milk protein allergy were included in this study (n = 47). Blood and saliva samples were collected from the participants. Parents were asked to fill in a questionnaire constructed by the research team (containing the DSM-5 symptoms checklist about attention deficit hyperactivity disorder). Method: One of the most widely used diagnostic tool is the skin allergy test, which was performed in 47 subjects (n = 47, mean age: 7.36 years); only 2 children showed positive test result for cow's milk. Lymphocyte transformation test was observed to be positive in 8 children (17%), 4 subjects demonstrated questionable results. In our sub-study about psychological symptoms (n = 43, mean age: 7.88 years), the score was according to the attention deficit hyperactivity disorder symptom checklist before the diet (6.88, SD: 4.43) and showed significant decrease after 3 months of the elimination diet (4.48, SD: 3.69, p = 0.001). Scores of children with sleep disorder (10.62, SD: 4.23) also represented a significant reduction after 3 months of the diet (6.69, SD: 4.59, p = 0.009). Salivary cortisol levels did not show significant changes before and after elimination diet. Results: According to our data, skin allergy testing and lymphocyte transformation test are not reliable diagnostic tools for establishing the diagnosis. Conclusion: We conclude that a significant improvement in clinical symptoms can only be achieved with a strict elimination diet. Orv Hetil. 2019; 160(33): 1311-1318.


Assuntos
Alérgenos/imunologia , Imunoglobulina E/imunologia , Hipersensibilidade a Leite/diagnóstico , Hipersensibilidade a Leite/imunologia , Proteínas do Leite/efeitos adversos , Animais , Bovinos , Criança , Pré-Escolar , Feminino , Hipersensibilidade Alimentar , Humanos , Imunoglobulina E/sangue , Lactente , Recém-Nascido , Masculino , Proteínas do Leite/imunologia , Valor Preditivo dos Testes , Sensibilidade e Especificidade , Testes Cutâneos/métodos
10.
J Sci Food Agric ; 99(15): 6841-6849, 2019 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-31385312

RESUMO

BACKGROUND: This study aimed to investigate the reduction in the potential allergenicity of soymilk, and its rheological properties, after fermentation with Lactobacillus. Soymilk (SM) was fermented with Lactobacillus brevis and Lactobacillus sp. The molecular weight of fermented soymilk (FSM) was characterized using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), and the potential allergenicity of FSM was analyzed using enzyme-linked immunosorbent assay in vitro and the BALB/c mouse model to detect changes in histamine, mouse mast cell protease-1 (mMCP-1), allergen-specific IgG/IgE, and cytokine levels and histomorphology of jejunum in vivo. RESULTS: The SDS-PAGE and enzyme linked immunosorbent assay (ELISA) showed that allergens of soybean (ß-conglycinin and acidic subunit of glycinin) were almost degraded, and their immunoreactivity was decreased. In the BALB/c mouse model, the FSM group did not show anaphylactic shock symptoms compared with the SM group. Moreover, a tendency toward decreased serum allergen-specific IgG/IgE levels, plasma histamine levels, and mMCP-1 concentrations was observed in the FSM group. Furthermore, Th2-related cytokines were decreased, while IFN-γ production increased in spleen cell cultures. The intestinal villus was slightly damaged after the challenge. All these findings indicated that the Th1/Th2 balance in the FSM group shifted toward a Th1 response, ultimately reducing the potential allergenicity of FSM. Rheological assessment suggested that FSM has good viscous and pseudoplastic properties. CONCLUSION: Fermentation might be a promising method for producing tasty, hypoallergenic soybean products. © 2019 Society of Chemical Industry.


Assuntos
Alérgenos/metabolismo , Hipersensibilidade Alimentar/imunologia , Lactobacillus/metabolismo , Proteínas de Soja/imunologia , Soja/imunologia , Soja/microbiologia , Alérgenos/química , Alérgenos/imunologia , Animais , Biotransformação , Manipulação de Alimentos , Humanos , Imunoglobulina E/imunologia , Camundongos , Camundongos Endogâmicos BALB C , Reologia , Leite de Soja/química , Proteínas de Soja/metabolismo , Soja/química , Soja/metabolismo , Células Th1/imunologia , Células Th2/imunologia
11.
J Sci Food Agric ; 99(15): 7008-7015, 2019 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-31435932

RESUMO

BACKGROUND: Silkworm droppings have long been used in traditional medicine to remedy allergic itching, palsy, blood circulation problems, and arthritis in Asian countries. To investigate the anti-allergic effect of silkworm dropping extract (SDE) and its mechanism, we used a mouse model of food allergy induced by ovalbumin (OVA). RESULTS: SDE ameliorated the symptoms of OVA-induced food allergies, and the levels of T helper 2 (Th2)-related cytokines [such as interleukin (IL)-4, IL-5, IL-10, and IL-13] were found to be significantly decreased in both the spleen and mesenteric lymph nodes by SDE. Furthermore, SDE treatment directly inhibited OVA permeation, IL-4 production, and degranulation of mast cells; in contrast, immunoglobulin E (IgE) production from B cells was not affected. CONCLUSION: These results suggest that SDE has potential anti-allergic activities, and SDE may be useful in the treatment/prevention of allergic disorders such as food allergies, serving as therapeutic agents. © 2019 Society of Chemical Industry.


Assuntos
Antialérgicos/administração & dosagem , Bombyx/química , Fezes/química , Hipersensibilidade Alimentar/tratamento farmacológico , Células Th2/efeitos dos fármacos , Animais , Antialérgicos/química , Feminino , Hipersensibilidade Alimentar/genética , Hipersensibilidade Alimentar/imunologia , Humanos , Imunoglobulina E/imunologia , Interleucina-13/genética , Interleucina-13/imunologia , Interleucina-4/genética , Interleucina-4/imunologia , Interleucina-5/genética , Interleucina-5/imunologia , Mastócitos/imunologia , Camundongos , Camundongos Endogâmicos BALB C , Ovalbumina/efeitos adversos , Células Th2/imunologia
12.
Food Chem ; 300: 125143, 2019 Dec 01.
Artigo em Inglês | MEDLINE | ID: mdl-31326674

RESUMO

Tropomyosin (TM), a myofibrillar protein, is a major allergen in most crustaceans including king pawn (Litopenaeus vannamei). In this study, the structural modifications and allergenic response of TM in fresh king prawn as induced by cold argon plasma jet (CAPJ) were examined. The result showed that the level of α-helix structures declined as treatment time progressed, while the level of ß-sheets and random coils increased. The free sulfhydryl groups decreased as CAPJ treatment progressed due to the formation of disulphide bonds while surface hydrophobicity increased until equilibrium values. In addition, after 15 min of plasma exposure, the maximum reduction recorded for IgE and IgG binding capacities were 17.6% and 26.87% respectively as revealed by ELISA test. These findings correlated with the occurrence of protein unfolding and denaturation, evident by complementary structural analyses conducted. The study indicates that non-thermal plasma maybe a promising tool for developing hypoallergenic food products.


Assuntos
Alérgenos/química , Imunoglobulina E/imunologia , Penaeidae/imunologia , Gases em Plasma/química , Tropomiosina/química , Tropomiosina/imunologia , Animais , Argônio , Ensaio de Imunoadsorção Enzimática , Hipersensibilidade Alimentar , Humanos , Penaeidae/química
13.
Food Chem ; 299: 125025, 2019 Nov 30.
Artigo em Inglês | MEDLINE | ID: mdl-31295634

RESUMO

Peanut allergy is usually lifelong and accidental exposure impose formidable risk. The aim of this study was to assess the capacity of peanut proteins complexed to polyphenol extracts to reduce allergic response in C3H/HeJ mice. Mice were sensitized to peanut flour followed by exposure to amino acid diets fortified with peanut protein-polyphenol aggregates of either with low (15%; w/w) or high (40%; w/w) complexation ratios of blueberry (BB-Low and BB-High) and cranberry (CB-Low and CB-High) extracts. Treatment groups on diets with high complexation ratios of blueberry and cranberry aggregates showed significant reduction in peanut specific plasma Immunoglobulin E (IgE). Western blot analysis of spleen lysates showed CD63 protein expression was reduced in a dose-dependent manner in blueberry and cranberry complexed peanut protein supplemented diet groups. Our results demonstrate for the first time that complexation of polyphenols to peanut flour can potentially lower plasma IgE of peanut-sensitized C3H/HeJ mice.


Assuntos
Arachis/química , Arachis/imunologia , Imunoglobulina E/imunologia , Hipersensibilidade a Amendoim/prevenção & controle , Proteínas de Plantas/química , Proteínas de Plantas/imunologia , Polifenóis/química , Animais , Feminino , Camundongos , Camundongos Endogâmicos C3H , Especificidade da Espécie
14.
J Agric Food Chem ; 67(29): 8138-8148, 2019 Jul 24.
Artigo em Inglês | MEDLINE | ID: mdl-31294563

RESUMO

The aim of the present study was to compare various glycated ovalbumin (OVA)-monosaccharides, including OVA-mannose (Man), -glucose, -ribose, and -fructose, in the attenuation of OVA-induced allergic response in a BALB/C mouse model and the potential mechanisms of immunological modulation. The glycated OVA forms were prepared by Maillard reactions. OVA-Man significantly reduced the frequency of allergic signs. Mouse mast cell protease enzyme concentration was significantly reduced in the OVA-Man group (549.80 ± 84.67 ng/mL, p < 0.05). The OVA-Man group also had a lower histamine concentration (30.96 ± 1.12 ng/mL) as compared with the positive control OVA group (44.43 ± 0.71 ng/mL, p < 0.05). Both specific IgG and IgE were significantly reduced in the OVA-Man-treated group (p < 0.05). The OVA-Man group exhibited decreased concentrations of IL-4 (67.98 ± 3.11 pg/mL) and IL-17 (67.98 ± 3.11 pg/mL) and an increased concentration of IL-12 (336.70 ± 18.69 pg/mL, p < 0.05) compared with the positive control. Mannosylation played a vital role in allergen recognition, implicating deleterious downstream Th2 cell activation, cytokine secretion, and IgE production. This result indicates that different glycans target specific DC receptors, and differential DC processing, antigen presentation, and T cell response leads to altered variation in allergic response. OVA-Man exhibited minimal DC internalization, DC processing, MHC antigen presentation, and antigen-specific T cell activation, resulting in an attenuated allergic response and validating its efficacy as a potential immunotherapeutic candidate to treat egg allergy.


Assuntos
Hipersensibilidade a Ovo/imunologia , Monossacarídeos/química , Ovalbumina/química , Ovalbumina/imunologia , Animais , Citocinas/imunologia , Células Dendríticas/imunologia , Modelos Animais de Doenças , Hipersensibilidade a Ovo/etiologia , Feminino , Glicosilação , Humanos , Imunoglobulina E/imunologia , Reação de Maillard , Camundongos , Camundongos Endogâmicos BALB C , Ovalbumina/efeitos adversos , Linfócitos T/imunologia
15.
Parasitol Res ; 118(8): 2353-2359, 2019 Aug.
Artigo em Inglês | MEDLINE | ID: mdl-31263951

RESUMO

Simulium dermatitis is an IgE-mediated skin reaction in animals and humans caused by the bites of black flies. Although Simulium nigrogilvum has been incriminated as the main human-biting black fly species in Thailand, information on its salivary allergens is lacking. Salivary gland extract of S. nigrogilvum females was subjected to sodium dodecylsulfate-polyacrylamide gel electrophoresis, and the separated components were applied onto nitrocellulose membranes for immunoblotting, which was performed by probing the protein blots with sera from 17 individuals who were allergic to the bites of S. nigrogilvum. IgE-reactive protein bands were characterized further by liquid chromatography-mass spectrometry (LC-MS/MS) analysis. Nine protein bands (79, 42, 32, 25, 24, 22, 15, 13, and 11 kDa) were recognized in the serum of the subjects. Four of the nine protein bands (32, 24, 15, and 11 kDa) showed IgE reactivity in all (100%) of the tested sera, and they were identified as salivary secreted antigen 5-related protein, salivary serine protease, erythema protein, and hypothetical secreted protein, respectively. Three other proteins, salivary serine protease (25 kDa), salivary D7 secreted protein (22 kDa), and hypothetical protein (13 kDa), reacted with > 50% of the sera. The relevance of the identified protein bands as allergens needs to be confirmed by using pure recombinant proteins, either in the in vivo skin prick test or in vitro detection of the specific IgE in the serum samples of allergic subjects. This will be useful for the rational design of component-resolved diagnosis and allergen immunotherapy for the allergy mediated by the bites of black flies.


Assuntos
Mordeduras e Picadas/imunologia , Galectina 3/imunologia , Proteínas de Insetos/química , Glândulas Salivares/química , Simuliidae/fisiologia , Alérgenos/química , Alérgenos/imunologia , Animais , Mordeduras e Picadas/parasitologia , Cromatografia Líquida , Eletroforese em Gel de Poliacrilamida , Feminino , Galectina 3/química , Humanos , Imunoglobulina E/imunologia , Proteínas de Insetos/imunologia , Glândulas Salivares/imunologia , Simuliidae/química , Simuliidae/imunologia , Espectrometria de Massas em Tandem , Tailândia
16.
Vet Immunol Immunopathol ; 212: 38-42, 2019 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-31213250

RESUMO

Food allergen-specific sublingual immunotherapy (FA-SLIT) is a novel, safe and effective approach in dogs with adverse food reactions (AFR) to reduce their clinical symptoms. However, little is known about the specific immune components which mediate this reduction in clinical symptoms. In humans, regulatory T cells seem to play an important role in this desensitisation process. Here, we investigated changes in peripheral T cell responses of dogs with AFR upon FA-SLIT. Five dogs received a dose escalation of FA-SLIT over a six-month period. An oral food challenge was performed at the beginning and end of the study to assess the efficacy of the FA-SLIT. Using in vitro allergen-recall assays, we assessed the proliferation of T cell subsets before and at the end of the treatment. FA-SLIT significantly increased the percentage of proliferating CD4-CD8- double-negative (DN) T cells, while the percentage of allergen-specific CD4-CD8+ and CD4+CD8+ double-positive (DP) T cells decreased upon treatment. These findings indicate that sublingual immunotherapy in dogs activates DN T cells, which might be important for the desensitisation of dogs with adverse food reactions. However, further research is needed to corroborate these findings and to further elucidate the mechanism of action of FA-SLIT in dogs with AFR.


Assuntos
Hipersensibilidade Alimentar/imunologia , Hipersensibilidade Alimentar/terapia , Imunoterapia Sublingual , Linfócitos T Reguladores/imunologia , Animais , Linfócitos T CD4-Positivos/imunologia , Dessensibilização Imunológica/métodos , Cães , Imunoglobulina E/sangue , Imunoglobulina E/imunologia , Interleucina-10/imunologia , Ativação Linfocitária
17.
Immunol Med ; 42(1): 10-15, 2019 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-31204894

RESUMO

Atopic dermatitis (AD) is caused by complex interactions between a variety of genetic and environmental factors that contribute to the maintenance of the chronic inflammatory skin condition. Most conventional treatments have been designed for the so-called 'average patient'. In recent years however, many previously unknown details pertaining to the mechanisms of the pathogenesis of AD have been elucidated, and novel treatments based on these pathological mechanisms or on subgroup classifications have been developed. Herein, how future treatment strategies for AD can be developed is described.


Assuntos
Dermatite Atópica/tratamento farmacológico , Dermatite Atópica/etiologia , Terapia de Alvo Molecular/tendências , Animais , Anticorpos , Anticorpos Monoclonais/uso terapêutico , Dermatite Atópica/genética , Dermatite Atópica/imunologia , Humanos , Imunoglobulina E/imunologia , Subunidade alfa de Receptor de Interleucina-4/imunologia , Proteínas de Filamentos Intermediários/genética , Camundongos , Mutação , Ácidos Nucleicos/uso terapêutico , Oligodesoxirribonucleotídeos/uso terapêutico , Fator de Transcrição STAT6 , beta-Defensinas
18.
Mol Immunol ; 112: 330-337, 2019 08.
Artigo em Inglês | MEDLINE | ID: mdl-31247376

RESUMO

Shrimp is one of the predominant causes of food allergy among adults, often presenting with severe reactions. Current in vitro diagnostics are based on quantification of patient specific-IgE (sIgE) to shrimp extract. Tropomyosin is the known major shrimp allergen, but IgE sensitisation to other allergens is poorly characterised. In this study, the binding of IgE to various shrimp allergens, additional to tropomyosin, was investigated using sera from 21 subjects who had clinical reactions to one or more shellfish species. Total shrimp-sIgE was quantified using ImmunoCAP, while allergen-sIgEs were quantified using immunoblotting and mass spectrometry, and immuno-PCR to recombinant shrimp tropomyosin. Sixty-two percent of subjects (13/21) were positive to shrimp by ImmunoCAP. IgE from 43% of subjects (9/21) bound tropomyosin, while an additional 29% of subjects (6/21) demonstrated IgE-binding solely to other shrimp allergens, including sarcoplasmic calcium-binding protein, arginine kinase and hemocyanin. Furthermore, IgE sensitisation to other shrimp allergens was demonstrated in 50% of subjects (4/8) who were ImmunoCAP negative. The lack of standardised shrimp allergens and inadequacy of current extracts for shrimp allergy diagnosis is highlighted by this study. Comprehensive knowledge of less studied allergens and their inclusion in component-resolved diagnostics will improve diagnostic accuracy, benefitting the wider population suffering from shellfish allergy.


Assuntos
Alérgenos/imunologia , Artemia/imunologia , Hipersensibilidade Alimentar/diagnóstico , Hipersensibilidade Alimentar/imunologia , Adulto , Animais , Arginina Quinase/imunologia , Proteínas de Ligação ao Cálcio/imunologia , Feminino , Hemocianinas/imunologia , Humanos , Imunoglobulina E/imunologia , Masculino , Pessoa de Meia-Idade , Alimentos Marinhos , Tropomiosina/imunologia , Adulto Jovem
19.
Mol Immunol ; 112: 347-357, 2019 08.
Artigo em Inglês | MEDLINE | ID: mdl-31254775

RESUMO

Peach and apricot can cause allergic reactions with symptoms ranging from mild to very severe, including anaphylaxis. Sometimes subjects allergic to fruits of the Prunus genus have been reported to be also allergic to rubber latex products. The objective of this study is the characterization of a newly identified peach and apricot protein showing similarities with the allergens Hev b 5 from rubber latex and Man e 5 from manioc. This protein has been named ENEA on the basis of the single letter amino acid code of the first four N-terminal residues of the isolated molecule. It has been found in very variable amounts in different peach cultivars and batches. ENEA was isolated from peach pulp extracts by chromatographic separations and identified by direct protein sequencing. At that time, the full length sequence was available only for the homologous protein of the taxonomically closely related apricot, which was produced as a recombinant molecule in Escherichia coli. The following availability of the full length sequence of peach ENEA revealed a very high identity (97%) with the apricot homolog. Similarly to Hev b 5 and to Man e 5, the structural characterization indicated that ENEA is an intrinsically disordered protein. The immunological properties, investigated by dot blotting, the ABA system and the FABER test, showed that ENEA is recognized by specific IgE of allergic patients. In a selected population of 31 patients reporting allergic reactions to peach fruit and/or IgE positive to Hev b 5, 28 and 27 subjects resulted co-sensitized to rENEA and Hev b 5 in the ABA and ISAC test, respectively. In a random population of 3305 suspected allergic patients, analyzed with the FABER test, 17 of them were sensitized to rENEA and 10 of them were also positive to Hev b 5. In addition, both the natural molecule from peach and the recombinant protein of apricot partially inhibited the IgE binding to Hev b 5. In conclusion, a new peach and apricot IgE-binding protein, cross-reacting with the major latex allergen Hev b 5, has been identified. Its variable concentration in the fruit might explain some occasionally occurring allergic reactions. The apricot molecule has recently been registered by the WHO/IUIS Allergen Nomenclature Sub-Committee with the allergen name Pru ar 5. The recombinant form of apricot ENEA, now available, will contribute to allergy diagnosis.


Assuntos
Antígenos de Plantas/imunologia , Reações Cruzadas/imunologia , Hipersensibilidade ao Látex/imunologia , Látex/imunologia , Proteínas de Plantas/imunologia , Prunus armeniaca/imunologia , Prunus persica/imunologia , Adulto , Idoso , Alérgenos/imunologia , Criança , Feminino , Galectina 3/imunologia , Humanos , Imunoglobulina E/imunologia , Masculino , Pessoa de Meia-Idade , Prunus/imunologia , Proteínas Recombinantes/imunologia , Adulto Jovem
20.
Molecules ; 24(11)2019 May 31.
Artigo em Inglês | MEDLINE | ID: mdl-31159327

RESUMO

Food allergies originate from adverse immune reactions to some food components. Ingestion of food allergens can cause effects of varying severity, from mild itching to severe anaphylaxis reactions. Currently there are no clues to predict the allergenic potency of a molecule, nor are cures for food allergies available. Cutting-edge research on allergens is aimed at increasing information on their diffusion and understanding structure-allergenicity relationships. In this context, purified recombinant allergens are valuable tools for advances in the diagnostic and immunotherapeutic fields. Chitinases are a group of allergens often found in plant fruits, but also identified in edible insects. They are classified into different families and classes for which structural analyses and identification of epitopes have been only partially carried out. Moreover, also their presence in common allergen databases is not complete. In this review we provide a summary of the identified food allergenic chitinases, their main structural characteristics, and a clear division in the different classes.


Assuntos
Alérgenos/imunologia , Quitinases/imunologia , Hipersensibilidade Alimentar/imunologia , Alérgenos/química , Alérgenos/classificação , Animais , Quitinases/química , Reações Cruzadas/imunologia , Mapeamento de Epitopos/métodos , Epitopos/imunologia , Humanos , Imunoglobulina E/imunologia , Insetos/química , Insetos/enzimologia , Insetos/imunologia , Proteínas de Plantas/química , Proteínas de Plantas/imunologia , Relação Estrutura-Atividade
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