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1.
Scand J Immunol ; 91(1): e12824, 2020 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-31486118

RESUMO

The prevalence of food allergy (FA) has increased too rapidly, possibly due to environmental factors. The guidelines recommend strict allergen avoidance, but FA is still the main cause of anaphylaxis in all age groups. Immunotherapy is the only treatment able to change the course of allergic disease, and oral immunotherapy (OIT) is the more effective route in FA. However, it carries the risk of adverse reactions, including anaphylaxis. To improve OIT safety, adjuvant therapy with the immunoglobulin E (IgE) monoclonal antibody omalizumab has been extensively used. Results suggest particular benefit in patients with high risk of fatal anaphylaxis. An alternative approach is to use omalizumab instead of OIT to prevent severe allergic reactions upon accidental exposure. This paper reviews current evidence regarding IgE-mediated FA, focusing on natural tolerance and food sensitization acquisition, and on avoidance measures and their limitations.


Assuntos
Alérgenos/imunologia , Dessensibilização Imunológica , Hipersensibilidade Alimentar/imunologia , Hipersensibilidade Alimentar/terapia , Alimentos/efeitos adversos , Animais , Dessensibilização Imunológica/efeitos adversos , Dessensibilização Imunológica/métodos , Hipersensibilidade Alimentar/epidemiologia , Hipersensibilidade Alimentar/prevenção & controle , Humanos , Tolerância Imunológica , Imunização , Imunoglobulina E/imunologia
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.
Food Chem ; 302: 125348, 2020 Jan 01.
Artigo em Inglês | MEDLINE | ID: mdl-31442704

RESUMO

Tropomyosin (TM) is the main allergen of shrimp. Glycation reportedly reduced the allergenicity of TM, and the allergenicity reduction was heavily dependent upon the sources of saccharides. In this work we investigated, how glycation of tropomyosin by functional oligosaccharides affected the allergenicity. Compared to TM, the TM glycated by galacto-oligosaccharide (TM-GOS), mannan-oligosaccharide (TM-MOS) and maltopentaose (TM-MPS) had lower allergenicity and induced weaker mouse allergy responses. While the TM glycated by fructo-oligosaccharide (TM-FOS) had stronger allergenicity and induced severe mouse allergy symptoms, due to the generation of neoallergns that belonged to advanced glycation end products (e.g. CML). Therefore, GOS, MOS and MPS could be applied to desensitize shrimp TM-induced food allergy through glycation, while FOS was not suitable to reduce TM allergenicity. Glycation of TM by GOS, MOS and MPS, especially for MPS, significantly reduced allergenicity and alleviated allergy symptoms, which could be potentially explored for immunotherapy for shrimp-allergic patients.


Assuntos
Hipersensibilidade Alimentar/imunologia , Produtos Finais de Glicação Avançada/metabolismo , Palaemonidae/imunologia , Proteínas de Frutos do Mar/metabolismo , Tropomiosina/metabolismo , Adulto , Alérgenos/imunologia , Alérgenos/metabolismo , Animais , Pré-Escolar , Feminino , Hipersensibilidade Alimentar/sangue , Glicosilação , Humanos , Masculino , Camundongos Endogâmicos BALB C , Pessoa de Meia-Idade , Oligossacarídeos/imunologia , Oligossacarídeos/metabolismo , Proteínas de Frutos do Mar/química , Proteínas de Frutos do Mar/imunologia , Tropomiosina/química , Tropomiosina/imunologia
5.
Arerugi ; 68(9): 1141-1147, 2019.
Artigo em Japonês | MEDLINE | ID: mdl-31723111

RESUMO

We present a case of early childhood-onset pork-cat syndrome possibly due to sensitization by both cats and dogs. A 6-year-old girl was referred to our hospital because of repetitive episodes of urticaria when she consumed pork meat. The patient lived with a dog and the ground floor of her house was a veterinary clinic run by her veterinarian parents. Blood tests demonstrated high specific IgE (≥50UA/ml) against cat dander, dog dander, pork, Sus s 1, Fel d 2, Can f 1, Can f 2, and Can f 3. The skin prick test was positive for raw pork and beef. Western blotting analysis detected hot spots on 67-kDa proteins in pork meat and cat dander extract. Cross-reactivity between these two proteins was confirmed by an inhibition test. Furthermore, crossreactivity between pork meat and dog dander extract was also noted. Taken together, the diagnosis of porkcat syndrome was made, and both cats and dogs were suggested to have led to the sensitization. The patient was advised to only eat well-cooked pork, and has been followed thereafter without additional reactions. The previously reported cases of this syndrome developed during adolescence and young adulthood because a considerable period from the sensitization to the development cross-reactivity with pork meat is required. To our best knowledge, this is the youngest reported case of pork-cat syndrome among English and Japanese literatures. The nomenclature of this syndrome as pet animal-meat syndrome improves the understanding of the underlying pathogenesis of cross-reactivity between animal albumins and meat albumins.


Assuntos
Hipersensibilidade Alimentar/imunologia , Carne Vermelha , Alérgenos , Animais , Gatos , Bovinos , Criança , Reações Cruzadas , Cães , Feminino , Humanos , Imunoglobulina E/sangue , Testes Cutâneos , Suínos , Adulto Jovem
6.
Int J Nanomedicine ; 14: 7053-7064, 2019.
Artigo em Inglês | MEDLINE | ID: mdl-31564865

RESUMO

Background: Food allergy (FA) is a significant public health problem. The therapeutic efficacy for FA is unsatisfactory currently. The breakdown of intestinal immune tolerance is associated with the pathogenesis of FA. Therefore, it is of great significance to develop novel therapeutic methods to restore immune tolerance in treating FA. Methods: We proposed an oral administration strategy to treat FA by co-delivering food allergen epitope fragment (peptide: IK) and adjuvant R848 (TLR7 ligand) in the mPEG-PDLLA nanoparticles (PPLA-IK/R848 NPs). The generation of tolerogenic dendritic cells (DCs) and regulatory T cells (Tregs) induced by PPLA-IK/R848 NPs were evaluated in vitro and in vivo. The therapeutic effects of PPLA-IK/R848 NPs were also assessed in an OVA-induced FA model. Results: PPLA-IK/R848 NPs could efficiently deliver IK to DCs to drive DCs into the tolerogenic phenotypes and promote the differentiation of Tregs in vitro and in vivo, significantly inhibited FA responses through the recovery of intestinal immune tolerance. Conclusion: Oral administration of PPLA-IK/R848 NPs could efficiently deliver IK and R848 to intestinal DCs and stimulate DCs into allergen tolerogenic phenotype. These tolerogenic DCs could promote the differentiation of Tregs, which significantly protected mice from food allergic responses. This study provided an efficient formulation to alleviate FA through the recovery of immune tolerance.


Assuntos
Alérgenos/imunologia , Células Dendríticas/imunologia , Sistemas de Liberação de Medicamentos , Epitopos/imunologia , Hipersensibilidade Alimentar/tratamento farmacológico , Hipersensibilidade Alimentar/imunologia , Imidazóis/administração & dosagem , Imidazóis/uso terapêutico , Tolerância Imunológica , Linfócitos T Reguladores/imunologia , Sequência de Aminoácidos , Animais , Diferenciação Celular , Células Dendríticas/efeitos dos fármacos , Imidazóis/química , Imidazóis/farmacologia , Tolerância Imunológica/efeitos dos fármacos , Camundongos Endogâmicos BALB C , Peptídeos/química , Poliésteres/química , Polietilenoglicóis/química , Linfócitos T Reguladores/efeitos dos fármacos
7.
Int Arch Allergy Immunol ; 180(3): 212-220, 2019.
Artigo em Inglês | MEDLINE | ID: mdl-31533105

RESUMO

BACKGROUND: Although plant and fruit pollens are entomophilous and relevant in exposed workers, we have shown a high frequency of sensitisation and symptoms induction of peach tree pollen (PTP) and Prunus persica 9 (Pru p 9) in adults from areas of peach cultivars. METHODS: We studied the sensitisation and clinical relevance of PTP and Pru p 9 in a large group of children and adolescents aged 3-19 years. A detailed questionnaire plus skin prick testing to prevalent allergens, PTP, and Pru p 9 were carried out. The clinical relevance was established by nasal provocation test (NPT) and symptom score index. RESULTS: We evaluated 685 children (mean age 8.75 ± 3.3 years, median 9 years), 52% of them female. Sensitisation to PTP occurred in 20% of the cases following olive tree (33%) and Phleum pratense (26%). In a randomly selected subgroup of subjects sensitised to PTP, 30% were skin prick test-positive to Pru p 9. Most cases had rhinitis or rhinoconjunctivitis. NPT showed the relevance of PTP and Pru p 9 in the induction of symptoms. CONCLUSION: PTP and Pru p 9 are relevant in the induction of sensitisation and respiratory symptoms in children and adolescents. This allergen should be evaluated in children living in regions of peach tree cultivars.


Assuntos
Alérgenos/imunologia , Antígenos de Plantas/imunologia , Hipersensibilidade Alimentar/epidemiologia , Hipersensibilidade Alimentar/imunologia , Pólen/imunologia , Prunus persica/imunologia , Rinite Alérgica Sazonal/imunologia , Adolescente , Criança , Feminino , Humanos , Imunização , Masculino , Olea/imunologia , Phleum/imunologia , Espanha/epidemiologia
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.
Pediatr Clin North Am ; 66(5): 941-954, 2019 10.
Artigo em Inglês | MEDLINE | ID: mdl-31466683

RESUMO

Food allergy is an immune-mediated disease and must be differentiated from other adverse effects related to food that are non-immune mediated. Symptoms of immunoglobulin (Ig) E-mediated allergy can range from mild to severe, and life-threatening anaphylaxis may occur. Current recommended strategies for diagnosis include the use of skin prick tests, allergen-specific serum IgE, and/or oral food challenges. Management entails allergen avoidance and appropriate treatment of allergic reactions should accidental ingestions occur. Treatment approaches under investigation include immunotherapy as well as biologics and novel vaccines. Attention has also recently focused on implementing strategies for prevention of food allergy.


Assuntos
Dessensibilização Imunológica/métodos , Hipersensibilidade Alimentar/diagnóstico , Hipersensibilidade Alimentar/terapia , Administração Oral , Alérgenos/imunologia , Hipersensibilidade Alimentar/imunologia , Hipersensibilidade Alimentar/fisiopatologia , Humanos , Imunoglobulina E/imunologia , Testes Cutâneos
12.
Pediatr Clin North Am ; 66(5): 955-965, 2019 10.
Artigo em Inglês | MEDLINE | ID: mdl-31466684

RESUMO

Eosinophilic esophagitis is a recently defined condition that has dramatically increased in prevalence in the last several decades. It may occur at any age, but the clinical presentation in young children is often more vague than the classic solid food dysphagia and food impacting that are the major presenting symptoms of eosinophilic esophagitis in adults and adolescents. Successful therapies exist, including medications and dietary modifications, but disease typically recurs when the intervention is discontinued.


Assuntos
Esofagite Eosinofílica/diagnóstico , Esofagite Eosinofílica/imunologia , Esofagite Eosinofílica/terapia , Administração Tópica , Produtos Biológicos/uso terapêutico , Criança , Transtornos de Deglutição/diagnóstico , Diagnóstico Diferencial , Esofagoscopia , Hipersensibilidade Alimentar/dietoterapia , Hipersensibilidade Alimentar/imunologia , Humanos , Esteroides/uso terapêutico
13.
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
14.
Mol Immunol ; 114: 369-377, 2019 10.
Artigo em Inglês | MEDLINE | ID: mdl-31450182

RESUMO

The prevalence of IgE-mediated food allergy is increasing in the whole wide world which often causes skin and gastrointestinal tract symptoms, or even fatal anaphylactic shock. However, the evaluation of food allergens remains difficult, and the mechanism of food allergy is still not fully clear. To study the gene expression profile in food allergy animal models and identify the regulatory mechanism of the crucial genes, two administration routes were used to build animal models in our study. OVA-specific IgE and IL-4 levels were tested by ELISA, transcriptome profiling was carried out by microarray, and the regulatory mechanism of the highest expressed gene was studied in the primary spleen cells. We found that activation-induced cytidine deaminase (Aicda) is the highest expressed gene in the allergic mice, IL-21 can dramatically enhance the expression of Aicda in the lymph node microenvironment, and IL-17A can promote this effect significantly though it has only limited influence by itself. At last, we illuminated that the promotion of IL-21 on Aicda is partially through STAT3. In summary, our results suggest that IL-21 and IL-17A may play important role in the expression of Aicda as well as food allergy.


Assuntos
Citidina Desaminase/imunologia , Hipersensibilidade Alimentar/imunologia , Interleucinas/imunologia , Ovalbumina/imunologia , Alérgenos/imunologia , Anafilaxia/imunologia , Animais , Citocinas/imunologia , Modelos Animais de Doenças , Feminino , Imunoglobulina E/imunologia , Masculino , Camundongos , Camundongos Endogâmicos BALB C , Camundongos Endogâmicos C3H , Baço/imunologia
15.
Food Chem ; 299: 125166, 2019 Nov 30.
Artigo em Inglês | MEDLINE | ID: mdl-31323443

RESUMO

Dynamic high-pressure microfluidization (DHPM) pretreatment and glycation with lactose were employed to modify α-Lactalbumin (α-LA) with respect to the IgE/IgG binding capacities. No significant difference on incorporation ratio value of glycated α-LA was observed with and without DHPM pretreatment. However, IgE/IgG binding capacities of α-LA were decreased after glycation and DHPM pretreatment promoted the reduction. The lowest IgE/IgG binding capacities of glycated α-LA were obtained by DHPM pretreatment at 110 MPa. Native α-LA was mainly glycated at K62, K94, K98, whereas glycation sites and degree of substitution per peptide (DSP) were added after DHPM treatment. Therefore, the reduced IgE/IgG binding capacities of α-LA was attributed to the characteristics of glycated sites, including the amount, location, and DSP values. Interestingly, K98 played the most important role in decreasing IgE/IgG binding capacities of α-LA. The study revealed that glycation combined with DHPM was a promising way to decrease the allergenicity of proteins.


Assuntos
Hipersensibilidade Alimentar/imunologia , Imunoglobulina E/metabolismo , Imunoglobulina G/metabolismo , Lactalbumina/metabolismo , Alérgenos/química , Animais , Bovinos , Ensaio de Imunoadsorção Enzimática , Indústria de Processamento de Alimentos/métodos , Humanos , Lactalbumina/química , Lactalbumina/imunologia , Lactose/química , Lisina/metabolismo , Espectrometria de Massas/métodos , Pressão , Coelhos
16.
Food Chem ; 300: 125209, 2019 Dec 01.
Artigo em Inglês | MEDLINE | ID: mdl-31344629

RESUMO

Turbot can induce allergy in susceptible individuals due to the presence of parvalbumin (PV), a major fish allergen. This study aimed at evaluating the digestibility and the ability of PV to elicit the release of cellular degranulation, following treatment with tyrosinase (PV-Tyr), caffeic acid (PV-CA) and in combination (PV-Tyr/CA), using in vitro digestion and RBL-2H3 (passive rat basophil leukemia) cell line. The digestion assay products revealed that the stability of PV in simulated gastric fluid (SGF) was stronger, while in simulated intestinal fluid (SIF) was rather weak. Western blot analysis revealed that the IgG-binding abilities of the cross-linked PV were markedly reduced. Moreover, crosslinking hampered the release of cellular degranulation process in RBL-2H3 cell lines. PV-Tyr/CA showed highly significant reduction in the release rate of ß-hexosaminidase (66.02%), histamine (35.01%), tryptase (29.25%), cysteinyl leukotrienes (29.72%), prostaglandin D2 (34.96%), IL-4 (43.99%) and IL-13 (38.93%) and shown potential in developing hypoallergenic fish products.


Assuntos
Ácidos Cafeicos/química , Citocinas/metabolismo , Hipersensibilidade Alimentar/imunologia , Monofenol Mono-Oxigenase/química , Parvalbuminas/química , Alérgenos/química , Alérgenos/farmacocinética , Animais , Degranulação Celular/efeitos dos fármacos , Linhagem Celular , Digestão , Proteínas de Peixes da Dieta/química , Linguados , Suco Gástrico , Histamina/metabolismo , Humanos , Parvalbuminas/imunologia , Parvalbuminas/farmacologia , Ratos , beta-N-Acetil-Hexosaminidases/metabolismo
17.
Nutrients ; 11(8)2019 07 25.
Artigo em Inglês | MEDLINE | ID: mdl-31349704

RESUMO

Epidemiological studies identified raw cow's milk consumption as an important environmental exposure that prevents allergic diseases. In the present study, we investigated whether raw cow's milk has the capacity to induce tolerance to an unrelated, non-milk, food allergen. Histone acetylation of T cell genes was investigated to assess potential epigenetic regulation. Female C3H/HeOuJ mice were sensitized and challenged to ovalbumin. Prior to sensitization, the mice were treated with raw milk, processed milk, or phosphate-buffered saline for eight days. Allergic symptoms were assessed after challenge and histone modifications in T cell-related genes of splenocyte-derived CD4+ T cells and the mesenteric lymph nodes were analyzed after milk exposure and after challenge. Unlike processed milk, raw milk decreased allergic symptoms. After raw milk exposure, histone acetylation of Th1-, Th2-, and regulatory T cell-related genes of splenocyte-derived CD4+ T cells was higher than after processed milk exposure. After allergy induction, this general immune stimulation was resolved and histone acetylation of Th2 genes was lower when compared to processed milk. Raw milk reduces allergic symptoms to an unrelated, non-milk, food allergen in a murine model for food allergy. The activation of T cell-related genes could be responsible for the observed tolerance induction, which suggested that epigenetic modifications contribute to the allergy-protective effect of raw milk.


Assuntos
Montagem e Desmontagem da Cromatina , Epigênese Genética , Hipersensibilidade Alimentar/dietoterapia , Histonas/metabolismo , Tolerância Imunológica , Ativação Linfocitária , Leite/imunologia , Subpopulações de Linfócitos T/metabolismo , Acetilação , Animais , Células Cultivadas , Citocinas/imunologia , Citocinas/metabolismo , Modelos Animais de Doenças , Feminino , Hipersensibilidade Alimentar/genética , Hipersensibilidade Alimentar/imunologia , Hipersensibilidade Alimentar/metabolismo , Camundongos Endogâmicos C3H , Ovalbumina , Subpopulações de Linfócitos T/imunologia , Linfócitos T Reguladores/imunologia , Linfócitos T Reguladores/metabolismo , Células Th1/imunologia , Células Th1/metabolismo , Células Th2/imunologia , Células Th2/metabolismo
18.
Food Chem ; 298: 125087, 2019 Nov 15.
Artigo em Inglês | MEDLINE | ID: mdl-31272052

RESUMO

In this study, comprehensive analysis was performed to evaluate the impact of high hydrostatic pressure (HHP) and traditional thermal processing methods (baking and steaming) on cod proteins. Results showed that HHP, but not baking or steaming, was able to increase the content of soluble protein nitrogen (1.42-fold), compared with control. Total peptide contents of HHP-treated samples were also significantly higher than baked and steamed ones. In addition, protein oxidation was greatly increased after baking (1.56-fold) and steaming (1.97-fold), whereas HHP did not exhibit any appreciable effect. Furthermore, the allergenicity of cod was significantly reduced after HHP as reflected by the attenuated IgE and IgG-binding capacities (67-84% relative to control), while baking and steaming resulted in higher allergenicity. This study strongly supports the potential of HHP for reducing allergenicity, avoiding protein oxidation, and improving digestibility of cod and other protein-rich foods susceptible to quality deterioration during thermal processing.


Assuntos
Proteínas de Peixes da Dieta/química , Hipersensibilidade Alimentar/prevenção & controle , Indústria de Processamento de Alimentos/métodos , Gadus morhua , Animais , Culinária , Digestão , Produtos Pesqueiros/análise , Proteínas de Peixes da Dieta/farmacocinética , Hipersensibilidade Alimentar/imunologia , Humanos , Interações Hidrofóbicas e Hidrofílicas , Pressão Hidrostática , Imunoglobulina G/metabolismo , Nitrogênio/análise , Oxirredução , Carbonilação Proteica , Vapor , Compostos de Sulfidrila/análise , Compostos de Sulfidrila/química
19.
J Agric Food Chem ; 67(31): 8626-8631, 2019 Aug 07.
Artigo em Inglês | MEDLINE | ID: mdl-31287307

RESUMO

An almond allergen with two known short peptide sequences was reported as the almond 2S albumin but was later suspected to be almond vicilin. However, this allergen was not designated by the World Health Organization/International Union of Immunological Societies. This study aimed to determine the true identity of this elusive almond allergen. cDNAs were synthesized from total RNA of the Nonpareil almond. The complete sequence of the previously reported almond allergen was determined from its coding sequence. The deduced protein was produced recombinantly and was confirmed to be a food allergen by testing with 18 almond-allergic sera. The allergen is a potential cysteine-rich antimicrobial protein with characteristic C[X]3C-[X]10-12-C[X]3C motifs of the hairpinin antimicrobial protein. This first member of a novel family of food allergens was named Pru du 8. The signature motif of the hairpinin antimicrobial protein can be found in the N-terminal region of some vicilin allergens (e.g., Ara h 1). It can also be found in the signal peptide of other vicilin allergens (e.g., Car i 2). In many species, however, vicilins do not contain such a motif, indicating that the presence of the signature motifs of the hairpinin antimicrobial protein in vicilins might be a result of translocation during evolution.


Assuntos
Alérgenos/imunologia , Antígenos de Plantas/imunologia , Prunus dulcis/imunologia , Alérgenos/química , Alérgenos/genética , Motivos de Aminoácidos , Sequência de Aminoácidos , Antígenos de Plantas/química , Antígenos de Plantas/genética , DNA Complementar/genética , Hipersensibilidade Alimentar/imunologia , Humanos , Prunus dulcis/química , Prunus dulcis/genética , Proteínas de Armazenamento de Sementes/química , Proteínas de Armazenamento de Sementes/genética , Proteínas de Armazenamento de Sementes/imunologia , Alinhamento de Sequência , Análise de Sequência de DNA
20.
Nutrients ; 11(7)2019 Jun 30.
Artigo em Inglês | MEDLINE | ID: mdl-31262028

RESUMO

Raw cow's milk was previously shown to suppress allergic symptoms in a murine model for food allergy. In the present study, we investigated the contribution of fat content and heat-sensitive milk components to this allergy-protective effect. In addition, we determined the potency of alkaline phosphatase (ALP), a heat-sensitive raw milk component, to affect the allergic response. C3H/HeOuJ mice were treated with raw milk, pasteurized milk, skimmed raw milk, pasteurized milk spiked with ALP, or phosphate-buffered saline for eight days prior to sensitization and challenge with ovalbumin (OVA). Effects of these milk types on the allergic response were subsequently assessed. Similar to raw milk, skimmed raw milk suppressed food allergic symptoms, demonstrated by a reduced acute allergic skin response and low levels of OVA-specific IgE and Th2-related cytokines. This protective effect was accompanied by an induction of CD103+CD11b+ dendritic cells and TGF-ß-producing regulatory T cells in the mesenteric lymph nodes. Pasteurized milk was not protective but adding ALP restored the allergy-protective effect. Not the fat content, but the heat-sensitive components are responsible for the allergy-protective effects of raw cow's milk. Adding ALP to heat-treated milk might be an interesting alternative to raw cow's milk consumption, as spiking pasteurized milk with ALP restored the protective effects.


Assuntos
Fosfatase Alcalina/imunologia , Dermatite Atópica/prevenção & controle , Manipulação de Alimentos/métodos , Hipersensibilidade Alimentar/prevenção & controle , Proteínas do Leite/imunologia , Pasteurização , Animais , Basófilos/imunologia , Basófilos/metabolismo , Células Cultivadas , Citocinas/metabolismo , Dermatite Atópica/imunologia , Dermatite Atópica/metabolismo , Modelos Animais de Doenças , Feminino , Hipersensibilidade Alimentar/imunologia , Hipersensibilidade Alimentar/metabolismo , Imunoglobulinas/sangue , Lipídeos/imunologia , Linfonodos/imunologia , Linfonodos/metabolismo , Camundongos Endogâmicos C3H , Ovalbumina , Desnaturação Proteica , Pele/imunologia , Pele/metabolismo , Baço/imunologia , Baço/metabolismo
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