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Petrolatum, also known as petroleum jelly, is a widely used topical agent, with a variety of uses in dermatology. Despite its popularity, many myths surround this ubiquitous dermatologic staple. This review details the history of petrolatum and how it is manufactured as well as how its biologic properties make it a great moisturizer. Additionally, data on its potential for flammability, allergenicity, and comedogenicity are detailed, dispelling misconceptions about petrolatum use around oxygen and as a cause of acne. The uses and benefits of petrolatum in dermatology are wide-ranging—a patch test instrument, a vehicle for medicated ointments, and a wound care essential. Given its ubiquitous presence, it is important for dermatologists to understand the history, safety profile, and myths surrounding this humble skincare staple. [ABSTRACT FROM AUTHOR]

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This study investigated the effects of polyphenols from walnut pellicle on the structure and allergenicity of walnut globulin (WG). The allergenicity-guided assay revealed walnut globulin (WG) from walnut defatted powder without pellicle was the most allergenic protein fraction of walnut. Complexes of phenolic extracts from walnut pellicle (PEWP) and WG were prepared in different ratio and pH conditions to further investigate the effect of PEWP on the protein structure and allergenicity of globulin. The covalent interaction between PEWP and WG in pH 7 was lower than pH 11, according to the free amino groups' content and SDS-PAGE analysis. Comprehensive methods characterized the complexes, including UV–Visible, fluorescence, Fourier transform infrared, and circular dichroism spectroscopy, and indicated that combination of polyphenols with protein altered the secondary and tertiary structure of the protein, leading to the unfolding of the protein structure. Meanwhile, the combination with PEWP reduced the IgG-binding capacity of WG in a dose-dependent manner, reaching a minimum of 26.90 ± 4.31% (at pH 7), which was significantly (P < 0.05) lower compared to that at pH 11 (41.79 ± 1.25%). Correlation analysis revealed a significant correlation between IgG-binding capacity and protein structure, as well as the addition concentration of PEWP (r = −0.85, P < 0.01), and pH conditions may indirectly influence the structure and allergenicity of the protein by affecting the interaction between WG and PEWP. The interaction between WG and PEWP was characterized through fluorescence-quenching mechanism analysis, indicating that polyphenols from PEWP mainly interact with WG through hydrogen bond and hydrophobic interaction. [Display omitted] • Allergenicity-guided assay revealed WG as the main allergenic walnut protein. • Polyphenol ratio and pH value affected structural interaction between phenol and WG. • Pellicle polyphenol induced WG structure unfolding and allergenicity decrease. • Hydrogen bonds and hydrophobic interaction facilitated phenol and WG combination. [ABSTRACT FROM AUTHOR]

The allergenic potential of four digestion-resistant linear epitopes (EADRKYDE, ERAEERAEAG, RSVQKLQKEVDR, and VNEKEKYKGI) in Antarctic krill tropomyosin was investigated through in vivo and in vitro experiments. Mice induced by the four epitopes exhibited obvious clinical allergic symptoms, with significant increases in serum specific antibody levels and blood lymphocytes, neutrophils, and eosinophils (p < 0.05). Additionally, mast cells exhibited pronounced degranulation, as well as increased release of histamine and mMCP-1, and enhanced vascular permeability. Mice challenged with the four epitopes further displayed severe pathological damage. In contrast to the antagonistic effect of interleukin-4 and interferon-γ in the plasma of mice in previous studies, stimulation of the epitopes resulted in immune system dysregulation in mice, with significant increases in the levels of interleukin-4 and interferon-γ to 110.03 pg/mL and 103.59 pg/mL, respectively. The enhanced binding ability of the four epitopes to IgE was also indicated in vitro. The four digestion-resistant epitopes are the major factors to the allergenicity of tropomyosin and have strong sensitizing abilities. This study provides a theoretical basis for using site directed mutagenesis to reduce the allergenicity of tropomyosin in Antarctic krill. [Display omitted] • Four digestion-resistant epitopes from tropomyosin have strong sensitizing abilities. • The immune system was dysregulated with significantly elevated IL-4 and IFN-γ levels. • The enhanced binding ability of the four epitopes to IgE was indicated in vitro. • The four epitopes are the major factors to the allergenicity of tropomyosin. • To provide a scientific basis for further targeted mutation of tropomyosin epitopes. [ABSTRACT FROM AUTHOR]

Allergen modification is a novel strategy for preventing and treating food allergy. Resveratrol (RES) can be used as a modifying ligand for allergens, but the interaction mechanism between RES and allergens is still not detailed, and the ramifications of this interaction on the structure, epitope and allergenicity of allergens are also lacking a clear explanation. In addition, the application of heat can promote protein structure to unfold and expose more binding sites to facilitate interaction. Therefore, in this study, ovalbumin (OVA) was selected as the allergen model and was heated to expose more binding sites. The effects of the interaction between RES and heat-stressed ovalbumin (HOVA) on allergen structure, epitope and allergenicity were investigated by combining routine experimental analysis and computer simulation. Results showed heat stress at 323 K for 15 min could better unfold the molecular structure of OVA. On this basis, the interaction between RES and OVA was strengthened, which showed a static quenching of the ground state complex with binding affinity of 1.25 × 106 L/mol. The binding of RES induced the variation of protein microenvironment, and the overall structure tended to disordered direction. Computer simulation had shown RES could directly act on the IgE epitope region (AA251-260) of the OVA. The allergenicity evaluation experiment further indicated the combination of RES alleviated the IgE binding capacity of HOVA. These findings are helpful to further study the mechanism of RES ligand modification to change food allergy. • Heat at 323 K for 15 min can better expose internal hydrophobic groups of OVA. • The interaction between RES and OVA was strengthed with the application of heat. • RES changed the microenvironment and structural composition of HOVA. • Molecular docking indicated RES interfered with the IgE epitope regions of OVA. • MD simulations can be used as an effective tool to predict bimolecular interaction. [ABSTRACT FROM AUTHOR]

The study aimed to enhance soya milk's bioactivity, amino acid release, digestibility and reduce anti-nutritional factors via high-intensity ultrasound (HIU) 600W. Results demonstrated a substantial increase in the hydroxyl scavenging activity by 44%, a 41% improvement in DPPH, and 36% in ABTS. The amounts of AA released in treated samples were 1061.41 μmol/g, 1297.51 μmol/g, 1768.89 μmol/g, and 2014.23 μmol/g of protein at 0, 5, 10, and 15 min. Moreover, SDS PAGE unveiled a substantial decrease in the depth of bands corresponding to anti-nutritional and allergic proteins in the HIU-treated samples. Additionally, anti-nutritional factors (ANF) analysis demonstrated notable reductions in ANF content. The inhibition rates were 50%, 34%, 57%, 42% and 45% for phytic acid, trypsin inhibitor lipoxygenase, β-conglycinin and glycinin respectively with 15 min HIU application. In addition, in vitro digestion experiments showcased a substantial 21% increase in the digestibility with the applied method as well. [ABSTRACT FROM AUTHOR]

Plant proteins are spreading due to growing environmental, health and ethical concerns related to animal proteins. Proteins deriving from cereals, oilseeds, and pulses are witnessing a sharp growth showing a wide spectrum of applications from meat and fish analogues to infant formulations. Bakery products are one of the biggest markets of alternative protein applications for functional and nutritional motives. Fortifying bakery products with proteins can secure a better amino-acids profile and a higher protein intake. Conventional plant proteins (i.e., wheat and soy) dominate the bakery industry, but emerging sources (i.e., pea, chickpea, and faba) are also gaining traction. Each protein brings specific functional properties and nutritional value. Therefore, this chapter gives an overview of the main features of plant proteins and discusses their impact on the quality of bakery products. [ABSTRACT FROM AUTHOR]

The high-temperature water treatment is one of the methods used to reduce the molecular weight of proteins. In this study, in order to establish a practical method for preparing hypoallergenic materials using the high-temperature water treatment, we investigated the effects of processing temperature on the antigenicity and allergenicity of a food allergen. Additionally, the foaming ability of the samples was also evaluated as a function desired in the food industry. We used ovalbumin as a model allergen. As a result, although there was no significant difference among the samples treated with different processing temperatures, all the antigens treated with high-temperature water showed a decrease in antigenicity and allergenicity. In addition, when ovalbumin was treated at a temperature of 130 °C or higher, there was a significant improvement in foaming properties. These findings indicate that high-temperature water treatment is a potential strategy for preparing practical hypoallergenic materials. [ABSTRACT FROM AUTHOR]

Bovine casein, particularly α-casein, is a common source of allergenic epitopes that trigger adverse immune responses in susceptible individuals. In this study, we developed a method to significantly reduce the antigenicity of α-casein by combining hydrolysis with yeast and alkaline proteases. enzyme-linked immunosorbent assay, liquid chromatography coupled with tandem mass spectrometry, Tricine-SDS-PAGE, and electronic tongue were employed to assess the products of two-step hydrolysis. Infant and child allergy serum was used to evaluate IgE binding capacity. The serum IgE inhibition rate of the hydrolysate was 23.55% and the antigenicity of α-casein decreased by 81.40%. The bitterness and astringency produced during hydrolysis are also reduced. These results indicate that the combined hydrolysis of Clavispora lusitaniae DPU-MWFCl-D2 with an alkaline protease enhances the breakdown of allergenic epitopes, striking a balance between diminished antigenicity and good taste. This study provides a potential solution for developing hypoallergenic dairy products. [Display omitted] • Casein antigenicity reduced by a Clavispora lusitaniae strain and alkaline protease. • Allergic epitopes were targeted hydrolysis via computer simulation after strain fermentation. • The combined hydrolysis mitigates the bitter and astringent flavours. [ABSTRACT FROM AUTHOR]

Les allergènes polliniques appartiennent à différentes familles de protéines PR (PR pour Pathogenesis-Related), protéines impliquées dans les mécanismes de défense développés par les plantes : PR-2 ou endo β-glucanases, PR-3 ou chitinases, PR-5 ou thaumatin-like protéines (TLP), PR-10 ou protéines Bet v 1-like, PR-12 ou défensines et PR-14 ou protéines de transfert des lipides (LTP). D'autres allergènes polliniques correspondent à des protéines à rôle structural (profilines, expansines), métabolique (polcalcine) ou enzymatique (ribonucléases, pectate lyases, polygalacturonases). Les structures trimdimensionnelles de la plupart des allergènes polliniques ont été caractérisées, les structures manquantes étant souvent accessibles par modélisation moléculaire à partir de patrons structuraux connus. Les épitopes B liant les IgE d'un petit nombre d'allergènes polliniques ont été identifiés par différentes approches (cartes épitopiques et analyse des complexes allergène-IgE), et les épitopes T de nombreux allergènes sont actuellement connus. Le caractère dégénéré de la reconnaissance des épitopes T par les récepteurs TCR, explique qu'un même TCR puisse reconnaître des épitopes T différents et, inversement, qu'un même épitope T puisse être reconnu par des TCR différents. L'identification de ces épitopes apporte une contribution essentielle dans différents domaines comme l'utilisation des allergènes polliniques recombinants ou naturels pour le diagnostic biologique des pollinoses ou l'utilisation d'épitopes T en immunothérapie spécifique. Ils permettent également de prédire les possibilités de réactions croisées et de co-sensibilisation entre des allergènes polliniques d'origine différente ou dans le syndrome oral entre des allergènes polliniques et des allergènes de fruits ou de légumes. Ces différents aspects moléculaires sont abordés dans cette revue. Pollen allergens belong to various families of PR (i.e. pathogenesis-related) proteins involved in plant defense mechanisms, such as PR-2 (endo-glucanases), PR-3 (chitinases), PR-5 (thaumatin-like proteins or TLP), PR-10 (Bet v 1-like proteins), PR-12 (defensins) and PR-14 (lipid transfer proteins or LTP). They may also comprise proteins with other functions such as structural function (profilin, expansins), metabolic function (polcalcin) or enzymatic function (ribonucleases, pectate lyases, polygalacturonases) (e.g. ribonucleases, pectate lyases and polygalacturonases). The structural scaffolds of the major weed and tree pollen allergens have been identified either by X-ray crystallography or by NMR for smaller molecules such as LTP and polcalcin. Other pollen allergens of unknown structure have been successfully modelled from templates belonging to the same protein families. Epitope mapping of free allergens and analysis of allergen-IgE complexes enabled identification of IgE-binding B-cell epitopes at the surface of a few pollen allergens. A higher number of T-cell epitopes were identified along the amino acid sequence of various pollen allergens likely to interact with CD4+ T lymphocytes via T-cell receptors (TCRs). However, this low-affinity recognition of T-cell epitopes by TCRs is degenerate, allowing a single TCR to recognize different T-cell epitopes, and, conversely, enabling many different TCRs to recognize the same T-cell epitope. The identification of both B- and T-cell epitopes of pollen allergens is of paramount importance in optimizing the use of natural and recombinant pollen allergens as molecular tools for the component-resolved diagnosis of pollinoses and in improving current immunotherapy practice, for instance by reducing side effects associated with immunotherapy. In addition, identification of B- and T-cell epitopes may provide valuable assistance in the prediction of IgE-binding cross-reactivity and co-sensitization among pollen allergens of different origins, and between pollen and fruit or vegetable allergens responsible for oral allergy syndrome (OAS). Our review aims to present an overview of all these molecular aspects of pollen allergens. [ABSTRACT FROM AUTHOR]

Currently, the increasing frequency of inhalant allergy is often linked to the urbanization effect. The pollen forecasts for a given city are most often prepared using data from one aerobiological station. However, there is evidence that the pollen concentrations in the air might differ depending on the city area and the height of the pollen trap. This study evaluated the spatial differences in the daily concentrations of alder and birch pollen grains in an urban area in relation to the proximity of the pollen sources and meteorological parameters. Pollen grains were sampled in Rzeszów in 2014–2016 by three volumetric traps located at the roof and nose levels in two city areas that differed in the numbers of alder and birch trees. The daily pollen concentrations were categorized into three allergy symptom thresholds. The relationship between the daily pollen concentrations and meteorological variables was examined using a redundancy analysis and circular statistics. There were spatial differences in the pollen season intensity and, to a lesser extent, the variability in its course. Generally, higher concentrations were registered at the roof level and in the city suburbs than at the nose level and in the downtown area where alder and birch trees were less numerous. Despite the spatial variability of the pollen concentrations and the differences in the proximity and abundance of pollen sources, the risks for allergy sufferers were similar throughout the city. It was concluded that the main cause of this phenomenon is the high dispersal abilities of Alnus and Betula pollen grains. Although temperature seems to be a crucial factor that influences the airborne pollen of both taxa, several weather variables were found to have complex impacts on the daily concentrations. [ABSTRACT FROM AUTHOR]

Protein fractions were isolated from wheat flour including albumin, globulin, glutelin-1, glutelin-2 and prolamin. The free and bound phenolics were extracted from each protein fraction to determine the impact of their removal on allergenicity, antioxidant activity and the inhibitory activities of the angiotensin converting enzyme. The glutelin-1 fraction showed the highest protein content and yield of 71.02% and 21.02%, respectively. The highest antioxidant activity was noted in the glutelin-1 fraction (48.17%). The angiotensin converting enzyme inhibitory activities among the protein fractions ranged from 6.87% to 84.52%. The greatest reduction of allergenicity (39.66%) was demonstrated in the prolamin fraction. We conclude that the removal of phenolics appears to decrease significantly the allergenicity of wheat protein fractions while maintaining significant bioactivities related to anti-hypertensive, antioxidant, and anti-diabetic properties. [ABSTRACT FROM AUTHOR]

The levels of food allergens in worm-wounded or non-wounded green soybeans (edamame) and mature soybeans were investigated by immunoblotting and enzyme-linked immunosorbent assay (ELISA), using allergen-specific antibodies. Non-wounded and worm-wounded soybeans showed similar total protein profiles after Coomassie brilliant blue staining, but some protein bands were observed to have been changed by worm wounding. Immunoblotting with specific antibodies for major soybean allergens (Gly m 5, Gly m 6, Gly m Bd 30 K, and Kunitz soybean trypsin inhibitor) revealed that protein band profiles and intensities were not significantly changed by worm wounding. In contrast, levels of the pollen-related soybean allergens Gly m 4 and Gly m 3 were strongly increased by worm wounding in both green and mature soybeans, as detected by immunoblotting and ELISA. These results suggested that the pollen-related food allergen risk (i.e., oral allergy syndrome; OAS) from soybeans might be enhanced by worm wounding of soybeans. [ABSTRACT FROM AUTHOR]

Ozone (O 3 ) and nitrogen dioxide (NO 2 ) are thought to play primary roles in aggravating air pollution-induced health problems. However, the effects of joint O 3 /NO 2 on the allergenicity of pollen allergens are unclear. Humulus japonicus pollen allergen 1 (Hum j1) is a profilin protein that causes widespread pollinosis in eastern Asia. In order to study the effects of combined O 3 /NO 2 on the allergenicity of Hum j1, tandem six-histidine peptide tag (His6)-fused recombinant Hum j1 (rHum j1) was expressed in a prokaryotic system and purified through His6 affinity chromatography. The purified rHum j1 was used to immunize SD rats. Rat sera with high titers of IgG and IgE antibodies against rHum j1 were used for allergenicity quantification. The rHum j1 was exposed to O 3 /NO 2 , and changes in allergenicity of the exposed rHum j1 were assayed using the immunized rat antibodies. Tandem LC-MS/LC (liquid chromatography-mass spectrometer/liquid chromatography spectrometer) chromatography and UV and circular dichroism (CD) spectroscopy were used to study the structural changes in rHum j1. Our data demonstrated that a novel disulfide bond between the sulfhydryl groups of two neighboring cysteine molecules was formed after the rHum j1 exposure to joint O 3 /NO 2 , and therefore IgE-binding affinity was increased and the allergenicity was reinforced. Our results provided clues to elucidate the mechanism behind air pollution-induced increase in pollinosis prevalence. [ABSTRACT FROM AUTHOR]

• Digitization of 3D allergenicity data set. • Way of representing potential allergenicity in 3D maps. • Eco-design for reducing exposure and building healthier environment. It is essential to study the air quality of modern urban areas to improve the tolerance to health issues related to allergenicity in cities. The objective of this study was to develop a methodology for representing allergenicity by applying the Urban Green Zone Allergenicity Index (I UGZA) to urban environments and producing 3D maps. This study is based on an inventory of green infrastructure with information obtained through fieldwork and from accurate images of the actual conditions such as orthophotos and Light Detection and Ranging (LiDAR) clouds of points, which were used in the production of 3D maps. The inventory data were stored and georeferenced in a Geographic Information System (GIS) model, which was also used to extract geometrical information for the I UGZA index calculation. The allergenicity results from the index application are represented in the GIS model and exported to the Google Earth map system. The developed methodology was applied to a park (25 ha of surface) on the right margin of the Guadiana River in Badajoz (Spain). An I UGZA value of 0.093 was obtained for the inventory index calculation and 0.063 for the calculation method developed using GIS. Furthermore, two reduction-of-exposure simulations were performed to recalculate the I UGZA values, and successful results were obtained. The results showed that the proposed methodology provides an effective technique of representing potential allergenicity in 3D maps as an eco-design to reduce exposure to urban green infrastructure and to build a healthier environment in construction engineering. [ABSTRACT FROM AUTHOR]

The development process of fermented milk products with low-allergenic potential usually begins with the isolation and screening of strains. However, this bottom-up screening method is time-consuming and heavy workload. Once the target strain is not screened, it will cause a waste of time and money. This experiment adopted a top-down method to screen strains quickly and efficiently and prepared a fermented milk with low whey protein allergenic potential. The traditional fermented dairy products from Xinjiang are a good source for screening functional strains. We took 59 traditional fermented dairy products from Xinjiang as samples. The antigenicity of α-lactalbumin (α-LA) and β-lactoglobulin (β-LG), the main allergenic proteins which are easy to cause human allergy, were taken as the indicators. Through direct screening of the fermented dairy product with the lowest antigenicity, the BZ-21 sample was selected as the target sample. The 13 strains isolated from the BZ-21 sample were safe, and the antigenicity and immunoglobulin E (IgE)-binding capacity of the fermented milk prepared under optimized fermentation conditions were reduced. The results showed that the top-down screening method used in this experiment was effective, and these 13 strains will be potential probiotics in the development of low-allergenic dairy products. • A top-down method was used to screen strains for the preparation of fermented dairy product with low antigenicity. [ABSTRACT FROM AUTHOR]

[Display omitted] • Conjugation of EGCG and CHA reduced caused the structure of 11S to unfold. • Conjugation of EGCG and CHA reduced the allergenicity of 11S. • Hypoallergenic 11S-EGCG conjugates can induce oral tolerance in mice. Soybean 11S globulin is one of the most important allergens in soybean. This study investigated the effects of 11S covalent that conjugated covalently with (−)-Epigallo-catechin 3-gallate (EGCG) and chlorogenic acid (CHA) on protein structure, digestibility, and allergenicity. 11S conjugation with EGCG and CHA yielded covalent conjugates and formed cross-linked protein polymers, which changed the structures and increased the digestibility of the protein. In vitro experiments showed that the ability of IgE binding, and stimulation mast cell degranulation were lower for11S-EGCG and 11S-CHA conjugates compared to 11S. In vivo experiments showed that conjugation of EGCG and CHA reduced the allergenicity of 11S. The oral tolerance model showed that hypoallergenic 11S-EGCG conjugates successfully relieved allergic symptoms and induced oral tolerance by affecting antigen presentation, activating Treg cells to produce IL-10, and promoting Th1/Th2 immune balance. This study presented an innovative strategy to develop hypoallergenic food production that induce tolerance for allergen-specific immunotherapy. [ABSTRACT FROM AUTHOR]

[Display omitted] Presently, many studies assess allergenicity via IgE immunoblotting and IgE binding tests; however, IgE detection does not always signal the manifestation of a clinical allergy. However, the capacity of food allergens to trigger basophils makes it possible to use the in vitro functional basophil activation test (BAT) to assess allergenicity. The effect of the Maillard reaction (MR) on the allergenic potential of processed soy proteins was evaluated by two IgE binding tests (Competitive ELISA and Inhibition ImmunoCAP), a Western Blot and a functional BAT; with the aim to analyze whether the sIgE binding results correspond to the functional assay results. The results between the IgE binding tests and the functional assay were in-line for 2 of the 6 studied patients. For one patient there was no correlation between any of the results. For the raw soy protein extract heated with glucose for 10 and 30 min (SH SPE + Glu and LH SPE + Glu, respectively), the results were in-line for only 3 out of the 6 patients. Thus, the present study shows a discrepancy between IgE binding tests and basophil stimulation when assessing the effect of soy processing on its allergenicity. Since IgE-binding capacity does not always correlate to IgE cross-linking capacity, the conclusions of the allergenic potential based on the IgE binding tests alone should be drawn with care and further studies on this matter would benefit from the inclusion of a functional assay such as the BAT. [ABSTRACT FROM AUTHOR]

Résumé Introduction La compréhension des mécanismes d’hydrolyse des protéines alimentaires lors de la digestion est particulièrement importante pour étudier le potentiel antigénique des aliments. Le lait est l’un des aliments responsables de la majorité des réactions allergiques chez l’enfant, et cela même avec les formules infantiles hypoallergéniques, hydrolysats partiels de protéines du lait de vache, dans les cas où l’allaitement maternel n’est pas possible. Ces laits hypoallergéniques présentent toujours un risque fréquent d’allergie croisée constatée depuis plus de dix années. Il apparaît donc crucial d’étudier la dégradation des principaux allergènes de cet aliment. But de l’étude Ce travail avait pour but d’évaluer l’effet de l’hydrolyse enzymatique des protéines du lactosérum du lait de chamelle ( Camelus dromedarius ) sur l’activité antigénique des protéines comparé avec celle du lait de vache. Nous avons utilisé deux protéases gastro-intestinales : la pepsine et la trypsine. Matériel et méthode La première étape est la caractérisation biochimique. Nous avons mesuré la teneur en protéines solubles du lactosérum des deux laits par la méthode de Lowry, et par l’action de ces différentes protéases sur ces protéines, des hydrolysats partiels ont été obtenus. Ces derniers ont été mesurés par la quantité des fonctions α-NH 2 libérées selon la méthode de Doi et identifiés par l’électrophorèse. Une évaluation de l’antigénicité des hydrolysats du lactosérum vis-à-vis des IgG anti-β-lactoglobuline et anti-α-lactalbumine obtenues à partir d’un modèle animal (souris BALB/c) sensibilisé aux protéines du lait de vache la β-Lg et l’α-Lac par voie intrapéritonéale par la méthode Elisa. Résultats Les résultats obtenus montrent que le taux de protéines du lactosérum du lait de chamelle est plus élevé que celui du lait de vache. Le dosage des fonctions α-NH 2 libres montre que le lactosérum du lait de chamelle est plus sensible à la digestion pepsique/trypsique que le lactosérum bovin. Les profils électrophorétiques des hydrolysats révèlent que le lactosérum du lait de chamelle montre l’apparition de nouvelles bandes peptidiques, résultat de la dégradation des protéines. Par contre, le lactosérum bovin résiste à l’hydrolyse pepsique. L’hydrolyse pepsique/trypsique affecte d’avantage l’antigénicité des protéines du lactosérum du lait de chamelle que le lactosérum bovin en les diminuant significativement. Conclusion En conclusion la digestion pepsique/trypsique de lactosérum du lait de chamelle est plus importante que celle du lait de vache, avec une très forte diminution de l’antigénicité des hydrolysats trypsiques des lactosérums du lait des deux espèces vis-à-vis des IgG anti-α-Lac. Introduction Understanding the mechanisms of the hydrolysis of food proteins during digestion is particularly important when considering the antigenic potential of food. Milk is one of the foods responsible for a large majority of allergic reactions in children, even when the children are fed with hypoallergenic infant formulas or partial hydrolysates of cow's milk protein and in cases where breastfeeding is not possible. It has been known for over ten years that hypoallergenic milk carries a frequent risk of cross-reactivity. For this reason, it is important to study the degradation of the main milk allergens. Aim of the study This work was designed to evaluate the effect of enzymatic hydrolysis of whey proteins from camel's milk ( Camelus dromedarius ) on their antigenic activity compared to that of cow's milk whey proteins. Material and methods The first step was biochemical characterization. We used two gastrointestinal proteases, pepsin and trypsin, for partial hydrolysis of the two milk proteins. The soluble protein content of the whey of the two milks was determined using the Lowry method. The hydrolyzed protein content was determined by measuring the amount of liberated alpha-NH 2 functions according to the method of Doi and then they were identified by electrophoresis. Evaluation of the antigenicity of these whey hydrolysates using IgG anti-β obtained from an animal model (BALB/c mice) that were sensitized intraperitoneally to cow's milk proteins β-lactoglobulin and anti-α-lactalbumin Elisa. Results The results showed that the rate of hydrolysis of camel's milk whey proteins is greater than that of cow's milk whey proteins and that the measure of free alpha-NH 2 functions shows that camel's whey proteins are more sensitive to pepsin and trypsin digestion than cow's milk whey proteins. The electrophoresis profiles of the hydrolysates showed that camel's milk whey proteins were degraded more quickly; they also revealed new peptide bands unlike those seen with bovine whey, which means that bovine whey resists peptic hydrolysis. Conclusion Pepsin/trypsin hydrolysis can affect the allergenicity and the antigenicity of whey proteins of camel's milk, decreasing them significantly, whereas hydrolysis of bovine whey proteins may not affect their allergenicity and antigenicity. [ABSTRACT FROM AUTHOR]

Two protein fractions rich in γ-globulins (FI) and α- and β-globulins (FII) were generated from bovine blood and hydrolysed with the enzyme papain. The generated hydrolysates showed in vitro angiotensin-I-converting enzyme (ACE-I), renin, and dipeptidyl peptidase-IV (DPP-IV) inhibitory activities. A total of 626 and 2246 peptides were identified by LC-MS/MS from the 1 kDa fractions of FI and FII, and the potential toxicity and allergenicity of these peptides were assessed in silico using three independent predictive approaches. All of the peptides identified from the bioactive blood protein fractions FI and FII were predicted to be non-toxic. However, 72 peptides from FI and 492 peptides from FII were identified as potential allergens with at least two predictive approaches. Results suggested that papain hydrolysates of FI and FII contain potential allergenic peptides, and those products containing such hydrolysates should be labelled correctly in line with Food and Consumer legislation – Regulation (EU) No.1169/2011. [ABSTRACT FROM AUTHOR]

Interest in the climate and an awareness of the beneficial cooling influence exerted on it by biologically-vital areas is growing, as climate change progresses, hot weather is more frequent as well as the urban heat island more intense. It is necessary to protect existing greenery in the cities and to introduce new planting. However plants in a warmer climate can produce larger amounts of pollen and are more readily able to initiate an allergic reaction among those prone to them. That means—not every greenery is advantageous for humans in the cities. In the research two housing estates built at different times and differ in type, density and age of buildings, as well as in the composition and the percentage of biologically vital area and the species planted were examined. Detailed inventory of tall greenery entailed the trees and shrubs and next their assumed allergenic potential was made. Cooling effect likely is derived from the difference in greenery, but the other factors such as differences in the density of buildings and spatial organization of the estate could also influence it. The older estate with the ratio of biologically vital areas of 54.3% is characterised by more favourable local climate than the newer estate, with the ratio of biologically vital areas equals 40.7% and young vegetation. On the newer one the perceptible thermal conditions did not differ significantly compared with the city centre. Unfortunately, on Koło Estate trees creating mild thermal conditions are also the trees promoting allergies most severely: birches, poplars and limes. And they are planted usually around playgrounds and kindergarten. The trees of high allergenicity should be partially removed, even risking small worsening thermal conditions. [ABSTRACT FROM AUTHOR]

Résumé Des protéines végétales à propriétés édulcorantes sont utilisées dans différents secteurs de l’alimentation humaine où elles remplacent les édulcorants de synthèse. C’est le cas de la thaumatine, protéine édulcorante extraite de l’arille des fruits du katemfe ( Thaumatococcus daniellii ). Deux autres protéines édulcorantes à pouvoir sucrant élevé, la brazzéine des fruits de Pentadiplandra brazzeana et la monelline des fruits de Dioscoreophyllum cumminsii , sont également disponibles, mais leur production industrielle n’est pas encore programmée. Bien qu’elles soient exprimées de façon constitutive dans les fruits, la plupart de ces protéines correspondent à des protéines de défense de la plante ou protéines PR, dont la synthèse est exacerbée lorsque la plante est en conditions de stress, lors d’une attaque fongique, par exemple. Les homologies de séquence, et surtout de structure, que ces protéines édulcorantes partagent avec des allergènes avérés, avec Art v 1 pour la brazzéine, avec Mus a 4 ou Ole e 13 pour la thaumatine, avec Ana o 3 ou Pis v 1 pour la mabinline, avec l’inhibiteur de Kunitz du soja pour la monelline, suggèrent une possible allergénicité de ces protéines végétales. Néanmoins, leur potentiel allergénique reste à démontrer lors de leur consommation alimentaire. Plant proteins with sweet-tasting properties are increasingly used as substitutes for low-calorie sweeteners in the food industry. Thaumatin, the sweet protein isolated from the aril of the katemfe fruit ( Thaumatococcus daniellii ), is widely used as a natural sweetener. Two other low-calorie sweeteners with enhanced sweet-tasting properties, brazzein and monellin, which are isolated from the fruits of Pentadiplandra brazzeana and Dioscoreophyllum cumminsii , respectively, are still waiting to be produced on a large scale as recombinant sweet proteins for food industry. Although these sweet-tasting proteins are constitutively expressed in fruits, most of them consist of PR-proteins whose synthesis is strongly enhanced as a result of infection of the plant by phytopathogenic micro-organisms, fungi or molds. Both the sequence and structural similarities which the sweet proteins share with allergens, e.g., Art v 1 for brazzein, Mus a 4 and Ole a 13 for thaumatin, Ana o 3 and Pis v 1 for mabinlin, and Gly m Kunitz trypsin-inhibitor for monellin, suggest some possible allergenic propensity for these plant proteins. However, their allergenic potential following ingestion still remains to be demonstrated unambiguously. [ABSTRACT FROM AUTHOR]

Background: Modification of native peanut extracts could reduce adverse effects of peanut immunotherapy. Objective: We sought to compare native and chemically modified crude peanut extract (CPE) and major peanut allergens Ara h 2 and Ara h 6 in a mediator-release assay based on the rat basophilic leukemia (RBL) cell line transfected with human Fcε receptor. Methods: Native Ara h 2/6 was reduced and alkylated (RA), with or without additional glutaraldehyde treatment (RAGA). CPE was reduced and alkylated. Sera of subjects with peanut allergy (16 males; median age 7 years) were used for overnight RBL-passive sensitization. Cells were stimulated with 0.1 pg/mL to 10 μg/mL of peanut. β-N-acetylhexosaminidase release (NHR) was used as a marker of RBL degranulation, expressed as a percentage of total degranulation caused by Triton X. Results: Median peanut-specific immunoglobulin E was 233 kUA/L. Nineteen subjects were responders, NHR ≥ 10% in the mediator release assay. Responders had reduced NHR by RA and RAGA compared with the native Ara h 2/6. Modification resulted in a later onset of activation by 10- to 100-fold in concentration and a lowering of the maximum release. Modified RA-Ara h 2/6 and RAGA-Ara h 2/6 caused significantly lower maximum mediator release than native Ara h 2/6, at protein concentrations 0.1, 1, and 10 ng/mL (p < 0.001, < 0.001, and < 0.001, respectively, for RA; and < 0.001, 0.026, and 0.041, respectively, for RAGA). RA-CPE caused significantly lower maximum NHR than native CPE, at protein concentration 1 ng/mL (p < 0.001) and 10 ng/mL (p < 0.002). Responders had high rAra h 2 immunoglobulin E (mean, 61.1 kUA/L; p < 0.001) and higher NHR in mediator release assay to native Ara h 2/6 than CPE, which indicates that Ara h 2/6 were the most relevant peanut allergens in these responders. Conclusions: Chemical modification of purified native Ara h 2 and Ara h 6 reduced mediator release in an in vitro assay ∼100-fold, which indicates decreased allergenicity for further development of the alternative candidate for safe peanut immunotherapy. [ABSTRACT FROM AUTHOR]

Peanut allergy is a type of serious food allergy worldwide. In this study, peanuts were treated with two different cooking methods. The effect of cooking on digestion stability was evaluated by simulated gastrointestinal digestions. The effects of cooking on the allergenicity were assessed by immunoblotting, passive cutaneous anaphylaxis (PCA) mice model and rat basophilic leukemia (RBL)-2H3 cell model. Results showed that raw peanuts were more stable to digestion than boiled and fried peanuts. SDS-PAGE showed that the quantities of allergens Ara h 1 (64 kDa), Ara h 2 (20 kDa), and Ara h 3 (38 kDa) in the boiled and fried peanuts were all reduced. Meanwhile, immunoblotting revealed the IgE binding capacities of boiled and fried peanuts were decreased significantly, especially the fried peanuts. In the PCA mice model, the vascular permeability of allergic mice, as well as the release of histamine, were both alleviated in mice gavaged with boiled and fried peanuts compared with raw peanuts. Lastly, the release of β-hexosaminidase of RBL-2H3 cells treated with boiled and fried peanuts was significantly decreased compared with the raw peanuts. In addition, the analyses of circular dichroism (CD) spectra showed that the α-helical content of peanut proteins was decreased after boiling and frying, indicating the structure stability of peanut allergens decreased. The analyses of ultraviolet (UV) spectra showed that aromatic amino acid residues were exposed, causing the change of the tertiary structure of peanut allergens after boiling and frying. In conclusion, the allergenicity of peanuts was significantly reduced after boiling and frying, especially frying. [ABSTRACT FROM AUTHOR]

Various biosynthesised compounds from ornamental plants can be harmful to man, throughout a plant's entire life cycle or only during certain moments, present in all of its organs or restricted only to some. Interdisciplinary research regarding plant toxins and allergens are being conducted worldwide, aiming to prevent the production of diseases. The research aimed to phytochemically classify vegetal compounds with toxic and allergenic characteristics found in ornamental plants, to identify the main pathogenic pathways through which these compounds act and to come up with recommendations regarding valorification of these plants. The study focuses on ornamental plants in both spontaneous and cultivated flora, in protected or unprotected spaces, commonly met in Romania. The current review includes vegetal allergens in the toxic vegetal substances group, from the perspective of modern definitions of toxicity. Based on phytochemical criteria, a classification of toxic vegetal compounds (including allergens) was achieved. Common native toxic ornamentals from our habitat are tabulated. Some non-native species were included on the basis of their high presence as house plants. Correlated to the commercial practices in Romania, the risks for ambient health were identified, both at the work place, at home and in the public space. Ornamentals can be dangerous to man's health. The majority of toxic and allergenic substances (excluding pollens) are secondary metabolism compounds. Given these risk factors to health, it is necessary to impose health and safety regulations at work, to inform the general population regarding potential negative effects and to commercialize plants with labels which should contain warnings about the risk of diseases or the aggravation of existing ones. [ABSTRACT FROM AUTHOR]

The article offers information related to the effect of gamma irradiation on food allergens levels in Soybean. Topics discussed include irradiation of the soybeans, protein analysis of soybean extract by immunoblotting and enzyme-linked immunosorbent assay (ELISA) and evaluation of the allergen levels by competitive inhibition ELISA with allergen-specific antibodies.

The relatively easy access to fish worldwide, alongside the increase of aquaculture production contributes to increased fish consumption which result in higher prevalence of respective allergies. Allergies to fish constitute a significant concern worldwide. β-parvalbumin is the main elicitor for IgE-mediated reactions. Creatine, involved in the muscle energy metabolism, and ethylenediamine tetraacetic acid (EDTA), a calcium chelator, are potential molecules to modulate parvalbumin. The purpose of this study was to test creatine (2, 5 and 8%) and EDTA (1.5, 3 and 4.5%) supplementation in fish diets to modulate β-parvalbumin expression and structure and its allergenicity in farmed European seabass (Dicentrarchus labrax) while assessing its effects on the end-product quality. Fish welfare and muscle quality parameters were evaluated by plasma metabolites, rigor mortis , muscle pH and sensory and texture analysis. Proteomics was used to assess alterations in muscle proteome profile and metabolic fingerprinting by Fourier transform infrared spectroscopy was used to assess the liver metabolic profile. In addition, IgE-reactivity to parvalbumin was analysed using fish allergic patient sera. Metabolic fingerprinting of liver tissue revealed no major alterations in infrared spectra with creatine supplementation, while with EDTA, only absorption bands characteristic of lipids were altered. Comparative proteomics showed up regulation of (tropo) myosin and phosphoglycerate mutase 2 with Creatine supplementation. In the case of EDTA proteomics showed up regulation of proteins involved in cellular and ion homeostasis. Allergenicity seems not to be modulated with creatine or EDTA supplementation as no decreased expression levels were found and IgE-binding reactivity showed no quantitative differences. [Display omitted] [ABSTRACT FROM AUTHOR]

Cow milk allergy is a major cause of food hypersensitivity in infants and children. However, to the best of our knowledge, there has been minimal research on the antigenicity of cow milk (CM). As it is currently unknown if enzymatically hydrolyzed cow milk (HM) induces severe immunogenic responses, the potential allergenicity of HM was systematically evaluated in this work. HM effectively attenuated symptoms of weight loss and diarrhea, suppressed levels of mast cell tryptase, and relieved allergic inflammation of the intestine. Moreover, HM reduced the B220+ cell count in mouse blood. In addition, in vitro studies demonstrated that gastrointestinal digestion of HM was not resistant to pepsin or trypsin. Thus, HM effectively alleviated allergic reactions and exhibited lower potential allergenicity. These results provide practical information for the future development of hypoallergenic CM products. • Assessment of the allergenicity potential in HM. • HM could effectively attenuate symptoms of weight loss and diarrhea. • HM could suppress MCT levels, relieve allergic inflammation of intestines. • HM could reduce B220+ cell count in the blood of mice. • HM was not resistant to pepsin or trypsin in vitro digestion. [ABSTRACT FROM AUTHOR]

The article discusses a study which evaluated the immunological and clinical response of consumption of lysozyme-containing cheese in egg-sensitive adults with or without lysozyme sensitization. It describes the use of the lysozyme in the manufacture of cheese to prevent "late blowing," a defect of long-ripened hard cheese. The study observed no adverse reactions in the two groups of patients used after cheese samples were given.

Abstract: Urban green spaces are a key element in the planning of today''s cities, since they favor the interaction between citizens and the environment, as well as promoting human health. However, lack of planning in the design of urban spaces and in the choice of ornamental species has been among the factors triggering one of the most widespread diseases in urban populations: pollen allergy. In this paper are reviewed the major causes of this extensive allergenicity, including: low species biodiversity at planting; the overabundance of given species acting as key specific pollen sources; the planting of exotic species prompting new allergies in the population; the choice of male, pollen-producing individuals in dioecious species; the presence of invasive species; inappropriate garden management and maintenance activities; the appearance of cross-reactivity between phylogenetically related species; and the interaction between pollen and air pollutants. The findings of this analysis highlight the clear need for guidelines regarding the design and planning of urban green spaces with a low allergy impact. Proposals include increased biodiversity, careful control when planting exotic species, the use of low pollen producing species, the adoption of appropriate management and maintenance strategies, and active consultation with botanists when selecting the most suitable species for a given green space. [Copyright &y& Elsevier]

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Why specific, ubiquitous, otherwise innocuous environmental proteins tend to provoke maladaptive, TH2-polarized immune responses in susceptible hosts is a fundamental mechanistic question for those interested in the pathogenesis, therapy, and prevention of allergic disease. The current renaissance in the study of innate immunity has provided important insights into this question. The theme emerging from recent studies is that direct (dys)functional interactions with pathways of innate immune activation that evolved to signal the presence of microbial infection are central to the molecular basis for allergenicity. This article reviews these data. [Copyright &y& Elsevier]

Background: Fenugreek is an ingredient in Indian-style spiced foods. Reports of adverse reactions reflect a trend toward a more international cuisine. Fenugreek allergy has not been systematically investigated so far. Objective: Study the allergenicity and antigenicity of fenugreek proteins using patient sera and a newly developed polyclonal antifenugreek antibody. Methods: Allergenic fenugreek proteins were identified by immunoblotting, using sera from 29 patients with specific IgE to peanut and other legumes. In addition, 2 patients were evaluated by skin prick test and open food challenge with native fenugreek powder. Spiced and flavored food products were analyzed for fenugreek by semiquantitative IgE and IgG immunoblotting. Results: High levels of specific IgE to both peanut and fenugreek were seen in most sera. Fenugreek sensitization is believed to be a consequence of cross-reactivity in patients with peanut allergy. Primary fenugreek allergy was suspected in only 1 case. The fenugreek dose eliciting objective symptoms was about 2 mg in the open food challenge. Major fenugreek allergens were identified at 50, 52, and 74 kd and peanut proteins at 22, 36, and 40 kd. A specific polyclonal antifenugreek antibody was found suitable for food analysis. In a food survey, about 1/3 of the fenugreek-containing products were labeled correctly. Conclusion: Fenugreek seed powder, an ingredient in spiced foods, contains several potential allergens. There is evidence for a high rate of cross-reactivity to peanut. [Copyright &y& Elsevier]

Peanut allergy is among the most widespread and life-threatening food allergies. Roasting was conducted to improve the sensorial quality of peanut and to change the structure and allergenicity of allergens. The potential allergenicity of digested defatted peanut powder did not significantly differ between raw and roasted peanuts. The raw/roasted peanut proteins were digested by trypsin and then analyzed with isobaric tags for relative and absolute quantitation (iTRAQ) to discover the changes in peptide quantity. Among the 44 detected peptides, the abundance of 29 peptides significantly increased by up to 36.78 times after roasting. Among those 29 peptides, seventeen peptides overlapped with linear IgE-binding epitopes, which were either destroyed or exposed after roasting. Combined with the spatial structure model, the iTRAQ result indicated the breaking of disulfide bonds and depolymerization of proteins during roasting. Roasting changed the conformational structure of protein, which increased allergen digestibility but did not guarantee a decrease in the potential allergenicity of peanut. [ABSTRACT FROM AUTHOR]

[Display omitted] • OVA showed lower allergenicity in vitro and in vivo after oxidation. • Oxidation increased digestibility and functional properties of OVA. • Oxidation provide a new method to process hypoallergenic OVA. Ovalbumin (OVA) is one of the major allergenic proteins in egg that contain numerous functional properties. Here, oxidation-induced changes to the structure, functional properties, and allergenicity of OVA were evaluated after 2,2′-azobis (2-amidinopropane) dihydrochloride (AAPH) and acrolein treatment. Oxidation complexes were prepared by the lipid peroxidation, which caused structural changes, and increased digestibility, foaming, and emulsifying properties. The IgE-binding capacity of OVA decreased after oxidation. KU812 cell assay showed that the histamine and IL-4 levels decreased upon oxidation with AAPH and acrolein. A mouse model study showed that oxidation caused a reduction in the allergenicity by reducing IgE and IgG1 levels and the production of Th2 cytokines after acrolein (1 mmol/L) and AAPH (5 mmol/L) treatment. Thus, OVA could cause changes to structural and functional properties, modulating Th1/Th2 immunobalance, and reducing potential allergenicity after oxidation by lipid peroxidation, which might provide an effective and potential method to process hypoallergenic OVA. [ABSTRACT FROM AUTHOR]

The article reports on results of a study which determines antihypertensive peptides from an izumi shrimp hydrolysate. A description of the study design and method is presented. The study concluded that angiotensin I-converting enzyme inhibitory peptides isolated from the izumi shrimp hydrolysate had an anti-hypertensive effect on rats.

The article evaluates the allergenicity of the gliadin using sera from patients RAST-positive to wheat. According to the authors, the addition of cysteine before the treatment with a cation exchanger effectively increased the deamidation level of gliadin. They add deamidated gliadin showed higher solubility than the undeamidated form. They also mention that rats administered with deamidated gliadin showed suppressed elevation of the gliadin-specific immunoglobulin E level.

The article presents a study which analyzes the effect of the consumption of hypoallergenic wheat flour (HFW) on the expression of a wide spectrum of genes. A DNA microarray was used and gene expression profiles in the liver and intestines of rats fed mainly with HFW were compared with those of rats fed on a normal flour-based diet. The DNA microarray technology presents an efficient method for evaluating the safety of foods.

Background: The safety issues regarding foods derived from genetically modified (GM) plants are central to their acceptance into the food supply. The potential allergenicity of proteins newly introduced in GM foods is a major safety concern. Objective: We sought to monitor, in potentially sensitive human populations, the allergenicity effects of 5 GM materials obtained from sources with no allergenic potential and already under commercialization in the European Union. Methods: We have performed skin prick tests with protein extracts prepared from transgenic maize (MON810, Bt11, T25, Bt176) and soya (Roundup Ready) samples and from nontransgenic control samples in 2 sensitive groups: children with food and inhalant allergy and individuals with asthma-rhinitis. We have also tested IgE immunoblot reactivity of sera from patients with food allergy to soya (Roundup Ready) and maize (MON810, Bt11, Bt176) samples, as well as to the pure transgenic proteins (CryIA[b] and CP4 5-enolpyruvylshikimate-3-phosphate synthase). Results: None of the individuals undergoing tests reacted differentially to the transgenic and nontransgenic samples under study. None of the volunteers tested presented detectable IgE antibodies against pure transgenic proteins. Conclusion: The transgenic products under testing seem to be safe in terms of allergenic potential. We propose postmarket testing as an important screening strategy for putative allergic sensitization to proteins introduced in transgenic plants. [Copyright &y& Elsevier]

Background Recombinant human C1 inhibitor (rhC1INH) for on-demand treatment of hereditary angioedema is purified from milk of transgenic rabbits. It contains low amounts (<0.002%) of host-related impurities, which could trigger hypersensitivity reactions in patients with rabbit allergy (RA) and/or cow's milk allergy (CMA). Objective This study is an assessment of allergenicity and safety of rhC1INH in patients with RA and/or CMA. Methods Patients with CMA and/or RA underwent skin prick test (SPT), intracutaneous test (ICT), and, when results for both were negative, subcutaneous (SC) challenge with up to 2100U (14 mL) rhC1INH. The negative predictive value of the skin test protocol was calculated, defined as the ratio of patients without systemic symptoms of hypersensitivity following SC challenge, over the number of patients having tested negative for both the SPT and the ICT. Adverse events after exposure to rhC1INH were recorded. Results Twenty-six patients with RA and/or CMA were enrolled. Twenty-four had negative SPT and ICT results for rhC1INH, whereas 2 had negative SPT result but positive ICT result to rhC1INH (only the highest concentration). Twenty-two patients with negative SPT and ICT results underwent SC challenge. None developed allergic symptoms. Local treatment-emergent adverse events occurred in 7 patients (32%) after SC challenge. In 5 these were considered drug related. All were mild. Conclusions None of the patients with negative SPT and ICT results for rhC1INH had allergic symptoms during rhC1INH challenge. The negative predictive value of the combination of SPT and ICT for the outcome of the SC challenge was 100% (95% CI, 84.6%-100%). SC administration of rhC1INH was well tolerated. [ABSTRACT FROM AUTHOR]

Background: Several alternative mechanisms have been proposed to explain why some proteins are able to induce a TH2-biased and IgE-mediated immune response. These include specific interactions with receptors of the innate immune system, proteolytic activities, allergen-associated carbohydrate structures, and intrinsic structural determinants. Objectives: Available data suggest that a fold-dependent allergy-promoting mechanism could be a driving force for the TH2-polarization activity of Bet v 1, the major birch pollen allergen. Methods: Computer-aided sequence and fold analysis of the Bet v 1 family identified a short stretch susceptible for mutations inducing an altered fold of the entire molecule. With this knowledge, 7 consecutive amino acids of Bet v 1 were replaced with the homologous Mal d 1 sequence, creating the derivative BM4. Results: The minimal changes of the sequence led to a loss of the Bet v 1–like fold and influenced the immunologic behavior. Compared to wild-type Bet v 1, BM4 induced elevated T-cell proliferation of human PBMCs. In the mouse model, immunization with Bet v 1 absorbed to aluminum hydroxide triggered strong TH2 polarization, whereas BM4 immunization additionally recruited TH1 cells. Furthermore, the fold variant BM4 showed enhanced uptake by dendritic cells and a decreased susceptibility to endo-/lysosomal proteolysis. Conclusion: Modifications in the 3-dimensional structure of Bet v 1.0101 resulted in a change of its immunologic properties. We observed that the fold alteration led to a modified crosstalk with dendritic cells and a shift of the immune response polarization toward a mixed TH1/TH2 cytokine production. [ABSTRACT FROM AUTHOR]