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The most comprehensive exhibition catalog dedicated to the work of Brazilian artist Tarsila do Amaral (1886-1973), a pioneering figure in Latin American modernism. The focus of the exhibition is the popular, or the vernacular, a notion as complex in Brazil as it is contested, and which Tarsila explored in different ways throughout her career. The popular is associated with debates on national art or identity and the invention or construction of brasilidade, Brazilianness. In Tarsila, the popular is manifested in landscapes of the countryside or the suburbs, the farm or the favela, populated by people of indigenous or African descent, characters from Brazilian folklore, full of animals and plants, both real and fantastic. But Tarsila's palette (which served as inspiration for the colors of the exhibition design) is also popular: \"pure blue, violaceous rose, bright yellow, singing green.\" Much of the art criticism on Tarsila to this day in Brazil has emphasized her French affiliations and genealogies, possibly in search of the artist's international legitimization, but thus marginalizing the themes, characters, and popular narratives that she constructed. Today, after successful shows in the United States and Europe, we can look at Tarsila in other ways. In this sense, the essays and commentaries on her works included in the exhibition and in the catalog are central elements of this project. It is not by chance that the controversial painting A Negra [The Negress] has received special attention from the authors and is a central work in the exhibition. Tarsila do Amaral: Cannibalizing Modernism does not seek to exhaust all these discussions, which take into account questions of race, class and colonialism. But the project does point to the need to study this artist, so fundamental in our art history, from new perspectives and approaches. This exhibition is part of a series that MASP has organized reassessing the notion of the popular in Brazil: from A mنao do povo brasileiro, 1969/2016 [The Hand of the Brazilian People, 1969/2016] and Portinari popular [Popular Portinari] in 2016 to Agostinho Batista de Freitas in 2017 and Maria Auxiliadora in 2018. Tarsila do Amaral: Cannibalizing Modernism is contextualized in a full year dedicated to women artists at the museum in 2019 under the heading Women's Histories, Feminist Histories. The exhibition dialogues with two others dedicated to artists who explored the notion of the popular through different approaches: Djanira: Picturing Brazil, on view through May 19th, and Lina Bo Bardi: Habitat, on view through July 28th.

The detection of molecules belonging to the pathogenesis-related protein-4 (PR-4) family as a cause of allergic reactions towards the pomegranate fruit has already been suggested, although information regarding their isolation and characterization is not available in the literature. The objective of this study was the purification and description of some features of a pomegranate PR-4 protein. This protein, named punein, was purified by classical biochemical methods, identified by direct protein sequencing and mass spectrometry and analyzed by bioinformatic tools. Biochemical characterization shows that punein has a molecular mass of 13.29 kDa by mass spectrometry and about 14 kDa on SDS-PAGE, and it displays a blocked N-terminus. Bioinformatic analysis highlights that its primary structure shows similarity with the allergens prohevein (containing the strong allergen Hev b 6) and Bra r 2, from latex and turnip, respectively. In particular, punein could be aligned with the C-terminal region of prohevein, which shows IgE epitope regions, the amino acid sequences of which are partially conserved in the two molecules. However, further investigations are needed to understand the clinical relevance of this PR-4 food protein and the factors affecting the concentration of specific proteins, including punein, that are recognized by the immune systems of patients sensitized to pomegranate.

Vegetables represent a major source of Ni exposure. Environmental contamination and cultural practices can increase Ni amount in tomato posing significant risk for human health. This work assesses the tomato ( Solanum lycopersicum L.) response to Ni on the agronomic yield of fruits and the related production of allergens. Two cultivars were grown in pots amended with Ni 0, 30, 60, 120, and 300 mg kg −1 , respectively. XRF and ICP-MS analyses highlighted the direct increase of fruit Ni content compared to soil Ni, maintaining a stable biomass. Leaf water content increased at Ni 300 mg kg −1 . Total protein content and individual allergenic components were investigated using biochemical (RP-HPLC and N-terminal amino acid sequencing) and immunological (inhibition tests of IgE binding by SPHIAa assay on the FABER testing system) methodologies. Ni affected the fruit tissue concentration of pathogenesis-related proteins and relevant allergens (LTP, profilin, Bet v 1-like protein and TLP). This study elucidates for the first time that tomato reacts to exogenous Ni, uptaking the metal while changing its allergenic profiles, with potential double increasing of exposure risks for consumers. This evidence highlighted the importance of adequate choice of low-Ni tomato cultivars and practices to reduce Ni uptake by potentially contaminated matrices.

Background: IgE to cross-reacting carbohydrate determinants has already been described by several authors, but their function and distribution are still a matter of debate. In previous studies we showed how the presence of IgE to bromelain could be a useful and simple marker of the presence of IgE to carbohydrate epitopes. Methods: A survey of 1,831 subjects with a suspected allergic respiratory disease has been carried out by detecting IgE to bromelain. Data were analysed on the basis of demographical and allergological parameters. To find out whether a glycoprotein is capable of triggering an allergic reaction, 1,076 subjects were also skin tested with several purified molecules bearing carbohydrate side chains differing in number, composition and complexity. Results: An overall prevalence of 23% of positive IgE to cross-reacting carbohydrate determinants was recorded. Prevalence varied when subsets of non-allergic (5%), non-pollen-allergic (10%), and pollen-allergic (31%) subjects were considered. Prevalence further increased in subsets with multiple pollen sensitization (71%), and with a previous pollen immunotherapy course (46%), whereas minor differences were found in gender and age distribution. Almost all the allergenic extracts recorded negative in the skin test gave a positive IgE test in vitro. A higher correlation was found mainly with plant-derived allergenic extracts, whereas a lower one was recorded with mites and fungi. Horseradish peroxidase was the only glycoprotein capable of exerting a positive skin test in 21% of the subjects with IgE to cross-reacting carbohydrate determinants, 80% of them having IgE to the HRP molecule. Conclusions: IgE to cross-reacting carbohydrate determinants are common among the allergic population and the binding to skin test negative allergenic extracts further confirms their poor biological activity. Further studies on horseradish peroxidase should be carried out to define the role of the glycan side chains in its allergenic activity.

Nonspecific lipid transfer proteins (LTPs) are important allergens in fruits, vegetables, nuts, pollen, and latex. Despite their wide distribution throughout the plant kingdom, their clinical relevance is largely confined to the Mediterranean area. As they can sensitize via the gastrointestinal tract, LPTs are considered true food allergens, and IgE reactivity to LTPs is often associated with severe systemic symptoms. Although Pru p 3 represents the predominant LTP in terms of patients’ IgE recognition, the contribution of pollen LTPs in primary sensitization cannot be ruled out. Due to structural homology, LTPs from different allergen sources are generally IgE cross-reactive. However, sensitization profiles among allergic patients are extremely heterogeneous, and individual cross-reactivity patterns can be restricted to a single LTP or encompass many different LTPs. Molecule-based approaches in allergy research and diagnosis are important for better understanding of LTP allergy and could assist clinicians with providing adequate patient-tailored advice.

Several factors can affect the allergen content and profile of a specific food, including processing procedures often leading to a decrease in allergenicity, although no change, or even an increase, have also been reported. Evaluation of the effectiveness of a processing procedure requires the availability of reliable methodologies to assess the variation in molecules able to induce allergic reactions in the analyzed food. Conventional and innovative strategies and methodologies can be exploited to identify allergenic proteins in foodstuffs. However, depending on the specific purposes, different methods can be used. In this review, we have critically reviewed the advantages of an innovative method, the multiplex allergen microarray-based immunoassay, in the detection of allergens in foodstuffs. In particular, we have analyzed some studies reporting the exploitation of an IgE-binding inhibition assay on multiplex allergen biochips, which has not yet been reviewed in the available literature. Unlike the others, this methodology enables the identification of many allergenic proteins, some of which are still unknown, which are recognized by IgE from allergic patients, with a single test. The examined literature suggests that the inhibition test associated with the multiplex allergen immunoassay is a promising methodology exploitable for the detection of IgE-binding proteins in food samples.

Background: Diagnosis and immunotherapy of house-dust mite (HDM) allergy is still based on natural allergen extracts. The aim of this study was to analyze commercially available Dermatophagoides pteronyssinus extracts from different manufacturers regarding allergen composition and content and whether variations may affect their allergenic activity. Methods: Antibodies specific for several D. pteronyssinus allergens (Der p 1, 2, 5, 7, 10 and 21) were used to analyze extracts from 10 different manufacturers by immunoblotting. Sandwich ELISAs were used to quantify Der p 1 and Der p 2 in the extracts. Mite-allergic patients (n = 45) were skin-tested with the extracts and tested for immunoglobulin E (IgE) reactivity to a panel of 10 mite allergens (Der p 1, 2, 4, 5, 7, 8, 10, 14, 20 and 21) by dot blot. Results: Only Der p 1 and Der p 2 were detected in all extracts but their concentrations and ratios showed high variability (Der p 1: 6.0–40.8 µg ml –1 ; Der p 2: 1.7–45.0 µg ml –1 ). At least 1 out of 4 allergens (i.e. Der p 5, 7, 10 and 21) was not detected in 8 of the studied extracts. Mite-allergic subjects showed different IgE reactivity profiles to the individual mite allergens, the extracts showed different allergenic activity in skin-prick tests and false-negative results. Conclusions: Commercially available D. pteronyssinus extracts lack important allergens, show great variability regarding allergen composition and content and some gave false-negative diagnostic test results in certain patients.

The weed wall pellitory, Parietaria judaica , is one the most important pollen allergen sources in the Mediterranean area causing severe symptoms of hay fever and asthma in allergic patients. We report the expression of the major Parietaria allergens, Par j 1 and Par j 2 which belong to the family of lipid transfer proteins, in insect cells. According to circular dichroism analysis and gel filtration, the purified allergens represented folded and monomeric proteins. Insect cell-expressed, folded Par j 2 exhibited higher IgE binding capacity and more than 100-fold higher allergenic activity than unfolded Escherichia coli -expressed Par j 2 as demonstrated by IgE ELISA and basophil activation testing. IgE ELISA inhibition assays showed that Par j 1 and Par j 2, contain genuine and cross-reactive IgE epitopes. IgG antibodies induced by immunization with Par j 2 inhibited binding of allergic patients IgE to Par j 1 only partially. IgE inhibition experiments demonstrated that insect cell-expressed Par j 1 and Par j 2 together resembled the majority of allergenic epitopes of the Parietaria allergome and therefore both should be used for molecular diagnosis and the design of vaccines for allergen-specific immunotherapy of Parietaria allergy.

Oral allergy syndrome (OAS) is one of the most common IgE-mediated allergic reactions. It is characterized by a number of symptoms induced by the exposure of the oral and pharyngeal mucosa to allergenic proteins belonging to class 1 or to class 2 food allergens. OAS occurring when patients sensitized to pollens are exposed to some fresh plant foods has been called pollen food allergy syndrome (PFAS). In the wake of PFAS, several different associations of allergenic sources have been progressively proposed and called syndromes. Molecular allergology has shown that these associations are based on IgE co-recognition taking place between homologous allergens present in different allergenic sources. In addition, the molecular approach reveals that some allergens involved in OAS are also responsible for systemic reactions, as in the case of some food Bet v 1-related proteins, lipid transfer proteins and gibberellin regulated proteins. Therefore, in the presence of a convincing history of OAS, it becomes crucial to perform a patient’s tailored molecule-based diagnosis in order to identify the individual IgE sensitization profile. This information allows the prediction of possible cross-reactions with homologous molecules contained in other sources. In addition, it allows the assessment of the risk of developing more severe symptoms on the basis of the features of the allergenic proteins to which the patient is sensitized. In this context, we aimed to provide an overview of the features of relevant plant allergenic molecules and their involvement in the clinical onset of OAS. The value of a personalized molecule-based approach to OAS diagnosis is also analyzed and discussed.

Papain-like cysteine proteases are widespread and can be detected in all domains of life. They share structural and enzymatic properties with the group’s namesake member, papain. They show a broad range of protein substrates and are involved in several biological processes. These proteases are widely exploited for food, pharmaceutical, chemical and cosmetic biotechnological applications. However, some of them are known to cause allergic reactions. In this context, the objective of this review is to report an overview of some general properties of papain-like cysteine proteases and to highlight their contributions to allergy reactions observed in humans. For instance, the literature shows that their proteolytic activity can cause an increase in tissue permeability, which favours the crossing of allergens through the skin, intestinal and respiratory barriers. The observation that allergy to PLCPs is mostly detected for inhaled proteins is in line with the reports describing mite homologs, such as Der p 1 and Der f 1, as major allergens showing a frequent correlation between sensitisation and clinical allergic reactions. In contrast, the plant food homologs are often digested in the gastrointestinal tract. Therefore, they only rarely can cause allergic reactions in humans. Accordingly, they are reported mainly as a cause of occupational diseases.