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Biomedical subjects

A Curioni

Publications and source records attributed to A Curioni.

18 recordsLinked to original sources
PubMed2003

Oral allergy syndrome to fig.

BACKGROUND: The few cases of food allergy to fig reported to date, whose main manifestations were anaphylactic reactions, have been related to a cross-sensitisation to weeping fig (Ficus benjamina) or to the 'latex-fruit syndrome'. Here we report on two cases of the oral allergy syndrome (OAS) to fig in patients whose main allergic manifestations were related to sensitisation to grass and birch pollens. METHODS: The patients were characterised by clinical history, skin prick tests (SPT) with commercial and in-house extracts, prick-by-prick test, specific IgE measurements and challenge tests. PBS-soluble and insoluble extracts of both fig skin and pulp were examined for the presence of potential allergens by IgE immunoblotting. RESULTS: Both patients showed OAS followed by respiratory symptoms when challenged with fig. They were negative in both specific IgE detection and SPT with commercial extracts of fig and many other plant materials, including F. benjamina and Hevea Brasiliensis, while grass and birch pollens gave positive results. Prick-by-prick tests and SPT with in-house extracts indicated that the fig skin had a much higher allergenicity than the pulp. Despite negative IgE detection by the CAP assay, immunoblotting experiments showed that potential fig allergens were PBS-soluble and present only in the skin of the fruit. CONCLUSIONS: OAS to fig followed by respiratory symptoms can be present in patients not sensitised to weeping fig or having the latex-fruit syndrome. Different parts of the fig can have different allergenicities, the most important allergens being proteins related to the skin of the fruit. Improved commercial fig extracts to be used for the diagnosis of this type of allergy have to be developed.

Adult↗
PubMed2002

IgE-mediated allergy to corn: a 50 kDa protein, belonging to the Reduced Soluble Proteins, is a major allergen.

BACKGROUND: Although corn is often cited as an allergenic food, very few studies have been devoted to the identification of corn allergens and corn allergy has been rarely confirmed by double-blind, placebo-controlled food challenge (DBPCFC). Recently, Pastorello et al. (1) identified some salt-soluble IgE-binding proteins of corn flour as potential allergens. One of these, corresponding to corn Lipid Transfer Protein (LTP), appeared to be the major one. The aim of this study was to verify the clinical significance of the skin prick test (SPT) and CAP-FEIA CAP-System IgE fluozoenzyme immunosorbent assay (Pharmacia Diagnostic, Uppsala, Sweden) positivities to corn and to identify the presence of IgE-binding proteins in the corn flour salt-insoluble protein fractions (comprising up to 96% of the total protein) using sera of patients with DBPCFC-documented food allergy to corn. In addition the effect of cooking and proteolytic digestion on the corn allergens was investigated. METHODS: Sixteen subjects with SPT and CAP-FEIA positivities to corn flour were examined. Only six of them complained of suffering from urticaria and/or other symptoms after ingestion of corn-based foods. The patients were food challenged with cooked corn flour (polenta). IgE-binding proteins were detected by immunoblotting. The digestibility of the IgE-binding proteins was examined during a pepsin attack followed by a pancreatin digestion performed on a cooked corn flour sample. RESULTS: Oral challenge was positive only for six patients with symptoms after ingestion of corn. A 50 kDa protein, belonging to the corn Reduced Soluble Protein (RSP) fraction was recognized by the serum IgE of all the DBPCFC-positive subjects and resulted to be resistant to both heating and peptic/pancreatic digestion. SPT with the purified RSP fraction gave positive results for all of the DBPCFC-positive patients examined. CONCLUSIONS: SPT and CAP-FEIA positivities to corn flour had no clinical significance for most of the patients and food allergy to corn has to be proved by DBPCFC. A salt-unextractable protein of 50 kDa, belonging to the RSP fraction, represents a potential allergen in food hypersensitivity to corn because of its stability to cooking and digestion.

Allergens↗
PubMed2001

Detection of Saccharomyces cerevisiae carboxylesterase activity after native and sodium dodecyl sulfate electrophoresis by using fluorescein diacetate as substrate.

A simple method for the visualisation of wine yeast esterase (carboxylesterase EC 3.1.1.1) activity on electrophoretic gels was developed, using the fluorescent substrate fluorescein diacetate. The zymogram system allows a sensitive detection of esterase bands in only 5 min of incubation of both native and sodium dodecyl sulfate gels.

Carboxylesterase↗
PubMed2001

Modifications of wheat flour proteins during in vitro digestion of bread dough, crumb, and crust: an electrophoretic and immunological study.

The proteins of wheat flour have several biological activities that can affect human health and physiology when wheat-based foods are consumed. The modifications of bread crumb and crust proteins during an in vitro peptic/pancreatic digestion process were studied by electrophoresis and immunoblotting with polyclonal antibodies specific for single proteins or groups of homologous proteins of the wheat flour, and the results were compared to those obtained for an unheated dough sample. The results show that baking affects the extent of proteolysis and the immunological and physicochemical features of the digestion products in relation to the level of the heat treatment. Therefore, the results concerning the digestion of the unheated wheat flour or dough are not representative of what happens when baked products enter the human digestive tract.

Bread↗
PubMed2001

Food allergy to wheat products: the effect of bread baking and in vitro digestion on wheat allergenic proteins. A study with bread dough, crumb, and crust.

The effect of baking and digestion on the allergenicity of wheat flour proteins has been studied. Pooled sera of patients suffering from food allergy to wheat products were tested for IgE binding to the proteins of the wheat dough and of the bread crumb and crust, before and after being in vitro digested. During in vitro digestion, the IgE binding protein components of the unheated dough tended to disappear, whereas a permanence of IgE recognition was evident for both the bread crumb and crust. This indicates that the baking process increases the resistance of the potential allergens of the wheat flour to proteolytic digestion, allowing them to reach the gastrointestinal tract, where they can elicit the immunological response. Therefore, the effects of baking must be carefully considered in studying food allergies to wheat products.

Bread↗
PubMed2001

IgE binding to soluble and insoluble wheat flour proteins in atopic and non-atopic patients suffering from gastrointestinal symptoms after wheat ingestion.

BACKGROUND: The involvement of IgE-mediated hypersensitivity reactions in the genesis of gastrointestinal symptoms after ingestion of foods containing wheat has been rarely reported. OBJECTIVE: To detect IgE specifically binding to wheat proteins in the sera of atopic and non-atopic patients suffering from gastrointestinal symptoms after ingestion of wheat and to evaluate the reliability of skin prick test and CAP in the diagnosis of food allergy to wheat. METHODS: The sera of patients (10 atopic and 10 non-atopic) previously diagnosed as suffering from irritable bowel syndrome and complaining of symptoms after wheat ingestion were analysed by immunoblotting for IgE binding to water/salt-soluble and insoluble wheat flour proteins. RESULTS: All the atopic patients and only one of the non-atopic patients were positive to wheat CAP. For the patients tested, skin prick test was positive for all the atopic patients and for only one of the non-atopic patients. However, immunoblotting experiments showed the presence of specific IgE to wheat proteins in all the patients. Ten out of 11 of the wheat CAP-positive patients had IgE binding to a soluble 16-kDa band, but the same band was recognized, in a slighter way, by only two out of nine of the wheat CAP-negative patients. Moreover, although almost all of the patients were negative in CAP testing with gluten, 19 out of 20 recognized protein bands belonging to the prolamin fraction. CONCLUSIONS: For the atopic patients the positivity to skin prick test and CAP to wheat was in accordance with the immunoblotting results and a food allergy to wheat could be diagnosed. In these patients a major allergen was a 16-kDa band corresponding to members of the cereal alpha-amylase/trypsin inhibitors protein family, the major allergens involved in baker's asthma. In the non-atopic patients the positive immunoblotting results contrasted with the responses of the allergologic tests, indicating that the allergenic wheat protein preparations currently used are of limited value in detecting specific IgE to wheat and that the fraction of irritable bowel syndrome (IBS) patients with food allergy may be larger than believed.

Adult↗
PubMed2000

IgE binding to almond proteins in two CAP-FEIA-negative patients with allergic symptoms to almond as compared to three CAP-FEIA-false-positive subjects.

BACKGROUND: Allergy to almonds has been frequently reported, but data on the identification of the almond allergens, as well as on the reliability of the methods for in vitro detection of specific IgE for these allergens, are scant. This study aimed to identify the almond allergens and to evaluate the reliability of the CAP-FEIA as the standard system for detection of almond-specific IgE with clinical significance. METHODS: Immunoblotting performed with an almond-protein extract was carried out on the sera of five patients who had previously been tested by the CAP-FEIA system; two of these patients had tested negative with the CAP-FEIA system but suffered life-threatening laryngeal edema after eating almonds, whereas the other three subjects, who had tested positive with CAP-FEIA, did not present any symptoms subsequent to almond ingestion. RESULTS: The sera of the two symptomatic CAP-FEIA-negative patients had IgE that bound only to a 37-kDa protein in immunoblotting. On the contrary, the sera of the three asymptomatic subjects all showed IgE binding to two almond proteins of 62 and 50 kDa, corresponding to the glycosylated components of the extract. CONCLUSIONS: The results here presented suggest that, at least for the examined subjects, the positivity to almond, as measured with a standard laboratory method, is due to the presence of the 62/50-kDa glycoproteins with little or no immunologic significance, and not to the binding to the 37-kDa polypeptide, which appears to be a true almond allergen.

Adult↗
PubMed1999

Urticaria from beer: an immediate hypersensitivity reaction due to a 10-kDa protein derived from barley.

BACKGROUND: Urticaria from beer has been reported in atopic patients. In these subjects, the skin-prick test positivity to and presence of specific serum immunoglobulin (Ig)E for barley malt, the basic ingredient used in brewing, suggested a type I hypersensitivity to barley component(s). OBJECTIVE: To identify the beer allergen(s) and to investigate the presence of related proteins in barley. METHODS: Three patients with urticaria from beer and other atopic people, some of them suffering from baker's asthma, were examined for both prick test sensitivity to and the occurrence of serum-specific IgE for partially purified proteins from beer. Allergen identification in beer, malt and barley was performed by immunoblotting. RESULTS: Skin-prick tests and detection of specific IgE by both solid-phase (RAST) and liquid-phase (AlaSTAT) assays demonstrated that the 5-20-kDa beer protein fraction contained the allergen. Immunoblot analysis with sera of patients with urticaria from beer showed that IgE bound only the 10-kDa protein band in beer and malt, whereas a main 16-kDa protein was revealed in barley in addition to a very faint 10-kDa band. With the serum of a patient suffering from baker's asthma no IgE binding bands were observed in beer, whereas specific IgE binding to several proteins, including a major 16-kDa component, were detected for both malt and barley. CONCLUSIONS: Urticaria from beer is an IgE-mediated hypersensitivity reaction induced by a protein component of approximately 10 kDa deriving from barley. This allergen does not seem to be related to the major barley 16-kDa allergen responsible for baker's asthma. Because of the severity of the allergic manifestations to beer we recommend testing atopic patients positive to malt/barley and/or who exhibit urticarial reactions after drinking beer for their sensitivity to this beverage.

Adolescent↗
PubMed1998

The chemistry of water on alumina surfaces: reaction dynamics from first principles

Aluminas and their surface chemistry play a vital role in many areas of modern technology. The behavior of adsorbed water is particularly important and poorly understood. Simulations of hydrated alpha-alumina (0001) surfaces with ab initio molecular dynamics elucidate many aspects of this problem, especially the complex dynamics of water dissociation and related surface reactions. At low water coverage, free energy profiles established that molecularly adsorbed water is metastable and dissociates readily, even in the absence of defects, by a kinetically preferred pathway. Observations at higher water coverage revealed rapid dissociation and unanticipated collective effects, including water-catalyzed dissociation and proton transfer reactions between adsorbed water and hydroxide. The results provide a consistent interpretation of the measured coverage dependence of water heats of adsorption, hydroxyl vibrational spectra, and other experiments.

Journal Article↗
PubMed1996

In vitro assessment of acetic-acid-soluble proteins (glutenin) toxicity in celiac disease.

Acetic-acid-soluble storage proteins from gluten of the bread wheat cv. Sprint 3 were fractionated by adsorption chromatography on 2000 A controlled-pore glass (CPG) beads, and glutenin polymers with molecular mass higher than 10(7) Da and free from monomeric gliadins were recovered. The glutenin polymers were found to consist of high-molecular-weight (HMW) and low-molecular-weight (LMW) glutenin subunits. Peptic-tryptic (PT) digests of glutenins were examined for their agglutination activity on human myelogenous leukemia K 562(S) cells, agglutination being strongly correlated with toxicity for the celiac intestine. The peptide fraction at a concentration of 1 g/L of culture medium was able to agglutinate 30% of K 562(S) cells, suggesting a moderate toxic effect. This toxicity may be accounted for by homologies in amino acid sequences between glutenin subunits and alpha/beta- and gamma-gliadins.

Acetic Acid↗
PubMed1995

Purification of wheat glutenin subunits by preparative acid and two-dimensional electrophoresis.

Reduced alkylated glutenin subunits from wheat flour were fractionated by preparative electrophoresis at acid pH. The high molecular weight glutenin subunits (HMW-GS) and some of the low molecular weight glutenin subunits (LMW-GS) were purified by this one-step procedure, whereas the remainder of the LMW-GS, comigrating in the acid system, were purified in a second step by electroendosmotic preparative electrophoresis in the presence of sodium dodecyl sulfate. The quantities of recovered protein were sufficient for biochemical characterization and/or antibody production.

Acetates↗
PubMed1990

Preparative isoelectric focusing of reduced wheat gluten proteins.

Proteins extracted from gluten of the bread wheat cultivar Fiorello 2 in the presence of 2-mercaptoethanol or dithiothreitol were separated by isoelectric focusing in a free solution in a pH 3-10 gradient containing 50% v/v 1-propanol or urea. The collected fractions were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis in 10% gels (high and medium molecular weight glutenin subunits) and 16% gels (low molecular weight gliadins). The isoelectric focusing pattern of gluten polypeptides in 50% v/v 1-propanol was comparable to that obtained on two-dimensional gel electrophoresis, based on isoelectric focusing and polyacrylamide gel electrophoresis or nonequilibrium pH gradient electrophoresis and polyacrylamide gel electrophoresis. A similar isoelectric focusing pattern was also observed when 3M urea was used as solvent. New gluten polypeptides, similar in mobility to the high molecular weight subunits of glutenin were detected at acidic pH.

1-Propanol↗
PubMed1988

Purification of cellulases from Streptomyces strain A20 by electroendosmotic preparative electrophoresis.

Five cellulase components were identified and purified in one step from Streptomyces strain A20 using electroendosmotic preparative electrophoresis. By this procedure up to 18 mg of protein mixture could be loaded on the column, with an estimated recovery of 60-70% of total activity; activity and protein recovery could be estimated 32% and 47% respectively, if only activity peaks were considered. In comparison to other purification methods, this technique results in high protein recovery and resolution of applied samples.

Bacterial Proteins↗
PubMedDate not supplied

New scoring functions for virtual screening from molecular dynamics simulations with a quantum-refined force-field (QRFF-MD). Application to cyclin-dependent kinase 2.

A recently introduced new methodology based on ultrashort (50-100 ps) molecular dynamics simulations with a quantum-refined force-field (QRFF-MD) is here evaluated in its ability both to predict protein-ligand binding affinities and to discriminate active compounds from inactive ones. Physically based scoring functions are derived from this approach, and their performance is compared to that of several standard knowledge-based scoring functions. About 40 inhibitors of cyclin-dependent kinase 2 (CDK2) representing a broad chemical diversity were considered. The QRFF-MD method achieves a correlation coefficient, R(2), of 0.55, which is significantly better than that obtained by a number of traditional approaches in virtual screening but only slightly better than that obtained by consensus scoring (R(2) = 0.50). Compounds from the Available Chemical Directory, along with the known active compounds, were docked into the ATP binding site of CDK2 using the program Glide, and the 650 ligands from the top scored poses were considered for a QRFF-MD analysis. Combined with structural information extracted from the simulations, the QRFF-MD methodology results in similar enrichment of known actives compared to consensus scoring. Moreover, a new scoring function is introduced that combines a QRFF-MD based scoring function with consensus scoring, which results in substantial improvement on the enrichment profile.

Computer Simulation↗