35 results on '"Primavesi L"'
Search Results
2. Contributors
- Author
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Abe, C., primary, Accardi, G., additional, Andres-Lacueva, C., additional, Appendino, G., additional, Armentia, A., additional, Arora, R., additional, Azevedo, V., additional, Badole, S.L., additional, Bae, S.-C., additional, Baliga, M.S., additional, Balistreri, C.R., additional, Bermúdez-Humarán, L.G., additional, Bhat, H., additional, Bodhankar, S.L., additional, Bolling, S.F., additional, Bollor, R., additional, Bowden, R.G., additional, Bravo-Clouzet, R., additional, Calder, P.C., additional, Câmara, N.O.S., additional, Candore, G., additional, Castell, M., additional, Castellote, C., additional, Castrodeza, J., additional, Cerón, J.M., additional, Chacko, J., additional, Chowdhury, Z.T., additional, Comalada, M., additional, Contreras-Moreno, J., additional, Cordova, F.M., additional, Correa-Matos, N.J., additional, Crespo, J., additional, de Cienfuegos, G.Á., additional, de Gaetano, G., additional, de Luis, D., additional, de Moreno de LeBlanc, A., additional, de Pablo, M.A., additional, de Roos, B., additional, del Carmen, S., additional, Díaz, L.E., additional, di Giuseppe, R., additional, Donati, M.B., additional, Egger, G., additional, Elias, R.M., additional, Fayad, R., additional, Fazal, F., additional, Feleszko, W., additional, Fischer, A.K., additional, Franch, À., additional, Galena, A.E., additional, Gálvez, J., additional, Gómez-Martínez, S., additional, Graziano, C., additional, Hall, J., additional, Haniadka, R., additional, Hurst, R.D., additional, Hurst, S.M., additional, Iacoviello, L., additional, Inglada, L., additional, Jaffe, R., additional, Jaworska, J., additional, Kaufman, P.B., additional, Khan, N., additional, Kirakosyan, A., additional, Langella, P., additional, Latheef, L., additional, LeBlanc, J.G., additional, Llorach, R., additional, Lucas, E.A., additional, Malhotra, P., additional, Marcos, A., additional, Marín-Casino, M., additional, Martín-Armentia, S., additional, Mateu-de Antonio, J., additional, Menaa, A., additional, Menaa, B., additional, Menaa, F., additional, Mes, J., additional, Minato, K.I., additional, Miyoshi, A., additional, Monagas, M., additional, Moreillon, J., additional, Mullin, G.E., additional, Neyestani, T.R., additional, Oommen, B., additional, Pai, C., additional, Pai, R.J., additional, Pérez-Berezo, T., additional, Pérez-Cano, F.J., additional, Pérez de Heredia, F., additional, Petro, T.M., additional, Pozo-Rubio, T., additional, Prabhala, H.K., additional, Prabhala, R.H., additional, Pravettoni, V., additional, Prescott, S.L., additional, Primavesi, L., additional, Puertollano, E., additional, Puertollano, M.A., additional, Ramos-Romero, S., additional, Rastmanesh, R., additional, Rendina, E., additional, Romeo, J., additional, Sabetisoofyani, A., additional, Sampath, P., additional, Schauss, A.G., additional, Seymour, E.M., additional, Sharma, A., additional, Shelmadine, B., additional, Smith, B.J., additional, Somasundaram, S.G., additional, Sung, M.-K., additional, Togni, S., additional, Urpi-sarda, M., additional, Vaghefi, S.B., additional, Watson, R.R., additional, Weber, C.E., additional, West, C.E., additional, Wichers, H., additional, Wood, L.G., additional, Xaus, J., additional, Yashawanth, H.S., additional, and Zibadi, S., additional
- Published
- 2013
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3. Die Bestimmung der Tropfengrößen in künstlichen Nebeln
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Gessner, H. and Primavesi, L.
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- 1962
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4. Characterization of hte T-cell epitopes of the major peach allergen pru p 3
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Pastorello E.A., Monza M., Prevettoni V., Longhi R., Bonara P., Scibilia J., Primavesi L., and Scorza R.
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- 2010
5. Green bean (Phaseolus vulgaris): a new source of IgE-binding lipid transfer protein
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Pastorello E.A., Pravettoni V., Farioli L., Primavesi L., Scibilia J., Piantanida M., Mascheri A., and Conti A.
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- 2010
6. Metodo per la preparazione di derivati ipoallergenici di frutta e/o ortaggi in pezzi
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Pompei, C., Brenna, O.V., and Primavesi, L.
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Settore AGR/15 - Scienze e Tecnologie Alimentari - Published
- 2007
7. Arabidopsis sucrose non-fermenting-1-related protein kinase-1 and calcium-dependent protein kinase phosphorylate conserved target sites in ABA response element binding proteins
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Zhang, Y., Andralojc, P. J., Hey, S. J., Primavesi, L. F., Specht, M., Koehler, J., Parry, M. A J, Halford, N. G., Zhang, Y., Andralojc, P. J., Hey, S. J., Primavesi, L. F., Specht, M., Koehler, J., Parry, M. A J, and Halford, N. G.
- Abstract
Evidence is provided that plant transcription factors of the ABA response element binding protein (AREBP) class are phosphorylated by sucrose non-fermenting-1-related protein kinase-1 (SnRK1) and a calcium-dependent protein kinase at highly conserved target sites. Two target sites for SnRK1 were identified in AREBPs using a specially developed motif search pipeline. Peptides containing the AREBP sites were phosphorylated by purified SnRK1 in vitro and by calcium-dependent and calcium-independent activities present in soluble protein extracted from Arabidopsis seedlings grown in liquid culture. Most (69-77%) of the calcium-independent phosphorylation of these peptides was removed by immunoprecipitation using anti-SnRK1 antisera, linking this activity unambiguously to SnRK1. It is possible that the protein kinase responsible for the calcium-dependent activity was SnRK3, a protein kinase that is related to SnRK1 and which has similar requirements for target site recognition. However, the involvement of other calcium-dependent protein kinases cannot be ruled out.
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- 2008
8. Characterization of the T-Cell Epitopes of the Major Peach Allergen Pru p 3
- Author
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Pastorello, E.A., primary, Monza, M., additional, Pravettoni, V., additional, Longhi, R., additional, Bonara, P., additional, Scibilia, J., additional, Primavesi, L., additional, and Scorza, R., additional
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- 2010
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9. Integration of leaf metabolism and physiology by the trehalose pathway
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Paul, M., primary, Jhurreea, D., additional, Primavesi, L., additional, Zhang, Y., additional, Sivagnanam, T., additional, and Wingler, A., additional
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- 2008
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10. Cherry Allergy: How To Decrease The Allergenicity Of Cherry Industrial Derivatives
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Pravettoni, V., primary, Brenna, O., additional, Farioli, L., additional, Primavesi, L., additional, Bonomi, S., additional, Tonoli, S., additional, Pompei, C., additional, and Pastorello, E., additional
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- 2007
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11. Influence of Cultivar and Processing on Cherry (Prunus avium) Allergenicity
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Primavesi, L., primary, Brenna, O. V., additional, Pompei, C., additional, Pravettoni, V., additional, Farioli, L., additional, and Pastorello, E. A., additional
- Published
- 2006
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12. Isolation and characterization of behavioural mutants and genes of Agrobacterium tumefaciens
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Shaw, C. H., primary, Loake, G. J., additional, Brown, A. P., additional, Garrett, C. S., additional, Deakin, W., additional, Alton, G., additional, Hall, M., additional, Jones, S. A., additional, O'Leary, M., additional, and Primavesi, L., additional
- Published
- 1991
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13. Functional and rheological characteristics of fresh egg pasta
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CRISTINA ALAMPRESE, ERNESTINA CASIRAGHI, Primavesi, L., Rossi, M., and Alyssa Hidalgo
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Cooking behaviour ,Egg ,Fresh pasta ,Furosine ,Pasteurisation ,Rheology ,Settore AGR/15 - Scienze e Tecnologie Alimentari
14. Tomato hypersensitivity in peach allergic patients: rPru p3 and rPru p1 positivity is predictive of the symptom severity
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Piantanida Marta, Farioli Larua, Scibilia Joseph, Mascheri Ambra, Pravettoni Valerio, Primavesi Laura, Nichelatti Michele, Marocchi Alessandro, Schroeder Jan, Stafylaraki Chrysi, and Pastorello Elide
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Immunologic diseases. Allergy ,RC581-607 - Published
- 2011
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15. Tmoato industrial derivatives: mallardo reaction and residual allergenicity
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Pravettoni Valerio, Primavesi Laura, Piantanida Marta, Brenna Oreste V, Farioli Larua, Scibilia Joseph, Mascheri Ambra, and Pastorello Elide
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Immunologic diseases. Allergy ,RC581-607 - Published
- 2011
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16. Hypersensitivity to fennel is frequent in peach allergic patients and LTP is a major fennel allergen
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Stafylaraki Chrysi, Farioli Laura, Scibilia Joseph, Giuffrida Maria, Mascheri Ambra, Pravettoni Valerio, Baro C, Piantanida Marta, Primavesi Laura, Nichelatti Michele, Marocchi Alessandro, Schroeder Jan, and Pastorello Elide
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Immunologic diseases. Allergy ,RC581-607 - Published
- 2011
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17. Severe allergic symptoms to peach are a risk factor for severe symptoms to other plant food allergens
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Mascheri Ambra, Scibilia Joseph, Farioli Laura, Stafylaraki Chrysi, Pravettoni Valerio, Piantanida Marta, Primavesi Laura, Mirone Corrado, Nichelatti Michele, Marocchi Alessandro, and Pastorello Elide
- Subjects
Immunologic diseases. Allergy ,RC581-607 - Published
- 2011
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18. FUNCTIONAL AND RHEOLOGICAL CHARACTERISTICS OF FRESH EGG PASTA.
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Alamprese, C., Casiraghi, E., Primavesi, L., Rossi, M., and Hidalgo, A.
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PASTA products , *EGGS as food , *PASTA , *FOOD industry , *FOOD science , *COOKING - Abstract
The composition, colour, cooking behaviour and rheological properties of different samples of industrial packaged and retail-manufactured fresh egg pasta were evaluated. All of the parameters showed high variability, due to differences in product formulation and technology. Retail-manufactured pastas were clearly distinguished from packaged samples due to the absence of pasteurisation. Pasteurisation caused raw pasta to become tougher and harder, while its break strain and matter loss in cooking water decreased. Principal Component Analysis separated the pasta samples into three groups, according to the severity of the thermal treatment applied. It was observed that cooking caused an overall reduction in the variability of the rheological characteristics, making retail-manufactured and packaged pastas more similar to one another. [ABSTRACT FROM AUTHOR]
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- 2005
19. Determinants of venom-specific IgE antibody concentration during long-term wasp venom immunotherapy.
- Author
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Pravettoni V, Piantanida M, Primavesi L, Forti S, and Pastorello EA
- Abstract
Background: Venom immunotherapy (VIT) is an effective treatment for subjects with systemic allergic reactions (SR) to Hymenoptera stings, however there are few studies concerning the relevance of the venom specific IgE changes to decide about VIT cessation. We assessed IgE changes during a 5-year VIT, in patients stung and protected within the first 3 years (SP 0-3) or in the last 2 years (SP 3-5), and in patients not stung (NoS), to evaluate possible correlations between IgE changes and clinical protection., Methods: Yellow jacket venom (YJV)-allergic patients who completed 5 years of VIT were retrospectively evaluated. Baseline IgE levels and after the 3rd and the 5th year of VIT were determined; all patients were asked about field stings and SRs., Results: A total of 232 YJV-allergic patients were included and divided into the following groups: 84 NoS, 72 SP 0-3 and 76 SP 3-5. IgE levels decreased during VIT compared to baseline values (χ(2) = 346.029, p < 0.001). Recent vespid stings accounted for significantly higher IgE levels despite clinical protection. IgE levels after 5 years of VIT correlated significantly with Mueller grade (F = 2.778, p = 0.012) and age (F = 6.672, p = 0.002). During follow-up from 1 to 10 years after VIT discontinuation, 35.2 % of the contacted patients reported at least one field sting without SR., Conclusions: The yellow jacket-VIT temporal stopping criterion of 5 years duration did not result in undetectable IgE levels, despite a long-lasting protection. A mean IgE decrease from 58 to 70 % was observed, and it was less marked in elderly patients or in subjects with higher Mueller grade SR.
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- 2015
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20. Nutrieconomic model can facilitate healthy and low-cost food choices.
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Primavesi L, Caccavelli G, Ciliberto A, and Pauze E
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- Adult, Computer Simulation, Cost Savings, Costs and Cost Analysis, Databases, Factual, Diet adverse effects, Humans, Italy, Nutritive Value, Seasons, Diet economics, Food Supply economics, Models, Economic, Nutrition Policy
- Abstract
Objective: Promotion of healthy eating can no longer be postponed as a priority, given the alarming growth rate of chronic degenerative diseases in Western countries. We elaborated a nutrieconomic model to assess and identify the most nutritious and affordable food choices., Design: Seventy-one food items representing the main food categories were included and their nationally representative prices monitored. Food composition was determined using CRA-NUT (Centro di Ricerca per gli Alimenti e la Nutrizione) and IEO (Istituto Europeo di Oncologia) databases. To define food nutritional quality, the mean adequacy ratio and mean excess ratio were combined. Both prices and nutritional quality were normalised for the edible food content and for the recommended serving sizes for the Italian adult population., Setting: Stores located in different provinces throughout Italy., Subjects: Not applicable., Results: Cereals and legumes presented very similar nutritional qualities and prices per serving. Seasonal fruits and vegetables presented differentiated nutritional qualities and almost equal prices. Products of animal origin showed similar nutritional qualities and varied prices: the best nutrieconomic choices were milk, oily fish and poultry for the dairy products, fish and meat groups, respectively., Conclusions: Analysing two balanced weekly menus, our nutrieconomic model was able to note a significant decrease in cost of approximately 30 % by varying animal-protein sources without affecting nutritional quality. Healthy eating does not necessarily imply spending large amounts of money but rather being able to make nutritionally optimal choices. The nutrieconomic model is an innovative and practical way to help consumers make correct food choices and nutritionists increase the compliance of their patients.
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- 2015
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21. Shiitake mushroom (Lentinus edodes): a poorly known allergen in Western countries responsible for severe work-related asthma.
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Pravettoni V, Primavesi L, and Piantanida M
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- Adult, Asthma, Occupational drug therapy, Electrophoresis, Polyacrylamide Gel, Female, Glucocorticoids therapeutic use, Humans, Immunoglobulin E immunology, Italy, Respiratory Function Tests, Skin Tests, Allergens immunology, Asthma, Occupational etiology, Asthma, Occupational immunology, Shiitake Mushrooms immunology
- Abstract
Objectives: The aim of this study was to investigate the IgE-mediated pathogenesis of severe asthma presented by a patient only after handling shiitake (Lentinus edodes) mushrooms (SM)., Material and Methods: Skin tests were performed using in-house extracts from mushrooms that the patient usually handled, i.e., shiitake, porcini, oyster and black fungus mushroom varieties. Specific IgE to champignons and various molds were determined. Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) immunoblotting was performed to detect IgE-binding components. Four negative controls were included in the study., Results: Skin prick tests performed with in-house mushroom extracts from varieties other than shiitake were completely negative, in contrast to the positive test obtained for shiitake mushrooms. Serum specific IgE levels for common molds and champignons were all negative. SDS-PAGE revealed many protein bands in the four mushroom extracts. Immunoblotting using the patient's serum showed allergenic bands at about 15 and 24 kDa exclusively for SM that were not shared with negative controls. Another faint band was detectable at approximately 37 kDa for SM and porcini varieties., Conclusions: Here, we present the first European case of SM-induced occupational asthma, a disease more frequently occurring in Asia. Asthma attacks stopped when the patient avoided contact with shiitake mushrooms. No skin reactions and no IgE-binding proteins by immunoblotting were detectable with the other mushrooms tested. The positive skin test with shiitake mushrooms and IgE-binding components in the shiitake extract confirmed the IgE-mediated etiology of the reaction.
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- 2014
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22. Basal platelet-activating factor acetylhydrolase: prognostic marker of severe Hymenoptera venom anaphylaxis.
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Pravettoni V, Piantanida M, Primavesi L, Forti S, and Pastorello EA
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- Animals, Biomarkers metabolism, Humans, Prognosis, 1-Alkyl-2-acetylglycerophosphocholine Esterase metabolism, Allergens immunology, Anaphylaxis diagnosis, Anaphylaxis enzymology, Arthropod Venoms adverse effects, Hymenoptera immunology
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- 2014
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23. Fennel allergy is a lipid-transfer protein (LTP)-related food hypersensitivity associated with peach allergy.
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Pastorello EA, Farioli L, Stafylaraki C, Scibilia J, Giuffrida MG, Mascheri A, Piantanida M, Baro C, Primavesi L, Nichelatti M, Schroeder JW, and Pravettoni V
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- Adolescent, Adult, Aged, Allergens immunology, Antigens, Plant immunology, Cross Reactions, Female, Humans, Immunoblotting, Immunoglobulin E blood, Male, Middle Aged, Young Adult, Carrier Proteins immunology, Foeniculum chemistry, Food Hypersensitivity diagnosis, Food Hypersensitivity immunology, Prunus chemistry
- Abstract
Fennel allergy has been rarely reported, and the association with peach allergy has never been described. Our aim was to (i) study the correlation between symptom severity of peach and fennel and (ii) identify fennel allergens and the role of rPru p 3 antibodies in severe reactions to fennel. In 148 patients with peach allergy, we investigated 58 patients with symptoms and IgE antibodies positive to fennel. IgE to rPru p 1, 3, and 4 and rBet v 1, 2, and 4 were measured by immunoblotting, and the N-terminal amino acid sequences and relevant allergens were determined. We found significant association between severe reactions to fennel and peach (p = 0.0009). A major allergen was ~9 kDa lipid-transfer protein (LTP), cross-reactive with Pru p 3, a 15 kDa protein identified as a pathogenesis-related protein 1 of the Bet v 1 family. In conclusion, peach and fennel severe allergic symptoms are significantly related, and LTP is a major fennel allergen. Fennel should be included in the LTP syndrome.
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- 2013
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24. Rice allergy demonstrated by double-blind placebo-controlled food challenge in peach-allergic patients is related to lipid transfer protein reactivity.
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Pastorello EA, Scibilia J, Farioli L, Primavesi L, Giuffrida MG, Mascheri A, Piantanida M, Mirone C, Stafylaraki C, Violetta MR, Nichelatti M, Preziosi D, Losappio L, and Pravettoni V
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- Adult, Carrier Proteins chemistry, Carrier Proteins genetics, Chromatography, High Pressure Liquid, Double-Blind Method, Electrophoresis, Polyacrylamide Gel, Female, Humans, Immunoblotting, Immunoglobulin E blood, Male, Middle Aged, Plant Proteins immunology, Surveys and Questionnaires, Carrier Proteins immunology, Food Hypersensitivity immunology, Oryza immunology, Plant Preparations immunology, Prunus immunology
- Abstract
Background: The risk factors for sensitisation to rice and the involved allergens are still partially unknown. In this study we evaluated the clinically relevant aspects of rice allergy in DBPCF-positive patients, the major rice allergens, the severity of peach- and rice-induced symptoms in respect to Pru p 3 sensitisation and the role of anti-rPru p 3 IgE levels as a risk factor for rice allergy., Methods: In 148 peach-allergic subjects, patients with allergic reactions to rice and rice-positive serum IgE were selected. Symptoms were verified by double-blind placebo-controlled food challenges (DBPCFCs), performed at a maximum dosage of 25 g. Rice allergens, identified by IgE immunoblotting, were characterised by N-terminal amino acid sequencing. The relationship between anti-rPru p 3, 1 and 4 IgE levels and rice symptoms were statistically analysed., Results: Eight out of 10 recruited rice-allergic patients had positive DBPCFCs, while 2 patients were not challenged due to their previously documented severe reactions. All patients with rice-induced symptoms were Pru p 3 positive and presented with higher anti-rPru p 3 levels than the rice-sensitised but tolerant patients. A 9-kDa lipid transfer protein, which was highly homologous to Pru p 3, was identified as the major rice allergen and elicited a positive response in all of the patients. Five patients reacted to a putative 15- to 17-kDa rice allergenic protein, and 3 patients reacted to an [alpha]-amylase/subtilisin inhibitor that was approximately 20 kDa., Conclusion: Rarely, allergic reactions to rice can arise in patients with peach allergies who are sensitised to Pru p 3, particularly in patients with high anti-rPru p 3 IgE levels., (Copyright © 2013 S. Karger AG, Basel.)
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- 2013
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25. Anti-rPru p 3 IgE levels are inversely related to the age at onset of peach-induced severe symptoms reported by peach-allergic adults.
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Pastorello EA, Farioli L, Stafylaraki C, Mascheri A, Scibilia J, Pravettoni V, Primavesi L, Piantanida M, Nichelatti M, and Asero R
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- Adolescent, Adult, Age of Onset, Female, Humans, Male, Middle Aged, Antibodies, Anti-Idiotypic, Antigens, Plant immunology, Food Hypersensitivity immunology, Immunoglobulin E, Plant Proteins immunology, Prunus
- Abstract
Sensitisation to peach lipid transfer protein (LTP; Pru p 3) is significantly associated with severe allergic symptoms in adults, but little is known about the age at onset of peach allergy. We investigated a possible correlation between specific IgE levels to Pru p 3 and the age at onset of peach allergy. One hundred and forty-eight patients allergic to peach were divided into 6 classes according to the age at onset. Sera were analyzed for IgE antibodies to peach, rPru p 3, rPru p 1, rPru p 4, rBet v 1, rBet v 2, total IgE titre, and tryptase; all collected data were statistically analysed. A significant inverse correlation was found between the age at onset of peach allergy and anti-rPru p 3 IgE levels at diagnosis (p < 0.0005; Spearman's ρ = -0.3833). In contrast, the age at onset was directly correlated with both anti-rPru p 1 IgE levels (p = 0.0001; Spearman's ρ = 0.3197) and anti-rBet v 1 IgE levels (p = 0.0006; Spearman's ρ = 0.2914) at diagnosis. No correlations were detected between the reported age at onset and anti-peach, anti-rPru p 4, anti-rBet v 2 IgE and total IgE values and serum tryptase levels. At diagnosis, when peach allergy starts at a younger age, it is likely associated with Pru p 3 sensitisation, and the younger the onset, the higher the IgE titres. When peach allergy starts at an older age, it is more likely the result of cross-reactivity to Bet v1., (Copyright © 2013 S. Karger AG, Basel.)
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- 2013
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26. Anisakis simplex: current knowledge.
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Pravettoni V, Primavesi L, and Piantanida M
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- Adaptive Immunity, Animals, Anisakis immunology, Cytokines biosynthesis, Humans, Hypersensitivity etiology, Immunoglobulin E immunology, Anisakiasis epidemiology, Anisakiasis immunology, Anisakiasis therapy
- Abstract
Anisakiasis, firstly described in 1960s in the Netherlands, is a fish-borne parasitic disease caused by the consumption of raw or undercooked fish or cephalopods contaminated by third stage (13) larvae of the Anisakidae family, in particular Anisakis simplex (As), A. pegreffii and Pseudoterranova decipiens. Every year, approximately 20,000 cases of anisakiasis were reported worldwide, over 90% are from Japan and most others in Spain, the Netherlands and Germany, depending on the habits of fish consuming. Live As larvae can elicit i) a parasitic infection of the digestive tract or, occasionally, other organs, causing erosive and/or haemorrhagic lesions, ascites, perforations until granulomas and masses, if larva is not removed, and ii) allergic reactions, as anaphylaxis, acute/chronic urticaria and angioedema. Like other parasite infestations, As larva induces an immune adaptive response characterised by T-lymphocyte proliferation with polyclonal and monoclonal (responsible for As allergic symptoms) IgE production, eosinophilia and mastocytosis. Several As allergens, many of which thermostable, were described In particular the major allergen Ani s 1 and Ani s 7 could characterized a past or a recent infection. There is a general agreement that an active infection is required to initiate allergic sensitivity to Anisakis. Until now, the only effective treatment for anisakiasis is the endoscopic removal of live larvae and the best protection against anisakiasis is to educate consumers about the dangers of eating raw fish and to recommend avoiding the consumption of raw or inadequately thermally treated marine fish or cephalopods.
- Published
- 2012
27. Pru p 3-sensitised Italian peach-allergic patients are less likely to develop severe symptoms when also presenting IgE antibodies to Pru p 1 and Pru p 4.
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Pastorello EA, Farioli L, Pravettoni V, Scibilia J, Mascheri A, Borgonovo L, Piantanida M, Primavesi L, Stafylaraki C, Pasqualetti S, Schroeder J, Nichelatti M, and Marocchi A
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- Adolescent, Adult, Cross Reactions immunology, Cross-Sectional Studies, Female, Food Hypersensitivity blood, Food Hypersensitivity diagnosis, Humans, Immunoglobulin E blood, Italy, Male, Middle Aged, Plant Proteins, Reference Values, Sensitivity and Specificity, Skin Tests, Young Adult, Allergens immunology, Antigens, Plant immunology, Food Hypersensitivity immunology, Immunoglobulin E immunology, Prunus immunology
- Abstract
Background: The roles played by different peach allergens with respect to symptom severity have not been completely ascertained. We have evaluated the diagnostic efficacy of peach recombinant allergens ImmunoCAP compared to peach in the identification of subjects at an increased risk for severe reactions to peaches., Methods: 148 peach-allergic patients were divided based on their symptom severity into 2 groups: mild oral allergy syndrome (OAS) and severe OAS. Anti-rPru p 1, 3 and 4 IgE levels were measured. Statistical analyses were carried out using parametric and non-parametric tests., Results: anti-rPru p 1 and anti-rPru p 4 IgE levels were significantly higher in patients with mild OAS than in patients with severe OAS (p = 0.0001); in contrast, anti-rPru p 3 IgE levels were significantly higher in patients with severe OAS than in patients with mild OAS (p < 0.00005). Moreover, we found that any unitary increase in anti-rPru p 1 IgE values corresponded to a 2.48% reduction in the odds of having severe OAS (p = 0.048), whereas any unitary increase in anti-rPru p 3 IgE values corresponded to a 9.02% increase in the probability of having severe OAS (p = 0.001). Unexpectedly, we found that patients positive to rPru p 3 as well as rPru p 1 and 4 demonstrated a significant reduction of the odds of developing severe symptoms than those positive to rPru p 3 alone. Anti-rPru p 3 IgE levels were a significantly better indicator than anti-peach IgE values (p = 0.016) of patients with the highest risk for severe OAS. A cutoff of 2.69 kUA/l for anti-rPru p 3 IgE values better discriminated peach-allergic patients at a higher risk for symptoms., Conclusions: Italian patients with positive anti-rPru p 1, 4 and 3 IgE levels seemed less likely to experience the clinical effects of high anti-rPru p 3 IgE values., (Copyright © 2011 S. Karger AG, Basel.)
- Published
- 2011
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28. Green bean (Phaseolus vulgaris): a new source of IgE-binding lipid transfer protein.
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Pastorello EA, Pravettoni V, Farioli L, Primavesi L, Scibilia J, Piantanida M, Mascheri A, and Conti A
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- Adolescent, Adult, Amino Acid Sequence, Antigens, Plant immunology, Carrier Proteins chemistry, Female, Humans, Immunoglobulin E chemistry, Male, Molecular Sequence Data, Protein Binding, Young Adult, Carrier Proteins immunology, Food Hypersensitivity immunology, Immunoglobulin E immunology, Phaseolus immunology
- Abstract
Green beans belong to the Fabaceae family, which includes widely consumed species, such as beans, peanuts, and soybeans. In the literature, few cases have described allergic reactions upon the exposure to green bean boiling steam or ingestion. Here, we describe five patients reporting documented adverse reactions upon the ingestion of cooked green beans, and we characterize the responsible allergen. Fresh and cooked green beans were tested by a prick + prick technique. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and IgE immunoblotting were performed with boiled vegetable extract, and the N-terminal sequence of the immunoreactive protein was obtained by analyzing the excised band in a protein sequencer. Immunoblotting inhibition of cooked green bean with in-house-purified peach lipid transfer protein (LTP) Pru p 3 was performed. An interesting green bean protein was chromatographically purified, tested with a pool serum, and inhibited with Pru p 3. Moreover, its molecular mass was determined by mass spectrometry. Prick + prick tests with raw and cooked green beans were positive for all of the patients. IgE immunoblotting showed that all of the patients reacted toward a unique IgE-binding protein at about 9 kDa. The obtained N-terminal sequence revealed the following amino acids: Ala-Ile-Ser-X-Gly-Qln-Val-Thr-Ser-Ser-Leu-Ala, corresponding to an LTP. A complete inhibition of the IgE binding to this protein, in both raw and purified extract, was obtained by purified peach Pru p 3, confirming previous IgE immunoblotting results.
- Published
- 2010
- Full Text
- View/download PDF
29. Tomato allergy: detection of IgE-binding lipid transfer proteins in tomato derivatives and in fresh tomato peel, pulp, and seeds.
- Author
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Pravettoni V, Primavesi L, Farioli L, Brenna OV, Pompei C, Conti A, Scibilia J, Piantanida M, Mascheri A, and Pastorello EA
- Subjects
- Adult, Female, Fruit chemistry, Humans, Immunoblotting, Male, Plant Extracts immunology, Seeds chemistry, Seeds immunology, Skin Tests, Antigens, Plant analysis, Antigens, Plant immunology, Carrier Proteins analysis, Carrier Proteins immunology, Food Hypersensitivity immunology, Fruit immunology, Immunoglobulin E metabolism, Solanum lycopersicum immunology, Plant Proteins analysis, Plant Proteins immunology
- Abstract
There is an increasing consumption of tomatoes worldwide: fresh in salads, cooked in household sauces, or industrially processed. Although many tomato allergens have been identified, there is no information in the literature on the allergenic components found in commercial tomato products. The primary aim of the study was to evaluate the allergenic profile of commercial tomato products by skin prick tests (SPTs) and IgE/immunoblotting in tomato-allergic subjects. The secondary end point was the study of the IgE-binding profile of tomato peel, pulp, and seeds. Forty tomato-allergic patients, reporting oral allergy syndrome (OAS) at different grades of severity for fresh and, in some cases, also for cooked tomato, were selected on the basis of positive tomato allergy history or open food challenge (OFC). They were evaluated by SPTs with different experimental tomato extracts. SDS-PAGE/immunoblotting was performed to detect tomato allergens, which were then identified by Edman degradation. Twenty-three patients (57.5%) presented first-grade OAS at the OFC, whereas 17 (42.5%) reported severe symptoms. Ten of these 17 patients (25%) reported allergic reactions to cooked tomatoes; in immunoblotting tests, their sera reacted only to lipid transfer protein (LTP). In commercial products, LTP was the only detectable allergen. In contrast to other LTP-containing fruits, in tomato, an IgE-binding LTP was identified not only in the peel but also in the pulp and seeds. This study demonstrates that, in fresh tomato, different LTP isoforms are present and allergenic. Industrial tomato derivatives still contain LTP, thus presenting a problem for LTP-allergic patients.
- Published
- 2009
- Full Text
- View/download PDF
30. Maize food allergy: lipid-transfer proteins, endochitinases, and alpha-zein precursor are relevant maize allergens in double-blind placebo-controlled maize-challenge-positive patients.
- Author
-
Pastorello EA, Farioli L, Pravettoni V, Scibilia J, Conti A, Fortunato D, Borgonovo L, Bonomi S, Primavesi L, and Ballmer-Weber B
- Subjects
- Adult, Aged, Anaphylaxis etiology, Antigens, Plant, Child, Double-Blind Method, Female, Food Hypersensitivity immunology, Humans, Immunoglobulin E metabolism, Italy, Male, Middle Aged, Placebos, Plant Proteins, Protein Binding, Young Adult, Carrier Proteins immunology, Chitinases immunology, Food Hypersensitivity etiology, Serologic Tests methods, Zea mays immunology, Zein immunology
- Abstract
Italian patients with maize anaphylaxis have been shown to have IgE toward two major maize allergens: an alpha-amylase inhibitor and a 9-kDa LTP. A complete study on maize food allergens in patients with positive maize double-blind, placebo-controlled food challenge (DBPCFC) is lacking. The objective was to utilize the three maize protein fractions to identify and characterize the most relevant IgE-binding proteins recognized by the sera of Italian and Swiss patients with either a positive maize-DBPCFC or a history of maize-induced anaphylaxis. Osborne's protein fractions of maize were extracted to obtain water-soluble, total zein, and total protein fractions. Protein IgE-binding capacity was investigated by SDS-PAGE immunoblotting using the sera from DBPCFC-positive patients and from patients with maize-induced anaphylaxis. Purified maize LTP was used to inhibit the IgE immunoblotting of the three protein fractions. IgE immunoblotting demonstrated that the 9-kDa LTP was recognized by all the Italian patients and by none of the Swiss patients. Other allergens were: 14-kDa alpha-amylase inhibitor, 30-kDa endochitinases A and -B, 19 kDa zein-beta precursor, and 26 kDa zein-alpha precursor; a newly described allergen, the globulin-2 precursor, identified in the total protein fraction. It is noteworthy that maize LTP and endochitinase were cross-reactive with grape LTP and one grape endochitinase. LTP was found to be the only major allergen in Italian patients with either positive maize challenge or a history of maize-induced anaphylaxis. We have identified other maize allergens in subjects with maize food allergy, as grape cross-reactive endochitinase, however, the clinical significance of these proteins needs to be investigated in larger groups of patients with allergy to these food items.
- Published
- 2009
- Full Text
- View/download PDF
31. Silencing by plant Polycomb-group genes requires dispersed trimethylation of histone H3 at lysine 27.
- Author
-
Schubert D, Primavesi L, Bishopp A, Roberts G, Doonan J, Jenuwein T, and Goodrich J
- Subjects
- AGAMOUS Protein, Arabidopsis metabolism, Alleles, Amino Acid Sequence, Arabidopsis Proteins chemistry, Carrier Proteins metabolism, Cell Nucleus metabolism, Cold Temperature, DNA-Binding Proteins, Homeodomain Proteins chemistry, MADS Domain Proteins metabolism, Methylation, Mitosis, Models, Genetic, Molecular Sequence Data, Nuclear Proteins metabolism, Plant Leaves cytology, Plant Roots cytology, Point Mutation genetics, Polycomb-Group Proteins, Protein Structure, Tertiary, Transgenes, Arabidopsis metabolism, Arabidopsis Proteins metabolism, Gene Silencing, Genes, Plant genetics, Histones metabolism, Homeodomain Proteins metabolism, Lysine metabolism, Repressor Proteins genetics
- Abstract
The plant Polycomb-group (Pc-G) protein CURLY LEAF (CLF) is required to repress targets such as AGAMOUS (AG) and SHOOTMERISTEMLESS (STM). Using chromatin immunoprecipitation, we identify AG and STM as direct targets for CLF and show that they carry a characteristic epigenetic signature of dispersed histone H3 lysine 27 trimethylation (H3K27me3) and localised H3K27me2 methylation. H3K27 methylation is present throughout leaf development and consistent with this, CLF is required persistently to silence AG. However, CLF is not itself an epigenetic mark as it is lost during mitosis. We suggest a model in which Pc-G proteins are recruited to localised regions of targets and then mediate dispersed H3K27me3. Analysis of transgenes carrying AG regulatory sequences confirms that H3K27me3 can spread to novel sequences in a CLF-dependent manner and further shows that H3K27me3 methylation is not sufficient for silencing of targets. We suggest that the spread of H3K27me3 contributes to the mitotic heritability of Pc-G silencing, and that the loss of silencing caused by transposon insertions at plant Pc-G targets reflects impaired spreading.
- Published
- 2006
- Full Text
- View/download PDF
32. Functional analysis of linker insertions and point mutations in the alpha-Amy2/54 GA-regulated promoter.
- Author
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Tregear JW, Primavesi LF, and Huttly AK
- Subjects
- Base Sequence, DNA Mutational Analysis, Glucuronidase biosynthesis, Molecular Sequence Data, Mutagenesis, Insertional, Point Mutation, Recombinant Fusion Proteins biosynthesis, Triticum drug effects, Triticum enzymology, Gene Expression Regulation, Plant, Gibberellins pharmacology, Promoter Regions, Genetic, Triticum genetics, alpha-Amylases genetics
- Abstract
Functional analysis of a gibberellin-regulated wheat alpha-amylase promoter, alpha-Amy2/54, has indicated that three regions were essential for expression. By studying the ability of mutant promoters, containing a randomly inserted 22 bp excision linker, to direct expression in oat aleurone protoplasts we have refined the positions and extents of these three cis elements and also demonstrated the presence of two additional elements. By converting the linker insertions to either single base point mutations or deletions using the class IIS restriction endonuclease BsmI we have shown that nucleotides -119 and -109 within the GARE -121GTAACAGAGTCTGG-108 and nucleotide -152 within the proposed element -156GATTGACTTGACC-144 are essential for high level expression from this promoter.
- Published
- 1995
- Full Text
- View/download PDF
33. [ANALYSIS OF THE MOST COMMON LESIONS IN VARIOUS SPORTS; NEW THERAPEUTIC ORIENTATIONS IN 100 CASES].
- Author
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PRIMAVESI L
- Subjects
- Humans, Anti-Infective Agents, Local, Drug Therapy, Oxyphenbutazone, Sports, Sports Medicine, Wounds and Injuries
- Published
- 1964
34. [The physician and boxing].
- Author
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PRIMAVESI L
- Subjects
- Humans, Boxing, Physicians, Sports
- Published
- 1955
35. [A NEW TREATMENT OF ASCITOGENIC CIRRHOSIS. (PRELIMINARY REPORT)].
- Author
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PRIMAVESI L, FERRITO A, and GOLDNER R
- Subjects
- Humans, Ascites, Liver Cirrhosis, Thiamine Pyrophosphate, Thioctic Acid
- Published
- 1963
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