Person: Pastor Vargas, Carlos
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First Name
Carlos
Last Name
Pastor Vargas
Affiliation
Universidad Complutense de Madrid
Faculty / Institute
Ciencias Químicas
Department
Bioquímica y Biología Molecular
Area
Bioquímica y Biología Molecular
Identifiers
11 results
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Now showing 1 - 10 of 11
Item Occupational asthma caused by gerbil: purification and partial characterization of a new gerbil allergen(ANNALS OF ALLERGY ASTHMA & IMMUNOLOGY, 2010) de las Heras, Manuel; Cuesta-Herranz, Javier; Cases, Bárbara; de Miguel, Jaime; Fernández-Nieto, Mar; Sastre, Joaquin; Vivanco Martínez, Fernando; Pastor Vargas, CarlosItem Identification of potential allergens involved in systemic reactions to melon and watermelon(Annals of allergy, asthma & immunology, 2010) González-Mancebo, Eloina; López-Torrejón, Gema; González de Olano, David; Cembellín Santos, Sara; Gandolfo-Cano, Mar; Meléndez, Amaya; Salcedo, Gabriel; Cuesta-Herranz, Javier; Vivanco Martínez, Fernando; Pastor Vargas, CarlosItem Identification of new allergens in macadamia nut and cross-reactivity with other tree nuts in a Spanish cohort(Nutrients, 2024) Gutiérrez-Díaz, Gloria; Betancor, Diana; Parrón Ballesteros, Jorge; Gordo, Rubén G.; Castromil-Benito, Estela S.; Haroum, Eleisa; Vázquez de la Torre, María; Turnay Abad, Francisco Javier; Villalba Díaz, María Teresa; Cuesta-Herranz, Javier; Pastor Vargas, CarlosThe consumption of macadamia nuts has increased due to their cardioprotective and antioxidant properties. However, this rise is consistent with an increase in the cases of macadamia nut allergy, leading to severe reactions. Although two macadamia integrifolia allergens (Mac i 1 and Mac i 2) have been identified in Australian and Japanese patients, the allergenic sensitization patterns in Western European populations, particularly in Spain, remain unclear. For this purpose, seven patients with macadamia nut allergy were recruited in Spain. Macadamia nut protein extracts were prepared and, together with hazelnut and walnut extracts, were used in Western blot and inhibition assays. IgE-reactive proteins were identified using MALDI-TOF/TOF mass spectrometry (MS). Immunoblotting assays revealed various IgE-binding proteins in macadamia nut extracts. Mass spectrometry identified three new allergens: an oleosin, a pectin acetylesterase, and an aspartyl protease. Cross-reactivity studies showed that hazelnut extract but not walnut extract inhibited macadamia nut oleosin-specific IgE binding. This suggests that oleosin could be used as marker for macadamia–hazelnut cross-reactivity. The results show an allergenic profile in the Spanish cohort different from that previously detected in Australian and Japanese populations. The distinct sensitization profiles observed highlight the potential influence of dietary habits and environmental factors exposure on allergenicity.Item New allergen involved in a case of allergy to Solea solea, common sole(ANNALS OF ALLERGY ASTHMA & IMMUNOLOGY, 2010) Pérez-Gordo, Marina; Pastor Vargas, Carlos; Cases, Bárbara; De Las Heras, Manuel; Sanz, Aroa; Vivanco Martínez, Fernando; Cuesta-Herranz, JavierItem Novel liquid chromatography–mass spectrometry method for sensitive determination of the mustard allergen Sin a 1 in food(Food Chemistry, 2015) Posada-Ayala, Maria; Álvarez Llamas, Gloria; Maroto, Aroa; Maes, Xavier; Muñoz-Garcia, Esther; Villalba Díaz, María Teresa; Rodríguez García, Rosalía; Perez-Gordo, Marina; Vivanco Martínez, Fernando; Pastor Vargas, Carlos; Cuesta-Herranz, JavierMustard is a condiment added to a variety of foodstuffs and a frequent cause of food allergy. A new strategy for the detection of mustard allergen in food products is presented. The methodology is based on liquid chromatography analysis coupled to mass spectrometry. Mustard allergen Sin a 1 was purified from yellow mustard seeds. Sin a 1 was detected with a total of five peptides showing a linear response (lowest LOD was 5ng). Sin a 1 was detected in mustard sauces and salty biscuit (19±3mg/kg) where mustard content is not specified. Sin a 1, used as an internal standard, allowed quantification of this mustard allergen in foods. A novel LC/MS/MS SRM-based method has been developed to detect and quantify the presence of mustard. This method could help to detect mustard allergen Sin a 1 in processed foods and protect mustard-allergic consumers.Item Watermelon Profilin: Characterization of a Major Allergen as a Model for Plant-Derived Food Profilins(International Archives of Allergy Immunology, 2010) Cases, Bárbara ; Pastor Vargas, Carlos; Gil Dones, Félix; Perez-Gordo, Marina; Maroto, Aroa; las Heras, Manuel de las; Vivanco Martínez, Fernando; Cuesta-Herranz, JavierBackground: Plant profilins have been reported as minor allergens. They are a well-known pan-allergen family responsible for cross-reactivity between plant-derived foods and pollens. Watermelon profilin has been reported to be a major allergen in watermelon (Citrullus lanatus).The aim of this study was to characterize recombinant watermelon profilin, confirming its reactivity for diagnostic purposes and the development of immunotherapy. Methods: Native profilin was purified from watermelon extract by affinity chromatography using poly-L-proline. Recombinant His-tagged profilin was produced in Pichia pastoris yeast using pPICZαA vector and purified by metal chelate affinity chromatography. ELISA and immunoblot were carried out with sera from 17 watermelon-allergic patients. Biological activity was tested by the basophil activation test. Results: Native profilin and recombinant profilin were purified and identified by mass spectrometry. Both show similar IgE reactivity in vitro and are biologically active. Conclusions: Similarities were found in the IgE-binding patterns and biological activity of recombinant profilin and native profilin. Recombinant profilin may be a powerful tool for specific diagnosis.Item Allergy to pumpkin and cross-reactivity to other Cucurbitaceae fruits(The Journal of Allergy and Clinical Immunology, 2000) Figueredo, Elena ; Cuesta-Herranz, Javier ; Minguez, Ascensión ; Vidarte, Luis ; Pastor Vargas, Carlos; Heras González, Manuel De Las; Vivanco Martínez, Fernando; Lahoz, CarlosMost human nephritis is due to glomerular deposition and/or formation of immune complexes (IC). In cultured mesangial cells, Fc receptor stimulation induces proliferation, matrix synthesis, and release of several mediators implicated in the initiation and progression of glomerular injury. Since Ig Fc fragments in vitro modified these phenomena, we studied the effects of systemic administration of IgG Fc fragments on the evolution of experimental IC nephritis. Fc fragment injection (1 mg/day i.p.) to rats with ongoing nephritis (proteinuria 20–50 mg/24 h vs 9 6 0.2 mg/24 h in controls) markedly ameliorates proteinuria, renal function, and morphological renal lesions. This was accompanied by a reduction in the renal synthesis of chemokines (monocyte chemoattractant protein-1, IFN-inducible protein-10, and cytokine-induced neutrophil chemoattractant-1), matrix proteins, and growth factors (platelet-derived growth factor, and TGF-b), and in the activity of transcription factors. The treatment did not affect the glomerular deposition of IgG IC and complement C1q. In contrast, a decrease in the renal expression and production of C3 was observed without changes in serum complement levels. In vitro, very low complement consumption and no C3b covalent interaction were observed with Fc fragments, confirming that they did not modify systemic complement activity. These results indicate that the administration of Fc fragments prevents the development of glomerular damage in an aggressive model of proliferative glomerulonephritis through mechanisms involving a reduced local generation of complement, chemokines and growth factors. Modulation of IC-mesangial cell interaction by Fc fragment administration could represent a new approach to the treatment of severe immune nephritisItem Allergy to kiwi: a double-blind, placebo-controlled food challenge study in patients from a birch-free area.(Journal of Allergy and Clinical Immunology, 2004) Alemán, Ana; Sastre, Joaquín; Quirce, Santiago; Heras González, Manuel De Las; Carnés, Jerónimo; Fernández-Caldas, Enrique; Pastor Vargas, Carlos; Blázquez, Ana Belén; Vivanco Martínez, Fernando; Cuesta-Herranz, Javierackground: Allergy to kiwi fruit is being increasingly reported, but it has never been evaluated by means of a double-blind, placebo-controlled food challenge (DBPCFC) study. Objective: We sought to assess kiwi allergy on the basis of a DBPCFC and identify the patterns of allergen recognition in sensitized patients from a birch-free area. Methods: Forty-three patients with allergy symptoms who were sensitized to kiwi were evaluated by means of clinical history, skin tests, IgE determinations, and DBPCFCs. The pattern of allergen recognition was assessed by means of IgE immunoblotting. Sequence analysis of IgE-binding bands was performed by using Edman degradation. Results: DBPCFCs were performed in 33 patients; 4 patients had experienced severe anaphylaxis, and 6 patients declined informed consent. DBPCFC results were positive in 23 patients and negative in 10 patients. The most frequent clinical manifestation was oral allergy syndrome. Twenty-one percent of the patients were not allergic to pollen. Forty-six percent of patients experienced systemic symptoms, and this happened with higher frequency in patients not allergic to pollen (100%). Twenty-eight percent of the patients were sensitized to latex. The IgE-binding bands in kiwi extract more frequently recognized by patient sera were those of 30, 24, 66, and 12 kd, and they could not be associated with any pattern of kiwi-induced allergic reactions. Conclusion: The results provide evidence that kiwi allergy is not a homogeneous disorder because several clinical subgroups can be established. No definite allergen-recognition pattern was associated with the type of allergic reactions to kiwi. One of 5 patients with kiwi allergy was not allergic to pollen, and these patients had the highest risk of systemic reactions to kiwi.Item Identification of Major Allergens in Watermelon(International Archives on Allergy & Immunology, 2009) Pastor Vargas, Carlos; Cuesta-Herranz, Javier; Cases, Barbara; Pérez-Gordo, Marina; Figueredo, Elena; Heras González, Manuel De Las; Vivanco Martínez, FernandoBackground: Watermelon is a worldwide consumed Cucurbitaceae fruit that can elicit allergic reactions. However, the major allergens of watermelon are not known. The aim of this study is to identify and characterize major allergens in watermelon. Methods: Twenty-three patients allergic to watermelon took part in the study. The diagnosis was based on a history of symptoms and positive skin prick-prick tests to watermelon, confirmed by positive open oral challenge testing to watermelon pulp. Allergenic components were detected by SDS-PAGE and immunoblotting. Molecular characterization of IgE-binding bands was performed by N-terminal amino acid sequencing and mass spectrometry. Allergens were purified combining several chromatographic steps. Results: Several IgE binding bands (8-120 kDa) were detected in watermelon extract. Three major allergens were identified as malate dehydrogenase (36 kDa), triose phosphate isomerase (28 kDa) and profilin (13 kDa). Purified allergens individually inhibited IgE binding to the whole watermelon extract. Conclusions: All in all these results indicate that malate dehydrogenase, triose phosphate isomerase and profilin are major allergens involved in watermelon allergy.Item 2S albumins and 11S globulins, two storage proteins involved in pumpkin seeds allergy(Allergy: European Journal of Allergy and Clinical Immunology, 2021) Bueno Díaz, Cristina; Martín-Pedraza, Laura; León, Laura; Haroun-Díaz, Elisa; Pastor Vargas, Carlos; Muñoz-García, Esther; De las Heras, Manuel; Batanero Cremades, Eva; Cuesta-Herranz, Javier; Villalba Díaz, María TeresaMembers from Cucurbitaceae family have been reported to induce food allergy.1, 7 Pumpkin (Cucurbita maxima) pulp has been mostly the allergenic source but few studies are focused on the allergenic potential of its seeds.2 Pumpkin seed may be consumed as snacks or as components in other food products, becoming hidden allergens, eliciting infrequent but severe cases of allergy with life-threatening reactions.3 The nature of those allergens has not been investigated in detail so far. This study aimed to identify two allergens, from pumpkin seeds a 2S albumin and an 11S globulin, involved in severe allergic reactions of four patients allergic to these seeds and evaluate the cross-reactivity with other seeds and nuts containing homologous proteins. General characteristics of selected individuals, extracted from their clinical histories, are shown in Table S1. All patients described immediate allergic reactions with severe and systemic symptoms as anaphylaxis, showing a positive specific IgE (ImmunoCAP, Thermo Fisher) and Skin prick testing (SPT) to pumpkin seeds extract