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
7 results
Search Results
Now showing 1 - 7 of 7
- Project number: 322
Item La ciencia y tecnología químicas al servicio de la sociedad: actividad formativa para los alumnos del Máster en Ciencia y Tecnología Químicas(2023) Guzmán Solís, Eduardo; Guerrero Martínez, Andrés; Sánchez Benítez, Francisco Javier; Lobato Fernández, Álvaro; Barrio Redondo, Melissa del; Pradanas González, Fernando; Cano Rico, Israel; Castillo Martínez, Elisabet; Kayser González, Paula; Moya Cerero, Santiago de la; Gómez Gutiérrez, Julián; Palomares Gracia, Óscar; Pastor Vargas, Carlos; Encinas García, Noemí; García Martín, Gustavo; Lasanta Carrasco, María Isabel Item Food Allergens: When Friends Become Foes—Caveats and Opportunities for Oral Immunotherapy Based on Deactivation Methods(Nutrients, 2023) Gil, Victoria M.; Fernández-Rivera, Nuria; Pastor Vargas, Carlos; Cintas, PedroFood allergies represent a serious health concern and, since the 1990s, they have risen gradually in high-income countries. Unfortunately, the problem is complex because genetic, epigenetic, and environmental factors may be collectively involved. Prevention and diagnoses have not yet evolved into efficacious therapies. Identification and control of allergens present in edible substances hold promise for multi-purpose biomedical approaches, including oral immunotherapy. This review highlights recent studies and methods to modify the otherwise innocuous native proteins in most subjects, and how oral treatments targeting immune responses could help cancel out the potential risks in hypersensitive individuals, especially children. We have focused on some physical methods that can easily be conducted, along with chemo-enzymatic modifications of allergens by means of peptides and phytochemicals in particular. The latter, accessible from naturally-occurring substances, provide an added value to hypoallergenic matrices employing vegetal wastes, a point where food chemistry meets sustainable goals as well.Item 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 LTP Allergy Follow-Up Study: Development of Allergy to New Plant Foods 10 Years Later(Nutrients, 2021) Betancor, Diana; Gomez Lopez, Alicia; Villalobos Vilda, Carlos; Nuñez Borque, Emilio; Fernández Bravo, Sergio; De las Heras Gozalo, Manuel; Pastor Vargas, Carlos; Esteban, Vanesa; Cuesta Herranz, JavierIntroduction: Allergy to nonspecific lipid transfer protein (nsLTP) is the main cause of plant-food allergy in Spain. nsLTPs are widely distributed in the plant kingdom and have high cross-reactivity but extremely variable clinical expression. Little is known about the natural evolution of this allergy, which complicates management. The objective of this study was to assess the development of allergy to new plant foods in nsLTP-sensitized patients 10 years after diagnosis. Methods: One hundred fifty-one patients showing specific IgE to nsLTP determined by ISAC (Thermofisher) were included. After clinical workup (i.e., anamnesis, skin test, and challenge when needed), these patients were divided into two groups: 113 patients allergic to one or more plant food (74.5%) and 38 patients not allergic to any plant food (25.1%). Ten years later, a telephone interview was conducted to check whether patients had developed additional allergic reactions to plant foods. Results: Ten years after diagnosis, 35 of the 113 (31%) plant-food-allergic patients sensitized to nsLTP reported reactions to new, previously tolerated plant foods, mainly Rosaceae/Prunoideae fruits and nuts followed by vegetables, Rosacea/Pomoideae fruits, legumes, and cereals. Five out of 38 (13.2%) patients previously sensitized to nsLTP but without allergy to any plant food had experienced allergic reactions to some plant food: two to Rosaceae/Prunoideae fruits, two to Rosaceae/Prunoideae fruit and nuts, and one to legumes. Conclusion: Patients sensitized to nsLTP developed allergic reactions to other plant foods, mainly Rosaceae-Prunoideae fruits and nuts. This was more frequent among plant-food-allergic patients than among those who had never had plant-food allergy.Item Generation of an Ovomucoid-Immune scFv Library for the Development of Novel Immunoassays in Hen’s Egg Detection(Foods, 2023) Rodríguez, Santiago; García García, Aina; García Calvo, Eduardo Rafael; Esteban, Vanesa; Pastor Vargas, Carlos; Díaz-Perales, Araceli; García Lacarra, Teresa; Martín, RosarioHen’s egg allergy is the second most common food allergy among infants and young children. The possible presence of undeclared eggs in foods poses a significant risk to sensitized individuals. Therefore, reliable egg allergen detection methods are needed to ensure compliance with food labeling and improve consumer protection. This work describes for the first time the application of phage display technology for the generation of a recombinant antibody aimed at the specific detection of hen’s ovomucoid. First, a single-chain variable fragment (scFv) library was constructed from mRNA isolated from the spleen of a rabbit immunized with ovomucoid. After rounds of biopanning, four binding clones were isolated and characterized. Based on the best ovomucoid-binding candidate SR-G1, an indirect phage enzyme-linked immunosorbent assay (phage-ELISA) was developed, reaching limits of detection and quantitation of 43 and 79 ng/mL of ovomucoid, respectively. The developed ELISA was applied to the analysis of a wide variety of food products, obtaining a good correlation with a commercial egg detection assay used as a reference. Finally, in silico modeling of the antigen-antibody complex revealed that the main interactions most likely occur between the scFv heavy chain and the ovomucoid domain-III, the most immunogenic region of this allergen.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 extractItem Characterization of Relevant Biomarkers for the Diagnosis of Food Allergies: An Overview of the 2S Albumin Family(Foods, 2021) Bueno Díaz, Cristina; Martín-Pedraza, Laura; Parrón Ballesteros, Jorge; Cuesta-Herranz, Javier; Cabanillas, Beatriz; Pastor Vargas, Carlos; Batanero Cremades, Eva; Villalba Díaz, María Teresa2S albumins are relevant and often major allergens from several tree nuts and seeds, affecting mainly children and young people. The present study aims to assess how the structural features of 2S albumins could affect their immunogenic capacity, which is essential to comprehend the role of these proteins in food allergy. For this purpose, twelve 2S albumins were isolated from their respective extracts by chromatographic methods and identified by MALDI-TOF massspectrometry. Their molecular and structural characterization was conducted by electrophoretic, spectroscopic and in silico methods, showing that these are small proteins that comprise a wide range of isoelectric points, displaying a general high structure stability to thermal treatment. Despite low amino acid sequence identity, these proteins share structural features, pointing conformational epitopes to explain cross-reactivity between them. Immunoblotting with allergic patients’ sera revealed those possible correlations between evolutionarily distant 2S albumins from different sources. The availability of a well-characterized panel of 2S albumins from plant-derived sources allowed establishing correlations between their structural features and their allergenic potential, including their role in cross-reactivity processes