Person:
Pastor Vargas, Carlos

First Name

Carlos

Last Name

Pastor Vargas

URI

https://hdl.handle.net/20.500.14352/76123

Affiliation

Universidad Complutense de Madrid

Faculty / Institute

Ciencias Químicas

Department

Bioquímica y Biología Molecular

Area

Bioquímica y Biología Molecular

Identifiers

Full item page

Search Results

Now showing 1 - 10 of 21

Targeting antigens to an invariant epitope of the MHC Class II DR molecule potentiates the immune response to subunit vaccines
(Virus Research, 2011) Pérez-Filgueira, Mariano; Barderas, María G.; Alonso, Covadonga; José M, Escribano; Gil Dones, Félix; Pastor Vargas, Carlos; Vivanco Martínez, Fernando
Recombinant subunit and peptidic vaccines in general present a reduced immunogenicity in vaccinated individuals with respect to the whole pathogen from which they derived. The generation of strong immune responses to these vaccines requires the use of potent adjuvants, high antigen doses and repetitive vaccinations. In this report, we document the enhanced antibody response obtained against two recombinant subunit vaccines by means of targeting to antigen-presenting cells by a recombinant single chain antibody. This antibody, named APCH1, recognizes an epitope of MHC Class II DR molecule preserved in different animal species, including humans. We showed that vaccinal antigens translationally fused to APCH1 antibody and produced by recombinant baculoviruses in insect larvae (Trichoplusia ni), elicited an increased antibody response in comparison with the same antigens alone or fused to a carrier molecule. These results suggest that targeting of antigens to this invariant MHC Class II epitope has immunopotentiating effects that could circumvent the reduced potency of peptidic or subunit vaccines, opening the possibility of widespread application of APCH1 as a new adjuvant antibody of general use.
Identification of vitellogenin as an allergen in Beluga caviar allergy
(Allergy, 2008) Pérez‐Gordo, M.; Sánchez‐García, S.; Cases, B.; Cuesta‐Herranz, J.; Pastor Vargas, Carlos; Vivanco Martínez, Fernando
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, Carlos
Expression of endothelial nitric oxide synthase in human peritoneal tissue: regulation by escherichia coli lipopolysaccharide
(Journal of the American Society of Nephrology, 2000) Arriero, María M.; Rodríguez-Feo, Juan A.; Celdrán, Ángel; Sánchez de Miguel, Lourdes; González Fernández, Fernando; Fortes, José; Reyero, Ana; Frieyro, Octavio; Pinta, Juan C de la; Franco, Ángeles; Casado, Santos; López Farre, Antonio José; Pastor Vargas, Carlos
Changes in the expression of endothelial nitric oxide synthase (eNOS) in the peritoneum could be involved in the peritoneal dysfunction associated with peritoneal inflammation. Demonstrated recently in bovine endothelial cells was the existence of cytosolic proteins that bind to the 3′-untranslated region (3′-UTR) of eNOS mRNA and could be implicated in eNOS mRNA stabilization. The present work demonstrates that eNOS protein is expressed in human endothelial and mesothelial peritoneal cells. Escherichia coli lipopolysaccharide shortened the half-life of eNOS message, reducing eNOS protein expression in peritoneal mesothelial and endothelial cells. Moreover, under basal conditions, human peritoneal samples expressed cytosolic proteins that bind to the 3′-UTR of eNOS mRNA. The cytosolic proteins that directly bind to 3′-UTR were identified as a 60-kD protein. After incubation of human peritoneal samples with lipopolysaccharide, the binding activity of the cytosolic 60-kD protein increased in a time-dependent manner. Studies are now necessary to determine the involvement of this 60-kD protein in the regulation of eNOS expression in peritoneal cells and particularly its involvement in the peritoneal dysfunction associated with inflammatory reactions.
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, Carlos
The 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.
Characterization of allergens from the fish bait galleria mellonella
(J Allergy Clin Immunol, 2007) Madero, Mauro F.; Enríquez-Matas, Alicia; Fernández-Nieto, Mar; Sastre, Beatriz; Pozo, Victoria del; Santiago Quirce, Santiago; Sastre, Joaquín; Pastor Vargas, Carlos
Sensitive detection of major food allergens in breast milk: first gateway for allergenic contact during breastfeeding
(Allergy, 2015) Pastor Vargas, Carlos; Maroto, Aroa; Díaz‐Perales, Araceli; Villalba Díaz, María Teresa; Casillas Diaz, Natalia; Vivanco Martínez, Fernando; Cuesta‐Herranz, Javier
Food allergy is recognized as a major public health issue, especially in early childhood. It has been hypothesized that early sensitization to food allergens maybe due to their ingestion as components dissolved in the milk during the breastfeeding, explaining reaction to a food, which has never been taken before. Thus, the aim of this work has been to detect the presence of the food allergens in breast milk by microarray technology. We produced a homemade microarray with antibodies produced against major food allergens. The antibody microarray was incubated with breast milk from 14 women collected from Fundación Jiménez Díaz Hospital. In this way, we demonstrated the presence of major foods allergens in breast milk. The analysis of allergens presented in breast milk could be a useful tool in allergy prevention and could provide us a key data on the role of this feeding in tolerance induction or sensitization in children.
Epitope mapping of the major allergen from Atlantic cod in Spanish population reveals different IgE‐binding patterns
(Molecular Nutrition Food Research, 2013) Perez‐Gordo, Marina; Pastor Vargas, Carlos; Jing Lin; Bardina, Ludmilla; Cases, Barbara; Ibáñez, Maria Dolores; Vivanco Martínez, Fernando; Cuesta‐Herranz, Javier; Sampson, Hugh
Scope: IgE-epitope mapping of allergens reveal important information about antigen components involved in allergic reactions. The peptide-based microarray immunoassay has been used to map epitopes of some food allergens. We developed a peptide microarray immunoassay to map allergenic epitopes in parvalbumin from Atlantic cod (Gad m 1), the most consumed cod species in Spain. Methods and results: Sera from 13 fish-allergic patients with specific IgE to cod parvalbumin were used. A library of overlapping peptides was synthesized, representing the primary sequence of Gad m 1. Peptides were used to analyze allergen-specific IgE antibodies in patient sera. 100% of the patients recognized one antigenic region of 15 amino acids in length in Gad m 1. This region only partially correlated with one of the three antigenic determinants of Gad c 1 (Allergen M), parvalbumin from Baltic cod (Gadus callarias). In the 3D model of the protein, this region was located on the surface of the protein. Conclusion: We have identified a relevant antigenic region in Gad m 1. This epitope could be considered as a severity marker and provides additional information to improve fish allergy diagnosis and the design of safe immunotherapeutic tools.
Novel liquid chromatography–mass spectrometry method for sensitive determination of the mustard allergen Sin a 1 in food
(Food Chemistry, 2015) Maria Posada-Ayala; Álvarez Llamas, Gloria; Aroa S. Maroto; Xavier Maes; Esther Muñoz-Garcia; Villalba Díaz, María Teresa; Rodríguez García, Rosalía; Marina Perez-Gordo; Vivanco Martínez, Fernando; Pastor Vargas, Carlos; Javier Cuesta-Herranz
Mustard 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.
First case of airborne-induced anaphylaxis triggered by fruit
(ANNALS OF ALLERGY ASTHMA & IMMUNOLOGY, 2015) Eva M. Macías; Omar Sierra-Salgado; Borja Bartolomé; Pastor Vargas, Carlos; Francisco J. Muñoz-Bellido; Ignacio Dávila