Person:
Vivanco Martínez, Fernando

First Name

Fernando

Last Name

Vivanco Martínez

URI

https://hdl.handle.net/20.500.14352/84150

Affiliation

Universidad Complutense de Madrid

Faculty / Institute

Ciencias Químicas

Area

Bioquímica y Biología Molecular

Identifiers

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Search Results

Now showing 1 - 10 of 29

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.
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, Carlos
Allergy to Pumpkin With Cyclophilin as the Relevant Allergen
(ANNALS OF ALLERGY ASTHMA & IMMUNOLOGY, 2010) González de Olano, David; González-Mancebo, Eloina; Santos Macadán, Sara; Gandolfo Cano, Mar; Pérez-Gordo, Marina; Cases Ortega, Bárbara; Vivanco Martínez, Fernando; Pastor Vargas, Carlos
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
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, Javier
Allergy to Prairie Dog Lipocalins
(ANNALS OF ALLERGY ASTHMA & IMMUNOLOGY, 2010) González de Olano, David; Bartolomé, Borja; Cases Ortega, Bárbara; Pérez-Gordo, Marina; Vivanco Martínez, Fernando; Pastor Vargas, Carlos
Phosphorylation reduces the allergenicity of cow casein in children with selective allergy to goat and sheep milk.
(J Investig Allergol Clin Immunol, 2011) Cases, Barbara; García-Ara, Carmen; Boyano, Maria Teresa; Pérez-Gordo, Marina; Pedrosa, Maria; Vivanco Martínez, Fernando; Quirce, Santiago; Pastor Vargas, Carlos
This study aimed to characterize the role of phosphorylation of caseins in selective allergy to goat milk (GM) and sheep milk (SM) in patients with good tolerance to cow milk (CM). We performed skin prick tests with milk and caseins from CM, GM, and SM and immunoblotting and specific immunoglobulin (Ig) E determinations with milk and casein from cow and GM and SM. Sensitization to milk and caseins from goat and sheep was demonstrated in all 3 patients by skin tests, determination of specific IgE, or both. Immunoblotting confirmed that GM/SM proteins but not CM proteins were involved in the allergic symptoms. IgE reacted with several protein bands from the caseins and milk extracts of both sheep and goat. Phosphorylation was involved in the different allergenicity of CM caseins. We report the implication of phosphorylation in the allergenicity of caseins involved in selective allergy to GM and SM.
Secretome analysis of atherosclerotic and non-atherosclerotic arteries reveals dynamic extracellular remodeling during pathogenesis
(Journal of Proteome, 2012) Cuesta, Fernando de la; Barderas, Maria G.; Calvo, Enrique; Zubiri, Irene; Maroto, Aroa S.; Darde, Veronica M.; Martin-Rojas, Tatiana; Gil Dones, Félix; Posada-Ayala, Maria; Tejerina, Teresa; Lopez, Juan A.; Vivanco Martínez, Fernando; Alvarez-Llamas, Gloria
Aims: Early detection of cardiovascular diseases and knowledge of underlying mechanisms is essential. Tissue secretome studies resemble more closely to the in vivo situation, showing a much narrower protein concentrations dynamic range than plasma. This study was aimed to the analysis of human arterial tissue secretome and to the quantitative comparison of healthy and atherosclerotic secretome to discover proteins with key roles in atherosclerosis development. Methods and results: Secretomes from three biological replicates of human atherosclerotic coronary arteries (APC), preatherosclerotic coronaries (PC) and mammaries (M) were analyzed by LC-MS/MS. The identified proteins were submitted to Ingenuity Pathway Analysis (IPA) tool. Label-free MS/MS based quantification was performed and validated by immunohistochemistry. 64 proteins were identified in the 3 replicates of at least one of the 3 groups and 15 secreted proteins have not been previously reported in plasma. Four proteins were significantly released in higher amounts by mammary tissue: gelsolin, vinculin, lamin A/C and phosphoglucomutase 5. Conclusion: The study of tissue secretome reveals key proteins involved in atherosclerosis which have not been previously reported in plasma. Novel proteins are here highlighted which could be potential therapeutic targets in clinical practice. This article is part of a Special Issue entitled: Proteomics: The clinical link.
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.
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, Javier
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.