Person:
Gil Dones, Félix

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First Name
Félix
Last Name
Gil Dones
URI
https://hdl.handle.net/20.500.14352/74303
Affiliation
Universidad Complutense de Madrid
Faculty / Institute
Ciencias Biológicas
Department
Genética, Fisiología y Microbiología
Area
Genética
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2010 - 20113
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Author: Barderas, María G. ×

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Now showing 1 - 3 of 3
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    Development of an Optimal Protocol for the Proteomic Analysis of Stenotic and Healthy Aortic Valves
    (Revista Española de Cardiologia, 2010) Martín-Rojas, Tatiana; López-Almodovar, Luis F.; Juárez-Tosina, Rocío; Gil Dones, Félix; Cuesta, Fernando de La; Álvarez-Llamas, Gloria; Alonso-Orgaz, Sergio; Vivanco, Fernando; Rodríguez-Padial, Luis; Barderas, María G.
    Introduction and objectives: For many years, degenerative aortic stenosis was thought to be a passive process secondary to calcium deposition in aortic valves. Although its etiology remains unknown, several authors have pointed out that degenerative aortic stenosis is associated with the same risk factors as coronary artery disease. Furthermore, histological similarities have been found between aortic valve stenosis and atherosclerotic plaque, giving rise to the hypothesis that degenerative aortic stenosis is an inflammatory process similar to atherosclerosis. Nevertheless, some data do not fit with this hypothesis and, consequently, greater understanding of the condition is needed. The main aim of this study was to develop a practical protocol for extracting protein for use in proteomic analysis from both stenotic and healthy aortic valves. Methods: The study was carried out using a number of different proteomic methods: two-dimensional electrophoresis, mass spectrometry, and additional techniques. Results: We developed a simple and reproducible methodology in the laboratory for carrying out the proteomic analysis of human aortic valves and for identifying their component proteins. Conclusions: We developed a simple and reproducible method for extracting protein that can be used with mass spectrometry and that makes it possible to carry out large-scale proteomic analysis of stenotic aortic valves. Furthermore, the methodology will significantly increase our understanding of the valve proteome.
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    Targeting antigens to an invariant epitope of the MHC Class II DR molecule potentiates the immune response to subunit vaccines
    (Virus Research, 2011) Gil Dones, Félix; Pérez-Filgueira, Mariano; Barderas, María G.; Pastor Vargas, Carlos; Alonso, Covadonga; Vivanco, Fernando; Escribano, José M.
    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.
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    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.