Person:
Batanero Cremades, Eva

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First Name
Eva
Last Name
Batanero Cremades
Affiliation
Universidad Complutense de Madrid
Faculty / Institute
Ciencias Químicas
Department
Bioquímica y Biología Molecular
Area
Bioquímica y Biología Molecular
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Search Results

Now showing 1 - 5 of 5
  • Publication
    Characterization of Profilin and Polcalcin Panallergens From Ash Pollen
    (Esmon Publicidad, 2014) Mas García, Salvador; Garrido Arandia, María; Batanero Cremades, Eva; Purohit, A.; Pauli, G.; Rodríguez García, Rosalía; Barderas Manchado, Rodrigo; Villalba Díaz, Mayte
    Background: Ash (Fraxinus excelsior) is an important source of allergenic pollen in temperate areas of Europe. Profilin and polcalcin are 2 important panallergens involved in cross-reactivity between different sources. Objective: To clone and produce Fra e 2 (profilin) and Fra e 3 (polcalcin) as recombinant proteins and evaluate their immunological properties using the natural forms obtained from ash pollen. Methods: Total RNA from ash pollen was used as a template to obtain the specific complementary DNA (cDNA) sequences of the 2 panallergens. The cDNA-encoding sequences were cloned into the pET11b expression vector and used to transform BL21 (DE3) Escherichia coli cells. Proteins were expressed, purified by chromatography, and characterized structurally by circular dichroism, mass spectrometry, and immunologically by western blot and ELISA using profilin and polcalcin polyclonal antibodies and human sera from ash pollen–sensitized patients. Results: Profilin and polcalcin amino acid sequences from ash pollen showed a high degree of identity with homologous allergens from different sources. The cDNA-encoding allergen sequences were expressed as nonfusion recombinant proteins and purified to homogeneity. Secondary structure values were similar to those obtained from other members of these families. Allergenic Properties of the recombinant allergens were observed to be equivalent to those of the natural counterparts of F excelsior pollen.Conclusions: Fra e 2 and Fra e 3 recombinant allergens might be used in clinical diagnosis to determine profilin- and polcalcin-specific IgE levels present in the sera of ash pollen–sensitized patients, thus facilitating the finding of the sensitizing source in areas with complex sensitization profiles.
  • Publication
    Pollensomes as natural vehicles for pollen allergens
    (American Association of Immunologists, 2015-07-15) Prado, Noela; De Linares, C.; Sanz, M.L.; Gamboa, P.; Villalba Díaz, Mayte; Rodríguez García, Rosalía; Batanero Cremades, Eva
    Olive (Olea europaea) pollen constitutes one of the most important allergen sources in the Mediterranean countries and some areas of the United States, South Africa, and Australia. Recently, we provided evidence that olive pollen releases nanovesicles of respirable size, named generically pollensomes, during in vitro germination. Olive pollensomes contain allergens, such as Ole e 1, Ole e 11, and Ole e 12, suggesting a possible role in allergy. The aim of this study was to assess the contribution of pollensomes to the allergic reaction. We show that pollensomes exhibit allergenic activity in terms of patients' IgE-binding capacity, human basophil activation, and positive skin reaction in sensitized patients. Furthermore, allergen-containing pollensomes have been isolated from three clinically relevant nonphylogenetically related species: birch (Betula verrucosa), pine (Pinus sylvestris), and ryegrass (Lolium perenne). Most interesting, pollensomes were isolated from aerobiological samples collected with an eight-stage cascade impactor collector, indicating that pollensomes secretion is a naturally occurring phenomenon. Our findings indicate that pollensomes may represent widespread vehicles for pollen allergens, with potential implications in the allergic reaction.
  • Publication
    A Deletion Variant of the Aspergillus fumigatus Ribotoxin Asp f 1 Induces an Attenuated Airway Inflammatory Response in a Mouse Model of Sensitization
    (Esmon Publicidad, 2010-03) Álvarez García, Elisa; Batanero Cremades, Eva; García Fernández, Rosa; Villalba Díaz, Mayte; Gavilanes, José G.; Martínez del Pozo, Álvaro
    α-Sarcin is a natural variant of Asp f 1 produced by the nonpathogenic fungus Aspergillus giganteus. Both proteins show a sequence identity of 87% and almost identical 3-dimensional structures. α-Sarcin Δ(7-22) is a deletion mutant that displays reduced immunoglobulin (Ig) E reactivity and is much less cytotoxic than wild-type proteins against human transformed cells. Objective: A murine model of sensitization to Asp f 1 was established to test the response elicited by this α-sarcin Δ(7-22) deletion mutant. Methods: BALB/c mice were treated intraperitoneally with different mixtures of recombinant wild-type Asp f 1 and/or a suspension of a commercially available A fumigatus standard extract. Mice were then intranasally challenged with Asp f 1 or α-sarcin Δ(7-22). Sera were collected for subsequent measurement of Ig levels and histological analysis of the nostrils and lungs. Results: Sensitization to Asp f 1 was successful only when the purifi ed protein was fi rst administered together with the A fumigatus suspension. The model was characterized by elevated levels of total IgE in serum and histological lesions in the lungs and nostrils. These symptoms were less severe when the deletion variant was the protein administered, thus confi rming in vivo its lower toxic character. Conclusions: An easily reproducible mouse model of A fumigatus Asp f 1 sensitization was established. This model revealed α-sarcin Δ (7-22) to be a potential candidate for immunotherapy.
  • Publication
    Ash pollen immunoproteomics: Identification, immunologic characterization, and sequencing of 6 new allergens
    (Elsevier, 2014) Mas García, Salvador; Torres Pardo, María; Garrido-Arandia, María; Salamanca, Guillermo; Castro, Lourdes; Barral, Patricia; Purohit, Ashok; Pauli, Gabrielle; Rodríguez García, Rosalía; Batanero Cremades, Eva; Barderas Manchado, Rodrigo; Villalba Díaz, Mayte
    Immunoproteomics, IgE-inhibition assays and cDNA-cloning reveals that ash and olive allergenic protein profiles are mostly equivalent, thus explaining their high cross reactivity. Our data suggest simplifying diagnosis of patients by using indistinctly ash or olive pollen.
  • Publication
    Allium porrum Extract Decreases Effector Cell Degranulation and Modulates Airway Epithelial Cell Function
    (MDPI, 2019-06-08) Benedé, Sara; Gradillas, Ana; Villalba Díaz, Mayte; Batanero Cremades, Eva
    Allium genus plants, such as leek (Allium porrum), are rich sources of anti-inflammatory and anti-oxidant secondary metabolites; this is of interest because it demonstrates their suitability as pharmacological alternatives for inflammatory processes, including allergy treatment. The composition of methanolic leek extract (LE) was analyzed by GC–MS and LC–IT/MS, and the total phenolic content and antioxidant capacity were quantified by colorimetric methods. Its pharmacological potential was analyzed in human bronchial epithelial Calu-3 cells, human mast cells LAD2, and humanized rat basophiles RBL-2H3. LE exhibited a cytotoxic effect on Calu-3 cells and HumRBL-2H3 cells only at high concentrations and in a dose-dependent manner. Moreover, LE decreased the degranulation of LAD2 and HumRBL-2H3 cells. LE treatment also significantly prevented alterations in transepithelial electrical resistance values and mRNA levels of glutathione-S-transferase (GST), c-Jun, and NFκB after treatment with H2O2 in ALI-cultured Calu-3 cells. Finally, ALI-cultured Calu-3 cells treated with LE showed lower permeability to Ole e 1 compared to untreated cells. A reduction in IL-6 secretion in ALI-cultured Calu-3 cells treated with LE was also observed. In summary, the results obtained in this work suggest that A. porrum extract may have potential anti-allergic effects due to its antioxidant and anti-inflammatory properties. This study provides several important insights into how LE can protect against allergy.