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Bilbao, Spain

Ibrahim A.R.N.,Hiroshima University | Kawamoto S.,Hiroshima University | Nishimura M.,Hiroshima University | Pak S.,Hiroshima University | And 6 more authors.
Bioscience, Biotechnology and Biochemistry | Year: 2010

Japanese cedar (Cryptomeria japonica) pollen is a major cause of seasonal rhinitis and conjunctivitis in Japan, and an understanding of its full allergen repertoire is prerequisite for the development of future molecular diagnostics and immunotherapeutic strategies. Here we report the identification of a new C. japonica pollen IgE-binding antigen (CJP-8) homologous to lipid transfer proteins (LTPs), a class of plant cross-reactive allergens found in foods, latex, and pollen grains. The cjp-8 cDNA encodes a 165-amino acid polypeptide possessing the conserved eight cysteines characteristic of plant LTP family members. Escherichia coli-expressed recombinant CJP-8 (r-CJP-8) reacted with IgE antibody from Japanese cedar pollinosis patients at a 37.5% frequency (6/16). Source


Morin M.,University of Salamanca | Asturias J.A.,Bial Aristegui | Dominguez A.,University of Salamanca
FEMS Microbiology Letters | Year: 2012

Allergies affect almost 25% of the population in industrialized countries. Alternaria alternata is known to be a significant source of aeroallergens and sensitization to this mold is a risk factor for the development of wheezing, asthma, and atopic dermatitis. Diagnosis and treatment of allergies requires the production of large amounts of pure and well defined protein. Yarrowia lipolytica, a non-pathogenic ascomycete able to secrete high levels of enzymes that can grow in inexpensive substrates, has been considered a useful host for heterologous gene expression. In the present work, we have developed two vectors for expressing Alt a 1, the most relevant A. alternata allergen, in Y. lipolytica. One vector is autosomal and one is integrative. With both systems, rAlt a 1 was secreted into the culture medium. The immunological characteristics of the purified recombinant allergen were determined by IgE-blot using sera from 42 A. alternata-allergic patients. We have carried out ELISA-inhibition experiments using sera from four patients to compare the IgE-binding capacity of natural and recombinant allergens. Our results show that Y. lipolytica is able to produce a recombinant Alt a 1 which is immunochemically equivalent to the natural counterpart and could be used for immunotherapy and diagnostics.© 2012 Federation of European Microbiological Societies. Published by Blackwell Publishing Ltd. All rights reserved. Source


Gonzalez-Parrado Z.,University of Leon | Fernandez-Gonzalez D.,University of Leon | Fernandez-Gonzalez D.,CNR Institute of atmospheric Sciences and Climate | Camazon B.,Allergy Unit | And 6 more authors.
Annals of Agricultural and Environmental Medicine | Year: 2014

Introduction. Exposure to airborne pollen from certain plants can cause allergic disease, but allergens can also be found in non-pollen-bearing fractions of ambient air. This may explain why the allergic response in susceptible patients does not always coincide with the presence and magnitude of airborne pollen counts. Plantago pollen is an important cause of pollinosis in northern Mediterranean countries, but it is difficult to determine its incidence in allergies because Plantago pollen appears in the atmosphere at the same time as grass pollen. Objective. The study aimed to investigate the relationship between the atmospheric concentration of Pla l 1 aeroallergen and Plantago pollen, and its incidence in a population group. Materials and method. Pollen was sampled using a Hirst-type volumetric trap (Burkard™) and Burkard Cyclone sampler (Burkard™) for Pla l 1 allergen. Allergen was determined with a Pla l 1-specific ELISA. Serum-specific IgE levels to several plant allergens were measured with the EAST system. Results. The aerobiological dynamics of Plantago pollen grains and Pla l 1 did not follow the same trend, whereas the sum of Plantago with some other pollen types showed a more similar behaviour. Of the 118 subjects tested, sera from 52 contained IgE to Plantago pollen, but only 5 were monosensitized. Conclusions. The presence of Pla l 1 in the atmosphere depends not only on Plantago pollen but also on the pollen of other species from the Oleaceae family. Knowledge of the behaviour of allergen Pla l 1 in the atmosphere can help understand better asthma exacerbations associated with aeroallergens. Source


Martin-Munoz M.F.,Allergy Service | Bartolome B.,Bial Aristegui | Caminoa M.,Allergy Service | Bobolea I.,Allergy Service | And 2 more authors.
Allergologia et Immunopathologia | Year: 2010

Background: Bee pollen has been proposed as a food supplement, but it can be a dangerous food for people with allergy. We study an allergic reaction after ingestion of bee pollen in a 4-year-old boy who had developed rhinitis in the last spring and autumn. Methods: We performed a prick-by-prick test with bee pollen and skin prick tests with the most important local pollens, house dust mites, common fungi, and animal danders. The levels of serum tryptase, serum total IgE and specific IgE against bee venom and local pollen extracts were determined. The composition of the bee pollen was analysed and SDS-PAGE immunoblotting and blotting-inhibition were carried out. Results: Prick tests were positive to bee pollen and all local pollens extracts and negative to any other allergen sources. The bee pollen sample contained pollens from Quercus genus, and Asteraceae (Compositae) and Rosaceae families. Total IgE was 435. kU/l. Serum specific IgE to bee pollen was 6. kU/l and greater than 0.35. kU/L against pollens from Artemisia vulgaris, Taraxacum officinalis, Cupressus arizonica, Olea europaea, Platanus acerifolia and Lolium perenne as well as to n Art v 1 and other pollen marker allergens. Tryptase level was 3.5. mcg/mL. SDS-PAGE immunoblotting-inhibition points to Asteraceae pollen as the possible cause of the allergic reaction. Conclusion: Foods derived from bees can be dangerous to people with allergy to pollen. © 2009 SEICAP. Source


Sanchez-Lopez J.,University of Barcelona | Sanchez-Lopez J.,Center for Biomedical Investigation in Respiratory Diseases | Asturias J.A.,Bial Aristegui | Enrique E.,Hospital General de Castellon | And 3 more authors.
Journal of Investigational Allergology and Clinical Immunology | Year: 2011

Background: Lipid transfer proteins (LTP) are responsible for systemic manifestations in food allergy. Their relationship with pollinosis is not clear. In our area, many patients allergic to multiple LTP-containing foods present pollinosis due to Cupressus arizonica. Methods: We selected 6 patients with cypress pollinosis and food allergy to peach. Skin prick tests (SPT) were performed for pollens (grass, cypress, wall pellitory, plane tree, and olive tree) and plant foods (hazelnut, kiwifruit, peach peel, maize, wheat, peanut, lettuce, apple, mustard, and melon). In vitro assays included specifi c immunoglobulin (Ig) E to C arizonica and peach LTP (Pru p 3), enzyme allergosorbent test (EAST) inhibition, immunoblotting, immunoblotting-inhibition, and immunocytochemical techniques for the detection of Pru p 3-like LTP in cypress pollen grains. Results: SPT were positive for C arizonica, peach, lettuce, mustard, and hazelnut in all patients. Specifi c IgE to C arizonica and Pru p 3 was positive in all but 1 patient, whose Pru p 3 IgE was negative. Immunoblotting under nonreducing conditions with C arizonica extract and patients' sera showed a band at 14-15 kDa that was inhibited by Pru p 3. Pru p 3 partially inhibited the C arizonica pollen extract in EASTinhibition. Pru p 3-like LTP was localized in the cytoplasm and walls of C arizonica pollen grains. Conclusion: A 15-kDa allergen in C arizonica pollen was found in a group of patients presenting peach allergy and respiratory symptoms to cypress. In vitro tests and immunocytochemical techniques indicate that this protein is an LTP. © 2011 Esmon Publicidad. Source

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