0000000000408257

AUTHOR

G. Di Felice

showing 2 related works from this author

The major allergen of the Parietaria pollen contains an LPS-binding region with immuno-modulatory activity

2013

Background The major allergens in Parietaria pollen, Par j 1 and Par j 2, have been identified as lipid transfer proteins. The family of the Par j 1 allergens is composed of two isoforms, which differ by the presence of a 37 amino acid peptide (Par37) exclusive to the Par j 1.0101 isoform. The goal of this study was to elucidate the biological properties of the Par37 peptide. Methods In silico analysis, spectrofluorimetric experiments and in vitro cell culture assays were used to identify the biological properties of Par37. In addition, a mouse model of sensitization was used to study the influence of Par37 in the murine immune response. Results In silico analysis predicted that Par37 displ…

LipopolysaccharidesGene isoformParietariaIn silicoMolecular Sequence DataImmunologySettore BIO/11 - Biologia MolecolarePeptideBiologyAntibodiesInterferon-gammaMiceIn vivoAnimalsHumansImmunologic FactorsImmunology and AllergyAmino Acid SequencePlant ProteinsPolymyxin Bchemistry.chemical_classificationanimal modelallergens; animal models; environment; pollens.Allergensbiology.organism_classificationIn vitroAmino acidParietariachemistryBiochemistryLeukocytes MononuclearCytokinesPollenpollens.FemalePeptidesenvironmentSequence AlignmentPlant lipid transfer proteinsSpleenallergenProtein Binding
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A Hybrid Expressing Genetically Engineered Major Allergens of the <i>Parietaria</i> Pollen as a Tool for Specific Allergy Vaccination

2006

<i>Background:</i> Allergy is an immunological disorder affecting about 25% of the population living in the industrialized countries. Specific immunotherapy is the only treatment with a long-lasting relief of allergic symptoms and able to reduce the risk of developing new allergic sensitizations and inhibiting the development of clinical asthma in children treated for allergic rhinitis. <i>Methods:</i> By means of DNA recombinant technology, we were able to design a head to tail dimer expressing disulphide bond variants of the major allergen of the <i>Parietaria </i>pollen. IgE binding activity was studied by Western blot, ELISA inhibition assays and the …

Allergyeducation.field_of_studyParietariabiologyGenetically engineeredImmunologyPopulationSpecific immunotherapyGeneral Medicinebiology.organism_classificationmedicine.disease_causemedicine.diseaseVaccinationAllergenPollenImmunologymedicineImmunology and AllergyeducationInternational Archives of Allergy and Immunology
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