timothy-grass/proline

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Hypoallergenic mutants of the Timothy grass pollen allergen Phl p 5 generated by proline mutations.

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BACKGROUND Phl p 5 is a major allergen of Timothy grass (Phleum pratense). A recombinant native Phl p 5 has already been used in clinical trials of allergen-specific immunotherapy as a component of a cocktail of allergens. Recombinant hypoallergenic allergens should further improve the treatment by

In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress.

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An association between pollution (e.g., from traffic emissions) and the increased prevalence of respiratory allergies has been observed. Field-realistic exposure studies provide the most relevant assessment of the effects of the intensity and diversity of urban and industrial contamination on pollen

Post-translational modifications influence IgE reactivity to the major allergen Phl p 1 of timothy grass pollen.

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BACKGROUND Grass group I consists of very potent allergenic components which are found in the pollen of all temperate grasses. Several post-translational modifications are predicted from the cDNA data. OBJECTIVE The aim of this study was to identify sequential IgE-binding sites on the allergen Phl p

Characterization of profilin polymorphism in pollen with a focus on multifunctionality.

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Profilin, a multigene family involved in actin dynamics, is a multiple partners-interacting protein, as regard of the presence of at least of three binding domains encompassing actin, phosphoinositide lipids, and poly-L-proline interacting patches. In addition, pollen profilins are important

Recombinant DNA technology in allergology: cloning and expression of plant profilins.

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Profilin, an ubiquitous protein involved in eukaryotic cytoskeleton regulation, has been previously described as allergen in grasses, weeds and trees and in many fruits and vegetables, and it is in part responsible for cross-reactivities pollen and food allergic patients. Completed cDNA clones

Comparison of natural and recombinant isoforms of grass pollen allergens.

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More than 95% of grass pollen allergic patients possess IgE antibodies against grass group I, a heterogeneous group of glycoproteins found in all temperate grasses. We studied the structural variability of the group I allergens in single species and among different grasses. By 2-DE blotting using

Cross-reactivities between date palm (Phoenix dactylifera L.) polypeptides and foods implicated in the oral allergy syndrome.

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BACKGROUND Date fruit and pollen antigens share a number of cross-reactive epitopes. Date pollen has been shown to cross-react with antigens from Artemisia, cultivated rye (Secale cereale), Timothy grass (Phleum pratense), Sydney golden wattle (Acacia longifolia) and Bermuda grass (Cynodon dactylon)

High-level expression in Escherichia coli and purification of recombinant plant profilins: comparison of IgE-binding capacity and allergenic activity.

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Because of their structural similarity and ubiquitous distribution as actin binding proteins, plant profilins represent important cross-reactive allergens for almost 20% of patients suffering from Type I allergy to pollen and other plant products. The cDNAs coding for three birch profilin variants

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