Cloning and immunological characterization of the allergen Hel a 2 (profilin) from sunflower pollen

Asturias, Juan A.; Arilla, Maite; Gómez-Bayón, N; Aguirre, Manuel A.; Martı́nez, Alberto; Palácios, Ricardo; Martı́nez, Jorge

doi:10.1016/s0161-5890(98)00036-4

Cited by 54 publications

(34 citation statements)

References 41 publications

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“…Comparison of the deduced amino acid sequence of mugwort pollen profilin revealed high sequence identity with other plant profilin sequences. Pairwise alignments of Art v 4.01 and Art v 4.02 indicated the highest sequence identity with profilins from sunflower (84% and 86% identities; Asturias et al, 1998), olive (77%; Asturias et al, 1997b), Mercurialis annua (75% and 72%; Vallverdu et al, 1998), and tomato (75% and 73%, accession number AJ417553). The lowest homology among profilins from plant origin was found with peanut (68% and 67%; Kleber-Janke et al, 1999) and hazelnut (67% and 69%, acc.…”

Section: Discussionmentioning

confidence: 99%

Molecular and Immunological Characterization of Profilin from Mugwort Pollen

Wopfner¹,

Willeroidee²,

Hebenstreit³

et al. 2002

Biological Chemistry

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In late summer in Europe, pollen of mugwort is one of the major sources of atopic allergens. No information about the complete molecular structure of any mugwort allergen has been published so far. Here we report the isolation and characterization of mugwort pollen cDNA clones coding for two isoforms of the panallergen profilin. Thirty-six percent of the mugwort-allergic patients tested displayed IgE antibodies against natural and recombinant profilin, and no significant differences were observed in the IgE-binding properties of the isoforms. One profilin isoform was purified to homogeneity and detailed structural analysis indicated that the protein exists in solution as dimers and tetramers stabilized by sulfydryl and/or ionic interactions. Profilin monomers were detectable only after exposure of multimers to harsh denaturing conditions. Dimers and tetramers did not significantly differ in their ability to bind serum IgE from mugwort pollen-allergic patients. However, oligomeric forms might have a higher allergenic potential than monomers because larger molecules would have additional epitopes for IgE-mediated histamine release. Profilin isolated from mugwort pollen also formed multimers. Thus, oligomerization is not an artifact resulting from the recombinant production of the allergen. Inhibition experiments showed extensive IgE cross-reactivity of recombinant mugwort profilin and profilin from various pollen and food extracts.

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Section: Discussionmentioning

confidence: 99%

Molecular and Immunological Characterization of Profilin from Mugwort Pollen

Wopfner¹,

Willeroidee²,

Hebenstreit³

et al. 2002

Biological Chemistry

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“…The prevalence of sensitization to profilin was similar among grass (30%) and mugwort (33%) pollen allergic patients [19]. In another study, IgE binding to profilin from sunflower pollen was also about 30% in a population of sunflower-allergic patients from sunflower-growing areas [26]. Profilin seems to give rise to a higher frequency of sensitization among patients allergic to Chenopodium album [27], Mercurialis annua [28] and Phoenix dactylifera [29] pollen, but in some of these studies sensitization to profilin was only determined by IgE binding on immunoblot at the level of profilin’s molecular mass.…”

Section: Profilin: Prevalence Of Sensitizationmentioning

confidence: 99%

Profilins: Mimickers of Allergy or Relevant Allergens?

Santos

Ree

2011

Int Arch Allergy Immunol

144

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Profilins are ubiquitous proteins, present in all eukaryotic cells and identified as allergens in pollen, latex and plant foods. The highly conserved structure justifies the cross-reactive nature of IgE antibodies against plant profilins and their designation as pan-allergens. Primary sensitization to profilin seems to arise from pollen sensitization with later development of cross-reactive IgE antibodies against plant food (and possibly latex) profilins. The role of profilin in inducing allergic symptoms needs to be evaluated and raises important issues in allergy diagnosis due to cross-reactivity. IgE cross-reactivity among profilins is associated with multiple pollen sensitization and with various pollen-food syndromes. In respiratory allergy, sensitization to pollen to which the patient has virtually no environmental exposure has been identified as a manifestation of profilin sensitization. As a food allergen, profilin usually elicits mild reactions, such as oral allergy syndrome, is not modified by processing and is especially important in allergy to some fruits, such as melon, watermelon, banana, tomato, citrus fruit and persimmon. Purified natural and recombinant profilins for in vitro and in vivo allergy tests are helpful in the diagnostic work-up. Herein we review the current state of knowledge about the allergen profilin and its implications in the diagnosis and treatment of allergic diseases. We conclude that, although its role in triggering allergic symptoms is still controversial, profilin is undoubtedly a relevant allergen. As a pan-allergen, profilin is associated with multiple pollen sensitization and pollen-food-latex syndromes that the allergist has to be aware of in order to accomplish an accurate diagnosis and successful treatment of allergic diseases.

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“…Several reports have been published on sensitization and allergy to sunflower seeds (Noyes et al 1979;Axelsson et al 1994) and sensitivity seems to be provoked by birch or mugwort pollen (Vieths et al 2002). Sunflower seed lipid transfer protein has been identified as an allergen (Yagami 2010), while profilin in this species has been shown to be non-allergenic (Asturias et al 1998). In one case, a patient with sunflower seed allergy was not reactive to other plants in the Asterales (mugwort, ragweed, dandelion) or to nuts (almonds, Brazil nuts, peanuts; Yagami 2010).…”

Section: Pistachios and Cashewsmentioning

confidence: 99%

An Evolutionary Perspective on Human Cross-sensitivity to Tree Nut and Seed Allergens

Fisher¹,

Nawrocki²

2015

aliso

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Tree nut allergies are some of the most common and serious allergies in the United States. Patients who are sensitive to nuts or to seeds commonly called nuts are advised to avoid consuming a variety of different species, even though these may be distantly related in terms of their evolutionary history. This is because studies in the literature report that patients often display sensitivity to multiple nut species (crosssensitivity) if they have an existing nut allergy. These reports suggest that cross-sensitivity in patients with nut allergies may be caused by an IgE antibody reacting with epitopes present in the seed proteins of different species (cross-reactivity), for example, if IgE isolated from the serum of a patient were able to bind to both almond and peanut allergens. We hypothesize that allergenic proteins in seeds may have similar amino acid sequences that cause the observed cross-sensitivity. Here, we test the hypothesis that similarity in the protein sequences of allergenic nuts drives cross-sensitivity and cross-reactivity by reconstructing the gene trees of three allergenic seed-storage proteins (vicilin, legumin, and 2S albumin) from species sampled across vascular plants. We generate estimates of their phylogenetic relationships and compare these to the allergen cross-sensitivity and cross-reactivity data that is reported in the literature. In general, evolutionary relationships of the three proteins are congruent with the current understanding of plant species relationships. However, we find little evidence that distantly related nut species reported to be crossreactive share similar vicilin, legumin, or 2S albumin amino acid sequences. Our data thus suggests that features of the proteins other than their amino acid sequences may be driving the cross-reactivity observed during in vitro tests and skin tests. Our results support current treatment guidelines to limit nut and seed consumption if allergies are present in a patient. More studies are necessary to better understand the characteristics of allergenic proteins and patterns of cross-sensitivity in patients who suffer from nut allergies.

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Cloning and immunological characterization of the allergen Hel a 2 (profilin) from sunflower pollen

Cited by 54 publications

References 41 publications

Molecular and Immunological Characterization of Profilin from Mugwort Pollen

Molecular and Immunological Characterization of Profilin from Mugwort Pollen

Profilins: Mimickers of Allergy or Relevant Allergens?

An Evolutionary Perspective on Human Cross-sensitivity to Tree Nut and Seed Allergens

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