The Spectrum of Allergens in Ragweed and Mugwort Pollen

Wopfner, Nicole; Gadermaier, Gabriele; Egger, Matthias; Asero, Riccardo; Ebner, Christof; Jahn‐Schmid, Beatrice; Ferreira, Fátima

doi:10.1159/000089188

Cited by 158 publications

(150 citation statements)

References 99 publications

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“…homology and cross-reactivity to mugwort pollen proteins (3,4,6,7). The presence of ␤-Ara patches in Art v 1 but not in Amb a 4 indicates the occurrence of a possibly unique epitope in mugwort pollen that would allow to differentiate sensitization to these pollens, at least for some patients.…”

Section: Discussionmentioning

confidence: 99%

A New Allergen from Ragweed (Ambrosia artemisiifolia) with Homology to Art v 1 from Mugwort

Léonard

Wopfner

Pabst

et al. 2010

Journal of Biological Chemistry

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Art v 1, the major pollen allergen of the composite plant mugwort (Artemisia vulgaris) has been identified recently as a thionin-like protein with a bulky arabinogalactan-protein moiety. A close relative of mugwort, ragweed (Ambrosia artemisiifolia) is an important allergen source in North America, and, since 1990, ragweed has become a growing health concern in Europe as well. Weed pollen-sensitized patients demonstrated IgE reactivity to a ragweed pollen protein of apparently 29 -31 kDa. This reaction could be inhibited by the mugwort allergen Art v 1. The purified ragweed pollen protein consisted of a 57-amino acidlong defensin-like domain with high homology to Art v 1 and a C-terminal proline-rich domain. This part contained hydroxyproline-linked arabinogalactan chains with one galactose and 5 to 20 and more ␣-arabinofuranosyl residues with some ␤-arabinoses in terminal positions as revealed by high field NMR. The ragweed protein contained only small amounts of the single hydroxyproline-linked ␤-arabinosyl residues, which form an important IgE binding determinant in Art v 1. cDNA clones for this protein were obtained from ragweed flowers. Immunological characterization revealed that the recombinant ragweed protein reacted with >30% of the weed pollen allergic patients. Therefore, this protein from ragweed pollen constitutes a novel important ragweed allergen and has been designated Amb a 4.The pollen of common ragweed (Ambrosia artemisiifolia) is a major cause of hay fever and associated asthma in Northern America. During the past few decades, ragweed has started to spread in many parts of central Europe, where it has become a serious health problem in the sensitized population. Several initiatives have formed to prevent further spread in e.g. France, Austria or southern Germany. The Compositae (or Asteraceae) family is one of the largest families of flowering plants, but only a few are important allergenic sources. These include Ambrosia (ragweed), Artemisia (mugwort), Helianthus (sunflower), and Parthenium (feverfew). It was further demonstrated that sera of mugwort allergic patients show considerable cross-reactivity with ragweed pollen extracts (1, 2). IgE-binding to mugwort allergens in immunoblots was inhibited effectively by ragweed pollen extract (1), which indicates close homology of the essential allergens in ragweed and mugwort pollen. So far, six groups of allergens have been identified in ragweed pollen. Most patients were classified as ragweed allergic if they reacted with the pectate lyases of the Amb a 1/2 group (3, 4). The homologous pectate lyase Art v 6 in mugwort has been reported to play only a minor role in allergic disease. Amb a 6 (lipid transfer protein), Amb a 8 (profilin), Amb a 9 and Amb a 10 (both calcium-binding proteins) are small proteins belonging to the group of well known cross-reactive pan-allergens (1, 4 -8). Amb a 7 and the fragment Amb a 3 are plastocyanins and are described only as minor ragweed allergens (9).In mugwort pollen, the major allergen is Art v 1, a protein w...

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Section: Discussionmentioning

confidence: 99%

A New Allergen from Ragweed (Ambrosia artemisiifolia) with Homology to Art v 1 from Mugwort

Léonard

Wopfner

Pabst

et al. 2010

Journal of Biological Chemistry

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“…However, for specific immunotherapy, it is of relevance whether these patients are actually sensitized to both weeds (cosensitized) or whether they are sensitized to one weed and cross-react to the other weed (crosssensitized) (11). Panallergens present in ragweed and mugwort pollen only to a minor extent account for the cross-reactivity of IgE Abs (10,(12)(13)(14). Amb a 1 is another conceivable candidate molecule for causing cross-reactivity, because mugwort pollen contains a homologous allergen, Art v 6, with 65% amino acid sequence identity and 85% amino acid similarity (12,13,15).…”

mentioning

confidence: 99%

“…Panallergens present in ragweed and mugwort pollen only to a minor extent account for the cross-reactivity of IgE Abs (10,(12)(13)(14). Amb a 1 is another conceivable candidate molecule for causing cross-reactivity, because mugwort pollen contains a homologous allergen, Art v 6, with 65% amino acid sequence identity and 85% amino acid similarity (12,13,15). Previous attempts to investigate IgE cross-reactivity of Amb a 1 and Art v 6 have been hampered by the lack of properly folded, IgE-reactive recombinant or natural molecules (5,16,17).…”

mentioning

confidence: 99%

Humoral and Cellular Cross-Reactivity between Amb a 1, the Major Ragweed Pollen Allergen, and Its Mugwort Homolog Art v 6

Jahn‐Schmid

Hauser

Wopfner

et al. 2012

The Journal of Immunology

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Ragweed and mugwort are closely related weeds that represent the major cause of pollen allergy in late summer. Concomitant sensitization and clinical cross-reactivity frequently occur in subjects who are coexposed to both pollen species, and have implications for diagnosis and specific immunotherapy. Molecules involved in this cross-reactivity might be Amb a 1, the major ragweed pollen allergen, and Art v 6, a highly homologous allergen from mugwort. Therefore, we investigated the IgE and T cell response to Art v 6 of 60 weed pollen-allergic patients and assessed its immunological cross-reactivity with Amb a 1. Results of ELISA inhibition experiments suggested that both allergens are largely cross-reactive, but Amb a 1 possesses more IgE epitopes than Art v 6. In patients with IgE to both allergens, Amb a 1-induced T cell lines and clones responded weakly to Art v 6. Moreover, Art v 6-induced T cell lines responded stronger to Amb a 1. T cell epitope mapping of Art v 6 revealed that it contains only a few cross-reactive epitopes, which is opposed to the multiple T cell-activating regions present in Amb a 1. In summary, Amb a 1 can elicit more diverse allergen-specific IgE and T cell responses than Art v 6 and dominates the cross-reactivity with its homolog. Nevertheless, Art v 6 can act as a primary sensitizing allergen in areas with high mugwort pollen exposure, and consequently may facilitate sensitization to Amb a 1 by epitope cross-recognition of T and B cells.

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“…It has been reported that about 20 to 36% of all pollensensitized patients recognize profilin [82,85]. Since profilin specific IgE cross-reacts with homologues from virtually every plant source, sensitization to these allergens is a risk factor for allergic reactions to multiple pollen sources and for the development of class II food allergy [86].…”

Section: Profilinsmentioning

confidence: 99%

Molecular Properties of Plant Food Allergens: A Current Classification into Protein Families

Hauser¹,

Egger²,

Wallner³

et al. 2008

TOIJ

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So far the allergen list of the International Union of Immunological Societies (IUIS) allergen nomenclature subcommittee comprises 130 plant-derived food allergens. Based on sequence homology these allergens can be classified into only 27 out of 9,000 known protein families according to the Allfam database. These families comprise the prolamin and cupin superfamilies, pathogenesis related proteins, profilins, thaumatin-like proteins, oleosins, expansins, a number of enzymes and protease inhibitors among others. The classification on structural and thus biochemical and functional similarities will provide a new outlook on the molecules and might contribute to answer the question about allergenicity of different proteins. This will help to define clinical relevant allergenic molecules and explain cross-reactive phenomena between single food allergen sources as well as between food allergens and allergenic molecules of other origins (e.g. pollen).

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The Spectrum of Allergens in Ragweed and Mugwort Pollen

Cited by 158 publications

References 99 publications

A New Allergen from Ragweed (Ambrosia artemisiifolia) with Homology to Art v 1 from Mugwort

A New Allergen from Ragweed (Ambrosia artemisiifolia) with Homology to Art v 1 from Mugwort

Humoral and Cellular Cross-Reactivity between Amb a 1, the Major Ragweed Pollen Allergen, and Its Mugwort Homolog Art v 6

Molecular Properties of Plant Food Allergens: A Current Classification into Protein Families

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