Array‐based profiling of ragweed and mugwort pollen allergens

Gadermaier, Gabriele; Wopfner, Nicole; Wallner, Michael; Egger, Matthias; Didierlaurent, A.; Regl, Gerhard; Aberger, Fritz; Lang, Roland; Ferreira, Fátima; Hawranek, Thomas

doi:10.1111/j.1398-9995.2008.01780.x

Cited by 89 publications

(66 citation statements)

References 19 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%

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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%

“…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.…”

mentioning

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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“…As of today, 10 short ragweed pollen allergens have been registered by the International Union of Immunological Societies (6). Among them, two are considered as major allergens, including the pectate lyase Amb a 1 and the cysteine protease Amb a 11, which are recognized by serum IgE of 90% (7,8) and 66% (9), respectively, of ragweed pollen-allergic patients. We recently identified natural Amb a 11 as a 28-kDa glycosylated protein displaying amino acid sequence identities with other allergens belonging to the C1A cysteine protease family, such as Der p 1 and Der f 1 (from house dust mite Dermatophagoides sp.…”

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confidence: 99%

Structural and Functional Characterization of the Major Allergen Amb a 11 from Short Ragweed Pollen

Groeme¹,

Airouche²,

Kopečný³

et al. 2016

Journal of Biological Chemistry

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Allergy to the short ragweed (Ambrosia artemisiifolia) pollen is a major health problem. The ragweed allergen repertoire has been recently expanded with the identification of Amb a 11, a new major allergen belonging to the cysteine protease family. To better characterize Amb a 11, a recombinant proform of the molecule with a preserved active site was produced in Escherichia coli, refolded, and processed in vitro into a mature enzyme. The enzymatic activity is revealed by maturation following an autocatalytic processing resulting in the cleavage of both N-and C-terminal propeptides. The 2.05-Å resolution crystal structure of pro-Amb a 11 shows an overall typical C1A cysteine protease fold with a network of molecular interactions between the N-terminal propeptide and the catalytic triad of the enzyme. The allergenicity of Amb a 11 was confirmed in a murine sensitization model, resulting in airway inflammation, production of serum IgEs, and induction of Th2 immune responses. Of note, inflammatory responses were higher with the mature form, demonstrating that the cysteine protease activity critically contributes to the allergenicity of the molecule. Collectively, our results clearly demonstrate that Amb a 11 is a bona fide cysteine protease exhibiting a strong allergenicity. As such, it should be considered as an important molecule for diagnosis and immunotherapy of ragweed pollen allergy.

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“…In Austria, it increased from 8.5% in 1997 to 17.5% of pollen allergies in 2007 (3), and around Milan (Italy), ragweed today is the second most frequent cause of respiratory allergy next to grass pollen (1). The major allergen in ragweed pollen, Amb a 1, is a highly allergenic molecule that is recognized by .90% of ragweed-sensitized individuals (4,5) and accounts for .90% of the allergenic activity in ragweed pollen (6). It is a 38-kDa nonglycosylated protein that belongs to the family of pectate-lyase proteins.…”

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confidence: 99%

“…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). Therefore, we intended to define the IgE cross-reactivity between Amb a 1 and Art v 6 by using the purified natural weed pollen allergens.…”

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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Array‐based profiling of ragweed and mugwort pollen allergens

Abstract: Molecule-based diagnosis provides essential information for the differential diagnosis between ragweed and mugwort pollen allergy and for the selection of the appropriate allergen source for specific immunotherapy.

Cited by 89 publications

References 19 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

Structural and Functional Characterization of the Major Allergen Amb a 11 from Short Ragweed Pollen

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

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