Isolation and characterization of an olive allergen‐like protein from lilac pollen

Batanero, Eva; Villalba, Mayte; López-Otı́n, Carlos; Rodrı́guez, Rosalı́a

doi:10.1111/j.1432-1033.1994.tb18728.x

Cited by 44 publications

(54 citation statements)

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“…By using immunoblotting and staining with 20 sera, the same authors visualized only six bands in this extract (10.5, 14.5, 15, 40, 60.5, 68 kD), all of them with a frequency lower than 15%. The protein studied here, Che a 1, would represent an allergen not previously reported, although the high tendency of Ole e 1-like proteins to aggregate [20, 22, 25, 26]could account for bands previously detected around 35–40 and 55 kD [8, 9]. These data, along with our results, suggest the existence of a low measurable IgE reactivity for chenopod allergens, which could agree with the low levels of chenopod-specific IgE present in the sera of allergic patients.…”

Section: Discussionmentioning

confidence: 99%

Identification and Characterization of Che a 1 Allergen from <i>Chenopodium album</i> Pollen

Barderas

Villalba

Lombardero

et al. 2002

Int Arch Allergy Immunol

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Background: Pollinosis to Chenopodium album has been reported, but no data are available on its allergenic proteins. Methods: An allergen from C. album pollen has been isolated by means of gel permeation and reverse-phase high-performance liquid chromatography. Molecular characterization was achieved by concanavalin A reaction, mass spectrometry, Edman degradation and cDNA sequence. Antigenic analyses were performed by immunoblotting, ELISA, and ELISA inhibition, using sera from allergic patients, two Ole e 1-specific monoclonal antibodies and an Ole e 1-specific polyclonal antiserum. Results: The isolated allergen, Che a 1, is a glycoprotein of molecular mass 17.088 kD and 143 amino acid residues, whose sequence exhibits 27–45% identity with known members of the Ole e 1-like protein family. 77% of sera from patients allergic to chenopod pollen were reactive to Che a 1. No correlation was found between the IgE reactivities to Che a 1 and Ole e 1, the major allergens from olive pollen, and both allergens display low, although detectable, IgE and IgG cross-reactivities. Conclusions: Che a 1, a relevant allergen from chenopod pollen, is structurally related to the Ole e 1-like protein family, but exhibits significant differences on its polypeptide sequence that could explain its different antigenic behavior and limited cross-reactivity.

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Section: Discussionmentioning

confidence: 99%

Identification and Characterization of Che a 1 Allergen from <i>Chenopodium album</i> Pollen

Barderas

Villalba

Lombardero

et al. 2002

Int Arch Allergy Immunol

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“…Protein bands on SDS/PAGE were transferred onto nitrocellulose membranes (BioRad) as described [13]. Blots were saturated in 140 mM NaCI/10 mM sodium phosphate, pH 7.2 (NaCl/P,) containing 3 % non-fat milk and 0.1 % Tween 20 (buffer A), and incubated with the human sera diluted tenfold in buffer A, followed by reaction with mouse anti-human IgE (5000-fold diluted).…”

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confidence: 99%

Ole e 3, An Olive‐Tree Allergen, Belongs to a Widespread Family of Pollen Proteins

Batanero

Villalba

Ledesma

et al. 1996

European Journal of Biochemistry

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An allergen has been isolated from a saline extract of olive tree (Olea europaea) pollen. The protein consists of a single polypeptide chain of 9.2-kDa, as determined by mass spectrometry. It contains neither tryptophan nor tyrosine residues, and displays an acidic isoelectric point. The secondary structure of the protein, estimated from the analysis of the circular-dichroism spectrum in the peptide-bond region, is composed of 52% a-helix, 10% a-strand, 29% Sturn and 9% non-regular conformation. The N-terminal end of the protein is blocked. Amino-acid-sequence data have been obtained from peptides produced by CNBr treatment of the native allergen. A partial sequence of 36 amino acids has thus been elucidated. The protein exhibits sequence similarity with pollen allergens from Brassica species and contains a Caz'-binding motif. The isolated protein displays IgE-binding activity against sera of patients allergic to olivetree pollen. It has been named Ole e 3, according to the recommendations of the IUIS Nomenclature Committee. IgG ELISA inhibition assays with polyclonal antibodies specific for Ole e 3 reveal the presence of proteins similar to Ole e 3 in the pollen from non-related plant species, which may explain allergic cross-reactivity processes.Keywords: allergen ; olive pollen ; Olea europaea ; Ole e 3 ; protein characterization.Type-I allergy is a clinical disorder that affects more than 15 % of the human population in developed countries. Olive pollinosis is one of the most important causes of type-I allergy in Mediterranean countries, where the olive tree is widely cultivated [l]. Ole e 1 has been shown to be a major allergen from olive pollen, since the IgE of more than 70% of olive-allergic patients recognize this protein [2-41. In addition to Ole e 1, other allergenic proteins have been detected in saline extracts of the olive pollen 15-71, some of which exhibit low molecular masses. Preliminary studies on these molecules were performed with pools of sera from patients hypersensitive to olive pollen. Lauzurica et al. 121 showed the existence of an IgE-reacting protein of 8 kDa upon SDS/PAGE of the pollen extract. Proteins of 7, 9, 14, 15 and 16 kDa, present in olive pollen, have been immunostained with individual sera from olive allergic patients [8]. However, isolation or molecular characterization was not performed for these allergens.Allergic cross-reactivities have been described among Oleaceae members. such as olive, ash and privet [9-131 as well as between olive-pollen and grass-pollen proteins [8]. In addition to profilin, which is an important and well defined panallergen involved in cross-reactions [ 141, other proteins contained in pollen from different species that have conserved sequences could be responsible for allergic processes in individuals not previously sensitized to a given biological source.In spite of the knowledge of a high number of allergenic structures, little is known about their B-cell and T-cell epitopes and the mechanism of induction of allergy. The protein allergens fre...

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“…1 shows that Zml3 has a significant end-to-end amino acid sequence homology with allergens from olive pollen, Ole el [19,20] (38% identity) and from rye grass, Lol pl 1 [21] (49% identity). A similar degree of sequence similarity was found with an allergen-like protein from lilac [37] and pollen specific proteins from rice [38], Arabidopsis, and tomato [39]. The …”

Section: The Cdna Coding For Zm13 Cross-hybridizes With Rna From Timomentioning

confidence: 77%

Expression of Zm13, a pollen specific maize protein, in Escherichia coli reveals IgE‐binding capacity and allergenic potential

et al. 1996

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Plant proteins belong to the most frequent elicitors of type I allergic symptoms in industrialized countries. Several relevant plant allergens have been found to be either specifically expressed or highly upregulated in mature pollen. The cDNA coding for a pollen specific maize protein, Zml3, shows significant sequence homology with a number of pollen or anther specific proteins from monocot and dicot plants as well as with recently described allergens from olive and rye grass. To test whether the Zml3 protein might possess IgE-binding capacity, Zml3 was expressed in E. coli. The coding region of Zml3 was PCR amplified from a genomic clone and expressed as as a gintathione-S-transferase fusion protein. The recombinant Zml3 fusion protein bound a Zml3 specific rabbit antiserum and reacted with serum IgE from grass pollen allergic patients indicating that Zml3 and homologous proteins represent a family of conserved plant allergens.

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Isolation and characterization of an olive allergen‐like protein from lilac pollen

Cited by 44 publications

References 38 publications

Identification and Characterization of Che a 1 Allergen from <i>Chenopodium album</i> Pollen

Identification and Characterization of Che a 1 Allergen from <i>Chenopodium album</i> Pollen

Ole e 3, An Olive‐Tree Allergen, Belongs to a Widespread Family of Pollen Proteins

Expression of Zm13, a pollen specific maize protein, in Escherichia coli reveals IgE‐binding capacity and allergenic potential

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