Olive (olea europea) pollen allergens—II Isolation and characterization of two major antigens

Lauzurica, Pilar; Maruri, N.; Galocha, Begoña; González, Juan Carlos; Diaz, Roger; Palomino, Pilar; Hernández, Dolores; Garcı́a, R.; Lahoz, Carlos

doi:10.1016/0161-5890(88)90028-4

Cited by 57 publications

(41 citation statements)

References 20 publications

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“…Ole e 3 may correspond to the olive allergen detected by Lauzurica et al (21, because of the similarity of its reported molecular mass (8 kDa) and PI (4.5). However, the iodination of tyrosines described for that protein [2] is not possible for Ole e 3 since it lacks this type of residue. The possibility of other allergens of 8 -13 kDa cannot be discarded, since a small percentage of sera, which are sensitive on immunoblotting to proteins of this molecular mass, did not react with Ole e 3 in ELISA.…”

Section: Discussionmentioning

confidence: 99%

“…This allergen was characterized, cloned and expressed in Escherichia coli [4,26,281. Although several allergenic protein bands have been detected in olive pollen by immunoblotting assays [2,, the proteins have not been isolated.…”

Section: Discussionmentioning

confidence: 99%

“…An ELISA titration with fixed Ole e 3 of this antiserum is shown in ELISA inhibition of the binding to wells coated with Ole e 3 was measured by means of a rabbit antiserum specific for Ole e 3 previously incubated with pollen extracts (500 pg or 50 pg total protein, calculated by the method of Lowry et al [20]) from (1) olive tree, (2) mugwort, (3) birch, (4) ryegrass, ( 5 ) rose, (6) pine, (7) cypress. Mustardseed saline extract (8) was used as control.…”

Section: ---I-p-ev-h--------p--f--f---t-gr--l---------p--vt-mentioning

confidence: 99%

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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

115

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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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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: ---I-p-ev-h--------p--f--f---t-gr--l---------p--vt-mentioning

confidence: 99%

See 1 more Smart Citation

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

115

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“…Once the pollen grains come in contact with an aqueous environment, such as the mucus layer in the lung airways, they swell and split and release many proteins (26). Pollen proteins that are allergens and elicit an immunological response have been studied abundantly (27)(28)(29)(30)(31). However, some of these allergens in fact appear to have, in addition, enzymatic functions displaying lyase (32), esterase (33), and polygalacturonase (34) activities.…”

Section: Discussionmentioning

confidence: 99%

Purification and Characterization of a Novel Peptidase (IImes) from Mesquite (Prosopis velutina) Pollen

Matheson

Travis

1998

Journal of Biological Chemistry

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Although the mesquite plant (Prosopis velutina) is not as widely distributed as some other allergenic species, its pollen can induce serious pollinosis in areas where it is localized. We previously isolated and characterized a peptidase from mesquite pollen with trypsin-like specificity (peptidase I mes ) (Matheson, N., Schmidt, J., and Travis, J. (1995) Am. J. Respir. Cell Mol. Biol. 12, 441-448). Now we have characterized a second enzyme with specificity for hydrophobic residues (mesquite pollen peptidase II mes ). This enzyme has a molecular mass near 92 kDa and activity that was not affected by reducing or chelating agents but was inhibited by specific synthetic serine proteinase inhibitors and the aminopeptidase inhibitor bestatin. However, it was not inhibited by human plasma proteinase inhibitors, nor did it inactivate any of those tested. The enzyme possessed amidolytic activity against p-nitroanilide substrates most effectively after alanine residues and also displayed aminopeptidase activity against non-p-nitroanilide peptides with a preference for phenylalanine. This specificity for hydrophobic amino acid residues was corroborated by inhibition studies with chloromethyl ketone and organophosphonate inhibitors. More interesting from a physiological point of view is that the bioactive peptides, angiotensins I and II and vasoactive intestinal peptide, were also hydrolyzed rapidly, indicating an ability of peptidase II mes to act also as an oligopeptidase. Because these bioactive peptides play a role in the inflammatory responses in allergic asthma, our data suggest that the purified mesquite pollen peptidase II mes may be involved in the degradation of neuro-and vasoactive peptides during pollen-initiated allergic reactions.Asthma is an allergic inflammation of the lungs which can occur after allergen sensitization. Such inflammatory responses are normally meant to defend against invading organisms or particulates or to effect tissue repair and are thus beneficial; however, in asthma, the response becomes exaggerated (perhaps because of a hereditary predisposition (1)), leading to adverse effects on the airways (2). Macrophages phagocytize the allergens introduced to the lungs by exposure to various environmental irritants such as dust, pollutants, and pollen, and process them to smaller fragments. As antigenpresenting cells, they then activate T-cells (3, 4) to stimulate B-cells to produce IgE. This immunoglobulin, when bound to a specific allergen, in turn, stimulates and activates several alveolar cell types to produce the many mediators of inflammation: histamine, prostaglandins, leukotrienes, cytokines, neutral proteases, active oxygen species, and chemoattractants (5). The interaction of these mediators leads to the pathology of asthma, including bronchoconstriction, hypertrophy of airway smooth muscle, vasodilation, submucosal edema, and mucus hypersecretion (6). Also, the mucociliary apparatus becomes dysfunctional, reducing the clearance of inhaled particulates. Epithelial cells lining the airwa...

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“…Among seasonal allergies, olivetree(O1ea eurupaea)-pollen allergy is a major health problem for humans throughout the mediterranean area [ 1 -31. At least two major allergens of different size (20.0 kDa and 8.0 kDa) are present in an aqueous extract of olive tree pollen [4]. The allergenic protein of 20.0 kDa, Ole e I (according to Correspondence to R. Rodriguez,…”

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confidence: 99%

The amino acid sequence of Ole e I, the major allergen from olive tree (Olea europaea) pollen

Villalba

Batanero

López-Otı́n

et al. 1993

European Journal of Biochemistry

137

188

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The complete primary structure of the major allergen from Olea europaea (olive tree) pollen, Ole e I (IUIS nomenclature), has been determined. The amino acid sequence was established by automated Edman degradation of the reduced and alkylated molecule as well as of selected fragments obtained by proteolytic digestions. Ole e I contains a single polypeptide chain of 145 amino acid residues with a calculated molecular mass of 16331 Da. No free sulfhydryl groups have been detected in the native protein. The molecule contains a putative glycosylation site. A high degree of microheterogeneity has been observed, mainly centered in the first 33% of the molecule. Comparison of Ole e I sequence with protein sequence databases showed no similarity with other known allergens. However, it has a 36% and 38% sequence identity with the putative polypeptide structures, deduced, respectively, from nucleotide sequences of genes isolated from tomato anthers and corn pollen, which have been suggested to be involved in the growing of the pollen tube. Therefore, the olive tree allergen may be a constitutive protein of the pollen involved in reproductive functions.Nowadays, about 15-20% of the human population suffer from some sort of allergy. The exposure by inhalation, ingestion, injection or contact with numerous antigens from diverse sources leads to this hypersensitive reaction in those individuals genetically predisposed. The most common sources of allergens include pollen from different weeds, trees and grasses, as well as molds, animal dander, insect venoms, house dust mites and foods. Moreover, each source usually contains multiple allergens responsible for the hypersensitivity against a particular species. Pollen allergies are dependent on environmental aspects such as geographical and seasonal conditions. Among seasonal allergies, olivetree(O1ea eurupaea)-pollen allergy is a major health problem for humans throughout the mediterranean area [ 1 -31. At least two major allergens of different size (20.0 kDa and 8.0 kDa) are present in an aqueous extract of olive tree pollen [4]. The allergenic protein of 20.0 kDa, Ole e I (according to Correspondence to R. Rodriguez,

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Olive (olea europea) pollen allergens—II Isolation and characterization of two major antigens

Cited by 57 publications

References 20 publications

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

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

Purification and Characterization of a Novel Peptidase (IImes) from Mesquite (Prosopis velutina) Pollen

The amino acid sequence of Ole e I, the major allergen from olive tree (Olea europaea) pollen

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