Characterization of a birch pollen allergen, Bet v III, representing a novel class of Ca2+ binding proteins: specific expression in mature pollen and dependence of patients' IgE binding on protein-bound Ca2+.

Seiberler, Susanne; Scheiner, Otto; Kraft, Dietrich; Lonsdale, David; Valenta, Rudolf

doi:10.1002/j.1460-2075.1994.tb06654.x

Cited by 118 publications

(101 citation statements)

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“…Immunolocalization of some BPC1 in the pollen walls was observed after hydration and germination, suggesting that leakage of the protein from the cytosol to the wall occurred as the grains hydrated. In addition, BPC1-related proteins have been characterized as human allergens (Knox et al, 1992;Toriyama et al, 1995;Batenero et al, 1997;Engel et al, 1997;Suphioglu et al, 1997;Twardosz et al, 1997), as have the BET vIII and BET vI pollen proteins, which have 2-to 2.5-fold greater molecular masses than BPC1 (Vrtala et al, 1993;Seiberler et al, 1994). This allergenicity implies a pollen-surface location or release upon pollen hydration.…”

Section: Discussionmentioning

confidence: 99%

Characterization and Immunolocalization of a Cytosolic Calcium-Binding Protein from Brassica napus and Arabidopsis Pollen1

Rozwadowski

Zhao

Jackman³

et al. 1999

Plant Physiology

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Two low-molecular-weight proteins have been purified from Brassica napus pollen and a gene corresponding to one of them has been isolated. The gene encodes an 8.6-kD protein with two EFhand calcium-binding motifs and is a member of a small gene family in B. napus. The protein is part of a family of pollen allergens recently identified in several evolutionarily distant dicot and monocot plants. Homologs have been detected in Arabidopsis, from which one gene has been cloned in this study, and in snapdragon (Antirrhinum majus), but not in tobacco (Nicotiana tabacum). Expression of the gene in B. napus was limited to male tissues and occurred during the pollen-maturation phase of anther development. Both the B. napus and Arabidopsis proteins interact with calcium, and the potential for a calcium-dependent conformational change was demonstrated. Given this affinity for calcium, the cloned genes were termed BPC1 and APC1 (B. napus and Arabidopsis pollen calcium-binding protein 1, respectively). Immunolocalization studies demonstrated that BPC1 is found in the cytosol of mature pollen. However, upon pollen hydration and germination, there is some apparent leakage of the protein to the pollen wall. BPC1 is also concentrated on or near the surface of the elongating pollen tube. The essential nature of calcium in pollen physiology, combined with the properties of BPC1 and its high evolutionary conservation suggests that this protein plays an important role in pollination by functioning as a calcium-sensitive signal molecule.

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Section: Discussionmentioning

confidence: 99%

Characterization and Immunolocalization of a Cytosolic Calcium-Binding Protein from Brassica napus and Arabidopsis Pollen1

Rozwadowski

Zhao

Jackman³

et al. 1999

Plant Physiology

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“…Thus, it can be postulated that the above potential family of pollen proteins may have a function in this tissue that is related to its Ca*+-binding ability. The birch allergen Bet v 111, which also contains Ca'+-binding sites [32], is unlikely to belong to this family of pollen proteins because of its molecular mass (26 m a ) , the presence of four Caz+-binding sequences, and the absence of sequence similarity with Bra r I and Bra r I1 except for the EF-hand motifs [30].…”

Section: Discussionmentioning

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

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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“…In this context it was found that several calcium-binding allergens exhibited varying IgE binding capacities depending on the presence or the absence of proteinbound calcium (24,43). To test the influence of calcium on the IgE binding of recombinant carp parvalbumin, we exposed sera from six representative fish-allergic patients to nitrocellulose-blotted rCyp c 1.01 in the presence (ϩ lanes ) or the absence (Ϫ lanes ) of protein-bound calcium (Fig.…”

Section: Calcium Depletion Leads To a Reduction Of Ige Binding To Rcymentioning

confidence: 99%

Recombinant Carp Parvalbumin, the Major Cross-Reactive Fish Allergen: A Tool for Diagnosis and Therapy of Fish Allergy

Swoboda¹,

Bugajska-Schretter²,

Verdino

et al. 2002

The Journal of Immunology

218

168

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IgE-mediated reactions to fish allergens represent one of the most frequent causes of food allergy. We have constructed an expression cDNA library from carp (Cyprinus carpio) muscle in phage λgt11 and used serum IgE from a fish allergic patient to isolate 33 cDNA clones that coded for two parvalbumin isoforms (Cyp c 1.01 and Cyp c 1.02) with comparable IgE binding capacities. Both isoforms represented calcium-binding proteins that belonged to the β-lineage of parvalbumins. The Cyp c 1.01 cDNA was overexpressed in Escherichia coli, and rCyp c 1.01 was purified to homogeneity. Circular dichroism analysis and mass spectroscopy showed that rCyp c 1.01 represented a folded protein with mainly α-helical secondary structure and a molecular mass of 11,416 Da, respectively. rCyp c 1.01 reacted with IgE from all fish-allergic patients tested (n = 60), induced specific and dose-dependent basophil histamine release, and contained most of the IgE epitopes (70%) present in natural allergen extracts from cod, tuna, and salmon. Therefore, it may be used to identify patients suffering from IgE-mediated fish allergy. The therapeutic potential of rCyp c 1.01 is indicated by our findings that rabbit Abs raised against rCyp c 1.01 inhibited the binding of IgE (n = 25) in fish-allergic patients to rCyp c 1.01 between 35 and 97% (84% mean inhibition) and that depletion of calcium strongly reduced IgE recognition of rCyp c 1.01. The latter results suggest that it will be possible to develop strategies for immunotherapy for fish allergy that are based on calcium-free hypoallergenic rCyp c 1.01 derivatives.

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Characterization of a birch pollen allergen, Bet v III, representing a novel class of Ca2+ binding proteins: specific expression in mature pollen and dependence of patients' IgE binding on protein-bound Ca2+.

Cited by 118 publications

References 41 publications

Characterization and Immunolocalization of a Cytosolic Calcium-Binding Protein from Brassica napus and Arabidopsis Pollen1

Characterization and Immunolocalization of a Cytosolic Calcium-Binding Protein from Brassica napus and Arabidopsis Pollen1

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

Recombinant Carp Parvalbumin, the Major Cross-Reactive Fish Allergen: A Tool for Diagnosis and Therapy of Fish Allergy

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