Immunological and Biological Properties of Bet v 4, a Novel Birch Pollen Allergen with Two EF-hand Calcium-binding Domains

Engel, Edwin; Richter, Klaus; Obermeyer, Gerhard; Briza, Peter; Kungl, Andreas J.; Simon, Birgit; Auer, Manfred; Ebner, Christof; Rheinberger, Hans Jörg; Breitenbach, Michael; Ferreira, Fátima

doi:10.1074/jbc.272.45.28630

Cited by 124 publications

(135 citation statements)

References 58 publications

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“…In addition to the demonstration of homologous sequences in Antirrhinum described here, related proteins have been identified in Betula verrucosa (Engel et al, 1997;Twardosz et al, 1997), Olea europaea (Batanero et al, 1997), Artemisia vulgaris (Engel et al, 1997), Cynodon dactylon (Knox et al, 1992), Phleum pratense, and Lilium longiflorum (Engel et al, 1997;Twardosz et al, 1997), and multiple types were identified in Brassica rapa and B. napus (Toriyama et al, 1995;Lim et al, 1996) during the course of this study. The partial amino acid sequence from the second pollen protein purified in this study, PP-A, indicates that it, too, is a member of this protein family.…”

Section: Discussionsupporting

confidence: 61%

“…In the presence of calcium, rBPC1 may assume a more compact conformation than in the apo state, enabling it to elute as a smaller protein. Conformational changes in response to calcium have been demonstrated in related proteins (Engel et al, 1997;Suphioglu et al, 1997;Twardosz et al, 1997). Second, it is possible that rBPC1 may interconvert between a monomeric and dimeric state in response to calcium.…”

Section: Discussionmentioning

confidence: 99%

“…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%

“…This linkage is highly conserved among diverse species. In addition to the Brassica proteins, highly related pollen allergens have been identified in Betula verrucosa (Engel et al, 1997;Twardosz et al, 1997), Olea europaea (Batanero et al, 1997), Artemisia vulgaris (Engel et al, 1997), and the monocots Cynodon dactylon (Suphioglu et al, 1997), Phleum pratens, and Lilium longiflorum (Engel et al, 1997;Twardosz et al, 1997). The present study also describes cloning of APC1, a homolog from Arabidopsis, and demonstrates the presence of related sequences in Antirrhinum but not in tobacco (Nicotiana tabacum).…”

mentioning

confidence: 84%

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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: Discussionsupporting

confidence: 61%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 84%

See 2 more Smart Citations

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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“…Some of the intracellular allergens and self-antigens that also occur in a similar structure within humans that have been described so far include: (Valenta et al, 2009) 15 enolases and several calcium-binding proteins, in the case of fungal allergies (Spinozzi et al, 2008;Achatz et al, 1996;Breitenbach et al, 1997;Engel et al, 1997;Unger et al, 1999;Simon-Nobbe et al, 2000) 16 malate dehydrogenase, triose phosphate isomerase and profiling in allergies to watermelon (Pastor et al, 2009) and other fruits.…”

Section: Mild and Severe Damage Resulting From The Mechanisms Of Apopmentioning

confidence: 99%

Hypothesis for a common-cause underlying both autoimmune-diseases and allergies

Arneth

2011

IJIS

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Abstract:Although autoimmune diseases and allergies have recently been associated with each other, the results of the few studies that are available are contradictory. While some of these studies suggest that there is no evidence to assume a connection between autoimmune diseases and allergies, other studies, including some recent animal studies, suggest a connection between these diseases. In this study, we describe the possible connection between autoimmune diseases and allergies. It is important to note that, for the considerations described here, it will be necessary to consider the two types of diseases in a completely different way than has been done so far.Keywords: autoimmunity; antigen presentation; food allergies; T-lymphocytes; CD4-T-lymphocytes; CD8-T-lymphocytes; allergies.Reference to this paper should be made as follows: Arneth, B.M. (2011) 'Hypothesis for a common-cause underlying both autoimmune-diseases and allergies', Int.

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Sensitization profile to sawtooth oak component allergens and their clinical implications

Jeong

Lee

Sang

et al. 2021

Clinical Laboratory Analysis

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Objective The component allergens from sawtooth oak, which is a main cause of tree pollinosis in Korea, have not been extensively characterized except Que ac 1. This study was undertaken to characterize the allergenic components from sawtooth oak pollen and investigate the diagnostic values of each component allergen. Methods Transcriptomic analysis was performed to identify the birch pollen allergen homologues from sawtooth oak pollen. Recombinant Que ac 1, 2, 3, 6, 7, and 8 were produced in an E. coli expression system. IgE reactivity to each allergen was examined by ImmunoCAP and ELISA using the sera of 50 Korean tree pollinosis patients. Results Six birch pollen allergen homologues were identified using transcriptome analysis, as follows: Que ac 1 (54.8% identity to Bet v 1), Que ac 2 (79.7% to Bet v 2), Que ac 3 (24.9% to Bet v 3), 6 (71.3% to Bet v 6), Que ac 7 (80.9% to Bet v 7), and Que ac 8 (78.9% to Bet v 8). Que ac 1 sIgE was the most frequently recognized (84.0%), followed by Que ac 2 (12.0%), Que ac 3 (6.0%), and three other allergens (2.0% each). Que ac 1 was a dominant allergen affecting 83.7% of patients suffering from allergic rhinoconjunctivitis, and 92.9% of pollen food allergy syndrome patients. Conclusion Five novel IgE reactive components of sawtooth oak were characterized using transcriptome analysis. Que ac 1 is the single most important component allergen of sawtooth oak pollen.

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Immunological and Biological Properties of Bet v 4, a Novel Birch Pollen Allergen with Two EF-hand Calcium-binding Domains

Cited by 124 publications

References 58 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

Hypothesis for a common-cause underlying both autoimmune-diseases and allergies

Sensitization profile to sawtooth oak component allergens and their clinical implications

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