scholarly journals NMR resonance assignments of the PR-10 allergens Act c 8 and Act d 8 from golden and green kiwifruit

2021 ◽  
Author(s):  
Ricarda Zeindl ◽  
Martin Tollinger
Keyword(s):  
Clinical Symptoms ◽  
Chemical Shifts ◽  
Birch Pollen ◽  
Resonance Assignments ◽  
Cross Reactivity ◽  
Food Sources ◽  
Structural Basis ◽  
Homologous Proteins ◽  
Dimensional Solution ◽  
Bet V 1

AbstractKiwifruits have become one of the most common food sources triggering allergic reactions. In patients suffering from birch pollen related food allergy, reactions result from initial sensitization to the birch (Betula verrucosa) pollen allergen Bet v 1, followed by immunological cross-reactivity to structurally homologous proteins in kiwifruit. Clinical symptoms range from scratching and itching of the oral cavity to more severe immunological reactions such as rhino conjunctivitis. In this work we assigned backbone and side chain 1H, 13C and 15N chemical shifts of the 17 kDa PR-10 allergens Act c 8.0101 and Act d 8.0101 from golden (Actinidia chinesis) and green (Actinidia deliciosa) kiwifruit by solution NMR spectroscopy. The chemical shift data confirm the characteristic Bet v 1 fold for both proteins, consisting of a seven-stranded antiparallel β-sheet interrupted by two short α-helices, along with a long C-terminal α-helix. Our data provide the basis for determining the three-dimensional solution structures of these proteins and characterizing their immunological cross-reactivity on a structural basis.

scholarly journals Cross-reactivity of pollen and food allergens: soybean Gly m 4 is a member of the Bet v 1 superfamily and closely resembles yellow lupine proteins

2009 ◽  
Vol 29 (3) ◽  
pp. 183-192 ◽  
Author(s):  
Hanna Berkner ◽  
Philipp Neudecker ◽  
Diana Mittag ◽  
Barbara K. Ballmer-Weber ◽  
Kristian Schweimer ◽  
...  
Keyword(s):  
Physiological Function ◽  
Three Dimensional ◽  
Birch Pollen ◽  
Cross Reactivity ◽  
Food Allergens ◽  
Homologous Proteins ◽  
Allergen Specific Immunotherapy ◽  
Ige Antibodies ◽  
Bet V 1 ◽  
Yellow Lupine

In many cases, patients allergic to birch pollen also show allergic reactions after ingestion of certain fruits or vegetables. This observation is explained at the molecular level by cross-reactivity of IgE antibodies induced by sensitization to the major birch pollen allergen Bet v 1 with homologous food allergens. As IgE antibodies recognize conformational epitopes, a precise structural characterization of the allergens involved is necessary to understand cross-reactivity and thus to develop new methods of allergen-specific immunotherapy for allergic patients. Here, we report the three-dimensional solution structure of the soybean allergen Gly m 4, a member of the superfamily of Bet v 1 homologous proteins and a cross-reactant with IgE antibodies originally raised against Bet v 1 as shown by immunoblot inhibition and histamine release assays. Although the overall fold of Gly m 4 is very similar to that of Bet v 1, the three-dimensional structures of these proteins differ in detail. The Gly m 4 local structures that display those differences are also found in proteins from yellow lupine with known physiological function. The three-dimensional structure of Gly m 4 may thus shed some light on the physiological function of this subgroup of PR10 proteins (class 10 of pathogenesis-related proteins) and, in combination with immunological data, allow us to propose surface patches that might represent cross-reactive epitopes.

scholarly journals Crossreactive allergen-specific IgE in children with birch pollen allergic rhinitis

2017 ◽  
Vol 14 (2) ◽  
pp. 66-70
Author(s):  
P V Samoylikov ◽  
S A Mazurina ◽  
P I Gushchin ◽  
V B Gervazieva
Keyword(s):  
Allergic Rhinitis ◽  
Birch Pollen ◽  
Humoral Response ◽  
Specific Ige ◽  
Cross Reactivity ◽  
Oral Allergy Syndrome ◽  
Food Allergens ◽  
Homologous Proteins ◽  
Total Ige ◽  
Bet V 1

Objective. The aim of this study was to research a sIgE allergen profile of birch pollen and to evaluate a contribution of some homologous food allergens as well as latex allergen to the development of sensibility in allergic rhinitis (AR) / rhinoconjunctivitis patients, in focus of cross-reactivity and oral allergy syndrome.. Methods. Blood sera of 21 AR/rhinoconjunctivitis patients (at the age of 3 to 16) and 20 healthy persons without allergy symptoms were used. sIgE to birch pollen, soybean, latex, apple and celery as well as the total IgE levels were measured by the ImmunoCAP method (Phadia, Sweden) and the ELISA kits (Alkorbio, Russia). Results. We detected high total IgE levels, sIgE to allergens of birch pollen, apple, celery, as well as to recombinant allergens of birch Bet v 1, Bet v 2 and soybean - Gly m 4 in AR patients. Correlation analysis of IgE humoral response to homologous proteins showed the direct valid dependence between the sIgE levels to birch isoallergen Bet v 1 and soy isoallergen Gly m 4 (r=0,84; p

Purification and characterization of natural Ara h 8, the Bet v 1 homologous allergen from peanut, provides a novel isoform

2008 ◽  
Vol 389 (4) ◽  
pp. 415-423 ◽  
Author(s):  
Susanne Riecken ◽  
Buko Lindner ◽  
Arnd Petersen ◽  
Uta Jappe ◽  
Wolf-Meinhard Becker
Keyword(s):  
Birch Pollen ◽  
Diagnostic Procedures ◽  
Cross Reactivity ◽  
Exchange Chromatography ◽  
Size Exclusion ◽  
Reactive Protein ◽  
Bet V 1 ◽  
Peanut Extract ◽  
Natural Counterpart

Abstract The peanut allergen Ara h 8 is an important allergen for birch pollen allergic patients because of the cross-reactivity to the homologous Bet v 1. As the existence of Ara h 8 has been shown at the cDNA level so far (AY328088) and the allergen has indirectly been detected as natural protein, it was the aim of our study to identify natural Ara h 8 in peanut extract and to develop a purification strategy. This was achieved using a unique combination of purification steps, including optimized extraction conditions, size exclusion and ion exchange chromatography and treatment of the interfering contaminants with iodo-acetic acid. A characterization of the protein by microsequencing showed discrepancies to the deduced amino acid sequence of AY328088. For this reason, we cloned and expressed a new Ara h 8 isoform from cDNA (EU046325). This IgE-reactive protein corresponds to the results of microsequencing, ESI-FTICR-MS and trypsin fingerprinting analysis of the authentic and purified nAra h 8. Apart from the ultimate use of recombinant allergens for diagnostic procedures, there is also a scientific need for the natural counterpart, as it represents an excellent reference point by which to compare protein characteristics and to standardize diagnostic and therapeutic allergens.

Bet v 1142-156 is the dominant T-cell epitope of the major birch pollen allergen and important for cross-reactivity with Bet v 1–related food allergens

2005 ◽  
Vol 116 (1) ◽  
pp. 213-219 ◽  
Author(s):  
Beatrice Jahn-Schmid ◽  
Astrid Radakovics ◽  
Dirk Lüttkopf ◽  
Stephan Scheurer ◽  
Stefan Vieths ◽  
...  
Keyword(s):  
T Cell ◽  
Cell Epitope ◽  
Birch Pollen ◽  
Cross Reactivity ◽  
Pollen Allergen ◽  
T Cell Epitope ◽  
Food Allergens ◽  
Bet V 1 ◽  
Birch Pollen Allergen

Crystallization and preliminary X-ray analysis of birch-pollen allergen Bet v 1 in complex with a murine monoclonal IgG Fab′ fragment

1999 ◽  
Vol 55 (12) ◽  
pp. 2035-2036 ◽  
Author(s):  
Michael D. Spangfort ◽  
Osman Mirza ◽  
L. Anders Svensson ◽  
Jørgen N. Larsen ◽  
Michael Gajhede ◽  
...  
Keyword(s):  
Immunoglobulin E ◽  
Birch Pollen ◽  
Pollen Allergen ◽  
Structural Basis ◽  
Type I ◽  
X Rays ◽  
Fab Fragment ◽  
Cell Parameters ◽  
Bet V 1 ◽  
Birch Pollen Allergen

The human type I allergic response is characterized by the presence of allergen-specific serum immunoglobulin E (IgE). Allergen-mediated cross-linking of receptor-bound IgE on the surface of mast cells and circulating basophils triggers the release of mediators, resulting in the development of the clinical symptoms of allergy. In order to study the structural basis of allergen–antibody interaction, a complex between the major birch-pollen allergen Bet v 1 and a Fab′ fragment isolated from the murine monoclonal Bet v 1 antibody BV16 has been crystallized. Complex crystals belong to space group P1, with unit-cell parameters a = 91.65, b = 99.14, c = 108.90 Å, α = 105.7, β = 98.32, γ = 97.62°, and diffract to 2.9 Å resolution when analyzed at 100 K using synchrotron-generated X-rays.

Kinetics, cross-reactivity, and specificity of Bet v 1-specific IgG4 antibodies induced by immunotherapy with birch pollen

Allergy ◽  
2013 ◽  
Vol 68 (11) ◽  
pp. 1377-1386 ◽  
Author(s):  
B. Subbarayal ◽  
D. Schiller ◽  
C. Möbs ◽  
N. W. de Jong ◽  
C. Ebner ◽  
...  
Keyword(s):  
Birch Pollen ◽  
Cross Reactivity ◽  
Bet V 1 ◽  
Specific Igg4

scholarly journals NMR resonance assignments of the four isoforms of the hazelnut allergen Cor a 1.04

2019 ◽  
Vol 14 (1) ◽  
pp. 45-49 ◽  
Author(s):  
Sebastian Führer ◽  
Ricarda Zeindl ◽  
Martin Tollinger
Keyword(s):  
Fruits And Vegetables ◽  
Chemical Shifts ◽  
Three Dimensional ◽  
Resonance Assignments ◽  
Subsequent Development ◽  
Dimensional Structure ◽  
Side Chain ◽  
Bet V 1 ◽  
Chemical Shift Data ◽  
Α Helix

Abstract In large parts of Europe, Northern America and China people are suffering from allergies after consuming certain kinds of fruits and vegetables. Typical allergic symptoms range from scratching and itching of the throat to severe symptoms like rhino conjunctivitis and anaphylaxis. For hazelnuts (Corylus avellana), these allergies result from initial sensitization to the birch (Betula verrucosa) pollen allergen Bet v 1 and subsequent development of allergic cross-reactions to proteins that are similar in their three-dimensional structure to the sensitizing protein Bet v 1. The cross-reactive proteins in hazelnut are the four isoforms Cor a 1.04 with a molecular weight of about 17.5 kDa. Significant differences regarding the immunologic behavior of these proteins have been reported. In this work we assigned backbone and side chain 1H, 13C, and 15N chemical shifts of these four isoforms, Cor a 1.0401, Cor a 1.0402, Cor a 1.0403, and Cor a 1.0404 by solution NMR spectroscopy. The chemical shift data confirm the characteristic Bet v onefold for all four isoforms, consisting of seven β-strands that are separated by two short α-helices, along with a long C-terminal α-helix. These data provide the basis for a comparative structural and dynamic analysis of these proteins by NMR in order to characterize their different immunologic cross-reactivities on a molecular level.

scholarly journals Dominant Epitopes and Allergic Cross-Reactivity: Complex Formation Between a Fab Fragment of a Monoclonal Murine IgG Antibody and the Major Allergen from Birch Pollen Bet v 1

2000 ◽  
Vol 165 (1) ◽  
pp. 331-338 ◽  
Author(s):  
Osman Mirza ◽  
Anette Henriksen ◽  
Henrik Ipsen ◽  
Jørgen N. Larsen ◽  
Margit Wissenbach ◽  
...  
Keyword(s):  
Complex Formation ◽  
Birch Pollen ◽  
Major Allergen ◽  
Cross Reactivity ◽  
Igg Antibody ◽  
Fab Fragment ◽  
Bet V 1

Roasting and lipid binding provide allergenic and proteolytic stability to the peanut allergen Ara h 8

2014 ◽  
Vol 395 (2) ◽  
pp. 239-250 ◽  
Author(s):  
Arnd Petersen ◽  
Sandra Rennert ◽  
Skadi Kull ◽  
Wolf-Meinhard Becker ◽  
Holger Notbohm ◽  
...  
Keyword(s):  
Birch Pollen ◽  
Lipid Binding ◽  
Homologous Proteins ◽  
Peanut Allergen ◽  
Maillard Reactions ◽  
Bet V 1 ◽  
Ige Reactivity ◽  
Hydrophobic Binding ◽  
Proteolytic Stability ◽  
The Impact

Abstract Ara h 8 is the peanut allergen homologous to the birch pollen allergen Bet v 1. Because Bet v 1 has been shown to bind lipophilic ligands, the aim of this investigation was to determine the impact of lipid binding and roasting on the Ara h 8 structure and their influences on allergenicity. For the characterization of natural Ara h 8 (nAra h 8) from roasted and unroasted peanuts, circular dichroism spectroscopy, hydrophobic binding assay, immunohistochemistry, and immunoblot with sera of peanut allergic patients were performed and compared with results from recombinant Ara h 8 (rAra h 8) and Bet v 1. rAra h 8 displayed stronger hydrophobicity than rBet v 1. Patients’ sera showed IgE reactivity with rAra h 8 and nAra h 8 from roasted peanuts, whereas fewer sera recognized nAra h 8 from unroasted peanuts. Simulated gastric digestion experiments demonstrated low proteolytic stability of rAra h 8, whereas the stability of nAra h 8 was increasingly higher in unroasted and roasted peanuts. The results demonstrate that IgE reactivity and thermal and proteolytic stability are reinforced in nAra h 8 after roasting, most likely due to Maillard reactions, lipid oxidations, and lipophilic associations. These aspects must be considered when estimating the allergenicity of Bet v 1-homologous proteins.

scholarly journals NMR resonance assignments of a hypoallergenic isoform of the major birch pollen allergen Bet v 1

2017 ◽  
Vol 11 (2) ◽  
pp. 231-234 ◽  
Author(s):  
Linda Ahammer ◽  
Sarina Grutsch ◽  
Michael Wallner ◽  
Fatima Ferreira ◽  
Martin Tollinger
Keyword(s):  
Birch Pollen ◽  
Resonance Assignments ◽  
Nmr Resonance Assignments ◽  
Pollen Allergen ◽  
Bet V 1 ◽  
Birch Pollen Allergen
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