POLLINI - Betula pendula Roth - BETULLA VERRUCOSA - BETULLA BIANCA

  BETULLA VERRUCOSA - BETULLA BIANCA
Betula pendula Roth. – Betulaceae

Pianta a foglia caduca, portamento arboreo, alta anche 25-30 metri, dalla corteccia bianca e liscia. Pianta monoica (con strutture riproduttive edi entrambi i sessi sullo stesso esemplare)

ALL-INA-BETULA_VERRUCOSA_01Classico esemplare in zona collinare

 

ALL-INA-BETULA_VERRUCOSA_02Cascata di infiorescenze maschili ad amento, lunghe 4-10 cm, e di color giallo-brunastro.

 

ALL-INA-BETULA_VERRUCOSA_03Amenti maschili

 

ALL-INA-BETULA_VERRUCOSA_04Infiorescenza femminile. Le femminili sono più corte, tozze, di color verdastro, in genere poco appariscenti.

 

ALL-INA-BETULA_VERRUCOSA_05Iinfruttescenze dove sono contenuti i frutti secchi indeiscenti o acheni. Foglie a forma rombo-triangolare con margine dentato e sottilmente seghettato.


POLLINE
Presenza del polline : MARZO - MAGGIO
Allergenicità del polline: ELEVATA
Descrizione : Granulo isopolare (= con faccia prossimale e distale simili), prevalentemente suboblato (= leggermente schiacciato ai poli), triporato (con tre pori). I pori sono circolari e circondati da un annulus (ispessimento attorno al poro). Esina (= parete esterna del granulo pollinico) con parete sottile e superficie liscia. Si ispessisce attorno ai pori formano aspides (=ispessimento a cupola più o meno sporgente). Dimensioni medio-piccole (diametro maggiore 21-23).

Reazione crociata nei confronti delle altre specie del genere Betulla. Verso il genere Alnus minore cross-reattività, che è anche possibile verso i genere Carpinus, Corylus, Castanea, Fagus, Quercus.

  

PRINCIPALI ALLERGENI INDIVIDUATI

  

  

NOME

ATTIVITA’

(vedi corrispondenti allergeni molecolari)

VIE  DI SENSIBILIZZAZIONE

Bet v 1

Bet v 1-like

Inalazione

Bet v 2

Profiline (actin-binding proteins)

Inalazione

Bet v 3

Polcalcine (calcium-binding proteins)

Inalazione

Bet v 4

Polcalcine (calcium-binding proteins)

Inalazione

Bet v 6

Isoflavone reduttasi

Inalazione

Bet v 7

Ciclofilina

Inalazione

Bet v 8

Pectinesterasi

Inalazione

Be v Glucanase

beta-1,3–glucanasi

Inalazione

  

Gli allergeni della betulla possono essere coinvolti in vari casi di cross-reattività con vari alimenti, che saranno trattati in file specifici.

  

Principali fonti documentali generali in Cultura Allergologica)
Per eventuali approfondimenti, alcune fonti documentali specifiche

Arquint O, Helbling A, et al. Reduced in vivo allergenicity of Bet v 1d isoform, a natural component of birch pollen. J Allergy Clin Immunol 1999;104:1239-1243

Cadot P, Diaz JF, et al. Purification and characterization of an 18-kd allergen of birch (Betula verrucosa) pollen: Identification as a cyclophilin. J Allergy Clin Immunol 2000;105:286-291

De Amici M, Mosca M, et al. Recombinant birch allergens (Bet v 1 and Bet v 2) and the oral allergy syndrome in patients allergic to birch pollen. Ann Allergy Asthma Immunol 2003;91:490-2

Diez-Gomez ML, Quirce S, et al. Fruit-pollen-latex cross-reactivity: implication of profilin (Bet v 2). Allergy 1999;54:951-61

Ebner C, Hirschwehr R, et al. Identification of allergens in fruits and vegetables : IgE cross-reactivities with the important birch pollen allergens Bet v 1 and Bet v 2 (profilin). J Allergy Clin Immunol 1995;95:962-969

Engel E, Richter K, et al. Immunological and biological properties of Bet v 4, a novel birch pollen allergen with two EF-hand calcium-binding domains. J Biol Chem 1997;272:28630-7

Ferreira FD, Hoffmann-Sommergruber K, Breiteneder H et al. Purification and characterization of recombinant Bet v I, the major birch pollen allergen.
Immunological equivalence to natural Bet v I. J Biol Chem 1993;268:19574-80

Fritsch R, Bohle B, et al. Bet v 1 , the major birch pollen allergen, and Mal d 1, the major apple allergen, cross-react at the level of allergen-specific T herper cells. J Allergy Clin Immunol 1998;102:679-686

Godnic-Cvar J, Susani M, et al. Recombinant Bet v 1, the major birch pollen allergen, induces hypersensitivity reactions equal to those induced by natural Bet v 1 in the airways of patients allergic to tree pollen. J Allergy Clin Immunol 1997;99:354-9

Grote M, Wiedemann, et al. Human monoclonal IgG antibodies derived from a patient allergic to birch pollen as tools to study the in situ localization of the major birch pollen allegen, Bet v 1, by immunogold electron microscopy. J Allergy Clin Immunol 2003;101:60-66

Jahn-Schmid B, Radakovics A, et al. Bet v 1 142-156 is the dominant T-cell epitope of the major birch pollen allergen and important for cross-reactivity with Bet v 1-related food allergens. J Allergy Clin Immunol 2005;116:213-219

Karamloo F, Schmitz, et al. Molecular cloning and characterization of a birch pollen minor allergen, Bet v 5, belonging to a family of isoflavone reductase-related proteins. J Allergy Clin Immunol 1999;104:991-9

Kaul S, Scheurer S, et al. Monoclonal IgE antibodies against birch pollen allergens: novel tools for biological characterization and standardization of allergens. J Allergy Clin Immunol 2003 Jun;111:1262-8

Kawamoto S, Fujimura T, et al. Molecular cloning and characterization of a new Japanese cedar pollen allergen homologous to plant isoflavone reductase family. Clin Exp Allergy 2002;32:1064-70

Kazemi-Shirazi L, Pauli G, et al. Quantitative IgE inhibition experiments with purified recombinant allergens indicate pollen-derived allergens as the sensitizing agents responsible for many forms of plant food allergy. J Allergy Clin Immunol 2000;105:116-25

Magnusson J, Lin XP, et al. Seasonal intestinal inflammation in patients with birch pollen allergy. J Allergy Clin Immunol 2003 ;112 :45-51

Mahler V, Vrtala S, et al. Vaccines for birch pollen allergy based on genetically engineered hypoallergenic derivatives of the major birch pollen allergen, Bet v 1. Clin Exp Allergy 2004;34:115-22

Martinez A, Asturias JA, et al. The allergenic relevance of profilin (Ole e 2) from Olea europaea pollen. Allergy 2002;57 Suppl 71:17-23

Menz G, Dolecek C,  et al. Serological and skin-test diagnosis of birch pollen allergy with recombinant Bet v I, the major birch pollen allergen. Clin Exp Allergy 1996;26:50-60

Mittag D, Akkerdaas J, et al. Ara h 8, a Bet v 1-homologous allergen from peanut, is a major allergen in patients with combined birch pollen and peanut allergy. J Allergy Clin Immunol 2004;114:1410-1417

Mutschlechner S, Egger M, et al. Naturally processed T cell-activating peptides of the major birch pollen allergen. J Allergy Clin Immunol 2010;125:711-718

Neudecker P, Nerkamp J, et al. Solution structure, dynamics, and hydrodynamics of the calcium-bound cross-reactive birch pollen allergen Bet v 4 reveal a canonical monomeric two EF-hand assembly with a regulatory function. J Mol Biol 2004;336:1141-57

Niederberger V, Laffer S,  et al. IgE antibodies to recombinant pollen allergens (Phl p 1, Phl p 2, Phl p 5, and Bet v 2) account for a high percentage of grass pollen-specific IgE. J Allergy Clin Immunol 1998;101:258-64

Niederberger V, Pauli G, et al. Recombinant birch pollen allergens (rBet v 1 and rBet v 2) contain most of the IgE epitopes present in birch, alder, hornbeam, hazel, and oak pollen: a quantitative IgE inhibition study with sera from different populations. J Allergy Clin Immunol 1998;102:579-591

Pauli G, Purohit A, et al. Comparison of genetically engineered hypoallergenic rBet v 1 derivatives with rBet v 1 wild-type by skin prick and intradermal testing: results obtained in a French population. Clin Exp Allergy 2000;30:1076-84

Petrucco S, Bolchi A, Fet al.. A maize gene encoding an NADPH binding enzyme highly homologous to isoflavone reductases is activated in response to sulfur starvation. Plant Cell 1996;8:69-80

Rossi RE, Monasterolo G, Monasterolo S. Detection of specific IgE antibodies in the sera of patients allergic to birch pollen using recombinant allergens Bet v 1, Bet v 2, Bet v 4: evaluation of different IgE reactivity profiles. Allergy 2003 ;58:929-932

Schappi GF, Suphioglu c. et al. Concentrations of the major birch tree allergen Bet v 1 in pollen and respirable fine particles in the atmosphere. J Allergy Clin Immunol 1997;100:656-661

Tresch S, Holzmann D, et al. In vitro and in vivo allergenicity of recombinant Bet v 1 compared to the reactivity of natural birch pollen extract. Clin Exp Allergy 2003;33:1153-8

Valenta R, Breiteneder H, et al. Homology of the major birch-pollen allergen, Bet v I, with the major pollen allergens of alder, hazel, and hornbeam at the nucleic acid level as determined by cross-hybridization. J Allergy Clin Immunol 1991;87:677-682

Valenta R, Duchene M,  et al. Recombinant allergens for immunoblot diagnosis of tree-pollen allergy. J Allergy Clin Immunol 1991;88:889-894

Valenta R, Ferreira F, et al. Identification of profilin as an actin-binding protein in higher plants. J Biol Chem 1993;268:22777-81

Vieths S, Frank E, et al. Characterization of a new IgE-binding 35-kDa protein from birch pollen with cross-reacting homologues in various plant foods.Scand J Immunol 1998;47:263-267

Wagner S, Radauer C, et al. Naturally occuring hypoallergenic Bet v 1 isoforms fail to induce IgE response in individuals with birch pollen allergy. J Allergy Clin Immunol 2008;121:246-252