Molecular cloning and characterization of a birch pollen minor allergen, Bet v 5, belonging to a family of isoflavone reductase–related proteins☆☆☆

Karamloo, Fariba; Schmitz, Nicole; Scheurer, Stephan; Foetisch, Kay; Hoffmann, Andreas; Haustein, Dieter; Vieths, Stefan

doi:10.1016/s0091-6749(99)70080-1

Cited by 89 publications

(75 citation statements)

References 41 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Recently, we identified and cloned a new allergen from birch pollen, Bet v 6 [10][11][12]. This displayed a high degree of amino-acid sequence identity of up to 81% with isoflavone reductase-homologous proteins (IFRH) [13 -15] and phenylcoumaran benzylic ether reductase (PCBER) [13,15], as well as lower identities of 60% and 51% with isoflavone reductases (IFR) [13 -15] and pinoresinollariciresinol reductase (PLR) [16], respectively.…”

mentioning

confidence: 99%

Phenylcoumaran benzylic ether and isoflavonoid reductases are a new class of cross‐reactive allergens in birch pollen, fruits and vegetables

Karamloo¹,

Wangorsch

Kasahara

et al. 2001

European Journal of Biochemistry

Self Cite

106

View full text Add to dashboard Cite

We investigated the biochemical function of the birch pollen allergen Bet v 6 and its role in the IgE‐cross‐reactivity between birch pollen and plant foods, and characterized Pyr c 5, a Bet v 6‐related food allergen, from pear; the proteins were expressed as His‐Tag fusion proteins in Eschershia coli and purified by Ni‐chelate affinity chromatography under native conditions. Nonfusion proteins were obtained by factor Xa protease treatment. The highest degree of amino‐acid sequence identity of Pyr c 5 and Bet v 6 was found with a plant protein related to a defense mechanism, which we have named phenylcoumaran benzylic ether reductase (PCBER) based on its ability to catalyze the NADPH‐dependent reduction of 8–5′ linked lignans such as dehydrodiconiferyl alcohol to give isodihydrodehydrodiconiferyl alcohol. Enzymatic assays with recombinant Pyr c 5 and Bet v 6 showed PCBER catalytic activity for both recombinant allergens. Both Pyr c 5 and Bet v 6 allergens had similar IgE binding characteristics in immunoblotting and enzyme allergosorbent tests (EAST), and bound IgE from 10 sera of birch‐pollen‐allergic patients including six pear‐allergic subjects. EAST inhibition experiments with Pyr c 5 as the solid phase antigen suggested that homologous allergens may be present in many vegetable foods such as apple, peach, orange, lychee fruit, strawberry, persimmon, zucchini (courgette), and carrot. In extracts of pear, apple, orange, and persimmon, the presence of proteins of approximately 30–35 kDa containing Bet v 6 cross‐reactive epitopes was demonstrated with two Bet v 6‐specific monoclonal antibodies. Recombinant Pyr c 5 triggered a strong, dose‐dependent mediator release from basophils of a pear‐allergic subject, suggesting that Pyr c 5 has the potential to elicit type I allergic reactions.

show abstract

mentioning

confidence: 99%

Phenylcoumaran benzylic ether and isoflavonoid reductases are a new class of cross‐reactive allergens in birch pollen, fruits and vegetables

Karamloo¹,

Wangorsch

Kasahara

et al. 2001

European Journal of Biochemistry

Self Cite

106

View full text Add to dashboard Cite

show abstract

“…1994;Tinghino et al 2002). Bet v 4, a 9 kDa Ca-binding protein (Engel et al 1997;Twardosz et al 1997;Ferreira et al 1999;Grote et al 2002), Bet v 5, a 35 kDa isoflavone reductase-related protein (Vieths et al 1998;Karamloo et al 1999;Stewart and McWilliam, 2001), Bet v 6, a 30-35 kDa protein, PCBER (Phenylcoumaran benzylic ether reductase) (Karamloo et al 2001), Bet v 7, a 18 kDa protein, characterized as a cyclophilin (Cadot et al 2000) and Bet v 11 (Moverare et al 2002).…”

Section: Birch (Betula Verrucosa Synonym: B Pendula)mentioning

confidence: 99%

“…A large number of these allergens have been expressed as recombinant proteins, including rBet v 1 (Ferreira et al 2003), rBet v 2 (Valenta et al 1991a-c;Niederberger et al 1998;Susani et al 1995;Valenta et al 1993), rBet v 3 (Valenta et al 1991a-c;Seiberler et al 1994), rBet v 4 (Engel et al 1997; Twardosz et al 1997;Ferreira et al 1999), rBet v 5 (Karamloo et al 1999) and rBet v 6 (Vieths et al 2002).…”

Section: Birch (Betula Verrucosa Synonym: B Pendula)mentioning

confidence: 99%

“…As significant allergenic behaviors, Bet v 1 displays a considerable degree of heterogeneity and consists of at least 20 isoforms which differ in their IgE-binding capacity (Bet v 1a to Bet v 1n), (Breiteneder et al 1989;Elsayed and Vik, 1990;Karamloo et al 1999;Friedl-Hajek et al 1999). Birch pollen-allergic individuals may not be sensitized to any of the major birch pollen allergens.…”

Section: Birch (Betula Verrucosa Synonym: B Pendula)mentioning

confidence: 99%

See 1 more Smart Citation

Pollen Allergenicity is Highly Dependent on the Plant Genetic Background: The “Variety”/“Cultivar” Issues

Alché¹,

Zafra²,

Jiménez-López³

et al. 2012

Current Insights in Pollen Allergens

View full text Add to dashboard Cite

show abstract

“…A recent example supporting this idea is isoflavone reductase, which is a defense-related protein that plays a role in the biosynthesis of phytoalexin (Bowles, 1990). This enzyme and its homologues were documented as a minor cross-reactive allergen for subjects sensitized by birch-pollen (Vieths et al, 1998;Karamloo et al, 1999). The question arises as to whether rubber trees cultured in plantations are receiving stresses that are sufficient to bring about the induction of defense-related proteins.…”

Section: Defense-related Proteins In Higher Plantsmentioning

confidence: 99%

Features and Mode of Action of Cross-reactive Plant Allergens Relevant to Latex-fruit Syndrome

Yagami

2002

Food and Agricultural Immunology

View full text Add to dashboard Cite

Immediate-type reactions to articles made from natural rubber latex are collectively referred to as latex allergy. Some latex-sensitized patients also experience allergic reactions to various fruits and vegetables. This phenomenon is RESEARCH ON ALLERGENSThere have been recent surprising advancements in immunology, and we expect it to progress even more rapidly and steadily in the future using the genomic information of the human being. By contrast, research on allergenic substances (allergens) is far behind the times. The accumulation of scientific knowledge about the features and modes of action of allergens is

show abstract

Molecular cloning and characterization of a birch pollen minor allergen, Bet v 5, belonging to a family of isoflavone reductase–related proteins☆☆☆

Cited by 89 publications

References 41 publications

Phenylcoumaran benzylic ether and isoflavonoid reductases are a new class of cross‐reactive allergens in birch pollen, fruits and vegetables

Phenylcoumaran benzylic ether and isoflavonoid reductases are a new class of cross‐reactive allergens in birch pollen, fruits and vegetables

Pollen Allergenicity is Highly Dependent on the Plant Genetic Background: The “Variety”/“Cultivar” Issues

Features and Mode of Action of Cross-reactive Plant Allergens Relevant to Latex-fruit Syndrome

Contact Info

Product

Resources

About