Molecular basis of allergic cross-reactivity between group 1 major allergens from birch and apple

Holm, Jens Christian; Bærentzen, G.; Gajhede, Michael; Ipsen, Henrik; Larsen, Jørgen Nedergaard; Løwenstein, Henning; Wissenbach, Margit; Spangfort, Michael D.

doi:10.1016/s0378-4347(01)00089-5

Cited by 43 publications

(39 citation statements)

References 19 publications

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“…The spectrum of epitopes recognized by IgE in any individual patient is thought to be determined by a combination of genetic factors and history of allergen exposure and therefore subject to variation between patients. Variation in dominating IgE-binding epitopes between patients has also been indicated by studies of cross-reactivity, for example, between Bet v 1 and the major allergen from apple, Mal d 1 (44). According to these studies, cross-reactivity may be explained by patients having IgE directed toward molecular surface areas, which are homologous in structure, whereas patients having IgE directed toward structurally different areas do not show cross-reactivity.…”

Section: Ab Responses Following Immunization In Micementioning

confidence: 99%

Allergy Vaccine Engineering: Epitope Modulation of Recombinant Bet v 1 Reduces IgE Binding but Retains Protein Folding Pattern for Induction of Protective Blocking-Antibody Responses

Holm

Gajhede

Ferreras

et al. 2004

The Journal of Immunology

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Human type 1 immediate allergic response symptoms are caused by mediator release from basophils and mast cells. This event is triggered by allergens aggregating preformed IgE Abs bound to the high-affinity receptor (FcεRI) on these cells. Thus, the allergen/IgE interaction is crucial for the cascade leading to the allergic and anaphylactic response. Two genetically engineered forms of the white birch pollen major allergen Bet v 1 with point mutations directed at molecular surfaces have been characterized. Four and nine point mutations led to a significant reduction of the binding to human serum IgE, suggesting a mutation-induced distortion of IgE-binding B cell epitopes. In addition, the mutated allergens showed a decrease in anaphylactic potential, because histamine release from human basophils was significantly reduced. Retained α-carbon backbone folding pattern of the mutated allergens was indicated by x-ray diffraction analysis and circular dichroism spectroscopy. The rBet v 1 mutants were able to induce proliferation of T cell lines derived from birch pollen allergic patients. The stimulation indices were similar to the indices of nonmutated rBet v 1 and natural Bet v 1 purified from birch pollen. The ability of anti-rBet v 1 mutant specific mouse IgG serum to block binding of human serum IgE to rBet v 1 demonstrates that the engineered rBet v 1 mutants are able to induce Abs reactive with nonmodified Bet v 1. rBet v 1 mutants may constitute vaccine candidates with improved efficacy/safety profiles for safer allergy vaccination.

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Section: Ab Responses Following Immunization In Micementioning

confidence: 99%

Allergy Vaccine Engineering: Epitope Modulation of Recombinant Bet v 1 Reduces IgE Binding but Retains Protein Folding Pattern for Induction of Protective Blocking-Antibody Responses

Holm

Gajhede

Ferreras

et al. 2004

The Journal of Immunology

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“…Over 30 Mal d 1 DNA sequences obtained from cDNA and gDNA of leaves and fruits of various apple cultivars (Vanek-Krebitz et al 1995;Hoffmann-Sommergruber et al 1997;Son et al 1999;Holm et al 2001;Ziadi et al 2001) were published in the database GenBank at the beginning of this study. Their phylogenetic tree indicated four distinct groups with seven members (Puehringer et al 2003).…”

Section: Introductionmentioning

confidence: 99%

Genomic cloning and linkage mapping of the Mal d 1 (PR-10) gene family in apple (Malus domestica)

et al. 2005

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Fresh apples can cause birch pollen-related food allergy in northern and central European populations, primarily because of the presence of Mal d 1, the major apple allergen that is cross-reactive to the homologous and sensitizing allergen Bet v 1 from birch. Apple cultivars differ significantly in their allergenicity. Knowledge of the genetic basis of these differences would direct breeding for hypoallergenic cultivars. The PCR genomic cloning and sequencing were performed on two cultivars, Prima and Fiesta, which resulted in 37 different Mal d 1 gDNA sequences. Based on the mapping of sequence-specific molecular markers, these sequences appeared to represent 18 Mal d 1 genes. Sixteen genes were located in two clusters, one cluster with seven genes on linkage group (LG) 13, and the other cluster with nine genes on the homoeologous LG 16. One gene was mapped on LG 6, and one remained unmapped. According to sequence identity, these 18 genes could be subdivided into four subfamilies. Subfamilies I-III had an intron of different size that was subfamily and genespecific. Subfamily IV consisted of 11 intronless genes. The deduced amino acid sequence identity varied from 65% to 81% among subfamilies, from 82% to 100% among genes within a subfamily, and from 97.5% to 100% among alleles of one gene. This study provides a better understanding of the genetics of Mal d 1 and the basis for further research on the occurrence of allelic diversity among cultivars in relation to allergenicity and their biological functions.

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“…The amino acid sequences of the major allergens Bet v 1 and the homologous apple allergen Mal d 1 are close to 50% identical (Holm et al, 2001). The molecular structures of Bet v 1 and Mal d 1 are very similar, resulting in the appearance of common IgE-binding epitopes (Schöning et al, 1996;Holm et al, 2011).…”

Section: Discussionmentioning

confidence: 92%

“…However, severe systemic effects have been reported and can occur upon food consumption outside the pollen season (Katelaris, 2010;Rashid et al, 2011). The immunologic basis for the clinical reactions is considered to be due to cross-reacting IgE antibodies that are specific to birch pollen allergens, in particular Bet v 1, but that can also recognize Bet v 1-homologous allergens from fruits and vegetables (Holm et al, 2001;Mittag et al, 2004;Tolkki et al, 2013). In a study evaluating severe oral allergy syndrome and anaphylactic reactions caused by a Bet v 1-related protein in soy bean (Glycine max), Gly m 4/SAM22, immediate-type allergic symptoms in patients with birch pollen allergy after ingestion of soy proteincontaining food items were reported to occur (KleineTebbe et al, 2002).…”

Section: Introductionmentioning

confidence: 99%

High correlation of specific IgE sensitization between birch pollen, soy and apple allergens indicates pollen-food allergy syndrome among birch pollen allergic patients in northern China

Hao

Zheng²,

Wang

et al. 2016

J. Zhejiang Univ. Sci. B

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Molecular basis of allergic cross-reactivity between group 1 major allergens from birch and apple

Cited by 43 publications

References 19 publications

Allergy Vaccine Engineering: Epitope Modulation of Recombinant Bet v 1 Reduces IgE Binding but Retains Protein Folding Pattern for Induction of Protective Blocking-Antibody Responses

Allergy Vaccine Engineering: Epitope Modulation of Recombinant Bet v 1 Reduces IgE Binding but Retains Protein Folding Pattern for Induction of Protective Blocking-Antibody Responses

Genomic cloning and linkage mapping of the Mal d 1 (PR-10) gene family in apple (Malus domestica)

High correlation of specific IgE sensitization between birch pollen, soy and apple allergens indicates pollen-food allergy syndrome among birch pollen allergic patients in northern China

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