Sensitization to <i>Ficus benjamina</i>: relationship to natural rubber latex allergy and identification of foods implicated in the Ficus‐fruit syndrome

Hemmer, Wolfgang; Focke, Margarete; Götz, M.; Jarisch, Reinhart

doi:10.1111/j.1365-2222.2004.02046.x

Cited by 40 publications

(26 citation statements)

References 32 publications

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“…Notably, some of them also experienced adverse reactions to mulberry, a species botanically closely related to Ficus. However, mulberry sensitization was not found in previous studies to be causally linked to FB allergy [3]. Instead, it was exclusively observed in patients with a concomitant birch pollen allergy indicating a specific relationship with birch pollen allergens.…”

Section: Introductionmentioning

confidence: 66%

“…Dried figs do not seem to retain much of their Bet v 1-related allergenicity according to skin test results and patient histories, and therefore are not a major concern for birch pollen-allergic patients. This is in sharp contrast to FB-associated fig allergy, where dried figs may elicitate clear-cut positive skin test responses (see Table 1) and cause severe systemic reactions [2,3].…”

Section: Discussionmentioning

confidence: 90%

“…Allergic reactions to fig fruit (Ficus carica) have been repeatedly described in patients with an inhalant sensitization to the closely related ornamental Ficus benjamina (FB) [1][2][3]. Ficin, a papain-like cysteine protease, appears to be the major allergen in these cases, and clinically relevant cross-reactions may occur with homologous proteases from other tropical fruits including kiwi (actini-din), papaya (papain) and banana [2,3]. In addition, fig allergy has been occasionally mentioned in the context of rubber latex allergy [4][5][6].…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Identification of Bet v 1‐related allergens in fig and other Moraceae fruits

Hemmer

Focke

Marzban

et al. 2010

Clin Experimental Allergy

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Section: Introductionmentioning

confidence: 66%

Section: Discussionmentioning

confidence: 90%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Identification of Bet v 1‐related allergens in fig and other Moraceae fruits

Hemmer

Focke

Marzban

et al. 2010

Clin Experimental Allergy

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“…CCD and thiolproteases homologous to Act d 1 are responsible for wheat-kiwi cross-reactivity in some patients [57]. In patients with allergic reactions to figs and other tropical fruits (kiwi fruit, papaya, avocado, banana and pineapple), thiolproteases can mediate, at least in part, this cross-reactivity [58].…”

Section: Foods Of Plant Originmentioning

confidence: 99%

Molecular diagnosis in allergy

Sastre

2010

Clin Experimental Allergy

212

158

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Development and progress made in the field of recombinant allergens have allowed for the development of a new concept in allergy diagnosis, molecular diagnosis (MD), which makes it possible to identify potential disease-eliciting molecules. Microarray-based testing performed with a small amount of serum sample enables clinicians to determine specific-IgE antibodies against multiple recombinants or purified natural allergen components. Performance characteristics of allergens so far tested are comparable with current diagnostic tests, but have to be confirmed in larger studies. The use of allergen components and the successful interpretation of test results in the clinic require some degree of knowledge about the basis of allergen components and their clinical implications. Allergen components can be classified by protein families based on their function and structure. This review provides a brief overview of basic information on allergen components, recombinants or purified, currently available or soon to become commercially available in ImmunoCAP or ISAC systems, including names, protein family and function. Special consideration is given to primary or species-specific sensitization and possible cross-reactivity, because one of the most important clinical utility of MD is its ability to reveal whether the sensitization is genuine in nature (primary, species-specific) or if it is due to cross-reactivity to proteins with similar protein structures, which may help to evaluate the risk of reaction on exposure to different allergen sources. MD can be a support tool for choosing the right treatment for the right patient with the right timing. Such information will eventually give clinicians the possibility to individualize the actions taken, including an advice on targeted allergen exposure reduction, selection of suitable allergens for specific immunotherapy, or the need to perform food challenges. Nevertheless, all in vitro tests should be evaluated together with the clinical history, because allergen sensitization does not necessarily imply clinical responsiveness.

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“…Similar cross-reactivities among allergens with a high degree of identity have been observed for profilins, lipid transfer proteins, calcium-binding proteins, and pathogenesis-related proteins (Breiteneder and Mills, 2005b; Egger et al, 2006; Midoro-Horiuti et al, 2001; Weber, 2005). Other examples include the ficus-fruit syndrome related to the similarity of cysteine proteases in tropical fruits (Hemmer et al, 2004) or the IgE-based cross-reactivity of shrimp with other crustaceans and even non-edible arthropods such as cockroaches or dust mites due to the similarity of the muscle protein tropomyosin in these organisms (Ayuso et al, 2002a; Reese et al, 2006). …”

Section: Introductionmentioning

confidence: 99%

Characteristic motifs for families of allergenic proteins

Ivanciuc¹,

Garcia²,

Torres³

et al. 2009

Molecular Immunology

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The identification of potential allergenic proteins is usually done by scanning a database of allergenic proteins and locating known allergens with a high sequence similarity. However, there is no universally accepted cut-off value for sequence similarity to indicate potential IgE cross-reactivity. Further, overall sequence similarity may be less important than discrete areas of similarity in proteins with homologous structure. To identify such areas, we first classified all allergens and their subdomains in the Structural Database of Allergenic Proteins (SDAP, http://fermi.utmb.edu/SDAP/) to their closest protein families as defined in Pfam, and identified conserved physicochemical property motifs characteristic of each group of sequences. Allergens populate only a small subset of all known Pfam families, as all allergenic proteins in SDAP could be grouped to only 130 (of 9318 total) Pfams, and 31 families contain more than four allergens. Conserved physicochemical property motifs for the aligned sequences of the most populated Pfam families were identified with the PCPMer program suite and catalogued in the webserver Motif-Mate (http://born.utmb.edu/motifmate/summary.php). We also determined specific motifs for allergenic members of a family that could distinguish them from non-allergenic ones. These allergen specific motifs should be most useful in database searches for potential allergens. We found that sequence motifs unique to the allergens in three families (seed storage proteins, Bet v 1, and tropomyosin) overlap with known IgE epitopes, thus providing evidence that our motif based approach can be used to assess the potential allergenicity of novel proteins.

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Sensitization to Ficus benjamina: relationship to natural rubber latex allergy and identification of foods implicated in the Ficus‐fruit syndrome

Cited by 40 publications

References 32 publications

Identification of Bet v 1‐related allergens in fig and other Moraceae fruits

Identification of Bet v 1‐related allergens in fig and other Moraceae fruits

Molecular diagnosis in allergy

Characteristic motifs for families of allergenic proteins

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