Immunological cross‐reactivity between lipid transfer proteins from botanically unrelated plant‐derived foods: a clinical study

Asero, Riccardo; Mistrello, Gianni; Roncarolo, Daniela; Amato, Stefano; Caldironi, Gianni; Barocci, Fiorella; Ree, Ronald van

doi:10.1034/j.1398-9995.2002.t01-1-23541.x

Cited by 160 publications

(135 citation statements)

References 37 publications

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“…Prominent examples of them are profilins (38), lipid transfer proteins (39), and cyclophilins (20). They are responsible for oftenobserved clinical syndromes like birch-mugwort-celery syndrome (40), oral allergy syndromes (41), and AE/dermatitis syndrome (42).…”

Section: Discussionmentioning

confidence: 99%

Cross-Reactivity and 1.4-Å Crystal Structure ofMalassezia sympodialisThioredoxin (Mala s 13), a Member of a New Pan-Allergen Family

Limacher¹,

Glaser²,

Meier³

et al. 2007

The Journal of Immunology

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We have identified thioredoxins (Trx) of Malassezia sympodialis, a yeast involved in the pathogenesis of atopic eczema, and of Aspergillus fumigatus, a fungus involved in pulmonary complications, as novel IgE-binding proteins. We show that these Trx, including the human enzyme, represent cross-reactive structures recognized by serum IgE from individuals sensitized to M. sympodialis Trx. Moreover, all three proteins were able to elicit immediate-type allergic skin reactions in sensitized individuals, indicating a humoral immune response based on molecular mimicry. To analyze structural elements involved in these reactions, the three-dimensional structure of M. sympodialis Trx (Mala s 13) has been determined at 1.4-Å resolution by x-ray diffraction analysis. The structure was solved by molecular replacement and refined to a crystallographic R factor of 14.0% and a free R factor of 16.8% and shows the typical Trx fold. Mala s 13 shares 45% sequence identity with human Trx and superposition of the solved Mala s 13 structure with those of human Trx reveals a high similarity with a root mean square deviation of 1.11 Å for all Cα atoms. In a detailed analysis of the molecular surface in combination with sequence alignment, we identified conserved solvent-exposed amino acids scattered over the surface in both structures which cluster to patches, thus forming putative conformational B cell epitopes potentially involved in IgE-mediated cross- and autoreactivity.

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Section: Discussionmentioning

confidence: 99%

Cross-Reactivity and 1.4-Å Crystal Structure ofMalassezia sympodialisThioredoxin (Mala s 13), a Member of a New Pan-Allergen Family

Limacher¹,

Glaser²,

Meier³

et al. 2007

The Journal of Immunology

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“…This condition has been termed lipid transfer protein syndrome [5] and is a consequence of the high degree of IgE cross-reactivity between lipid transfer proteins (LTPs), including those that are taxonomically distant [6][7][8]. Among the peculiarities of this syndrome are its geographical distribution (limited to the Mediterranean area), the frequent need for cofactors to elicit clinical reactivity, and reduced severity when pollen allergy is present [2,4].…”

Section: Introductionmentioning

confidence: 99%

Lettuce Allergy Is a Lipid Transfer Syndrome-Related Food Allergy With a High Risk of Severe Reactions

Muñoz-García¹,

Luengo²,

Moreno-Pérez³

et al. 2017

J Investig Allergol Clin Immunol

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Background and Objectives: Lipid transfer protein (LTP) sensitization is the most common cause of food allergy in the Mediterranean area, with peach allergy acting as the primary sensitizer in most cases. Lettuce has been described as a common offending food in patients with LTP syndrome. The aim of the study was to investigate the frequency and clinical expression of LTP syndrome in a sample of lettuceallergic patients. Methods: We determined specific IgE to Pru p 3 and lettuce in a sample of 30 patients with a diagnosis of lettuce allergy. Symptoms elicited by other LTP-containing plant-derived foods and the presence of cofactors were assessed. Results: The clinical symptoms of lettuce allergy were frequently severe, with 18 of the 30 patients experiencing anaphylaxis. All the patients had allergic reactions to other plant foods. Cofactors were involved in the clinical reactions of 13 of the 30 patients. Sensitization to pollens was found in 90% of patients. Conclusions: Lettuce allergy is found not as an isolated condition but in the context of LTP syndrome and it is characterized by severe reactions and frequent cofactor association.

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“…Thus, skin prick test (SPT) responses to the major peach LTP allergen Pru p 3 have been found positive in 60–90% of Spanish patients with allergy to this fruit [12, 13]. On the other hand, extensive cross-reactivity among allergenic LTPs from different foods is now well established, both in vitro and in vivo [10, 14]. …”

Section: Introductionmentioning

confidence: 99%

Lipid Transfer Proteins and Allergy to Oranges

Ahrazem¹,

Ibáñez

López‐Torrejón³

et al. 2005

Int Arch Allergy Immunol

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Background: Lipid transfer proteins (LTPs) are relevant fruit allergens, recently proposed as model plant food allergens. No citrus fruit allergen has been characterized to date. We sought to identify and isolate citrus fruit LTPs and to explore their relevance in orange allergy. Methods: Twenty-seven patients, showing mainly oral allergy syndrome after orange ingestion, as well as positive prick responses and serum-specific IgE levels to orange, were selected. Natural orange and lemon LTPs, as well as a recombinant orange LTP isoform expressed in Pichia pastoris, were isolated by chromatographic methods and characterized by N-terminal amino acid sequencing and matrix-assisted laser desorption/ionizaion mass spectrometry, and DNA sequencing of the corresponding cDNA in the case of the recombinant allergen. Specific IgE determination, immunodetection, ELISA-inhibition assays and in vivo skin prick tests (SPTs) were performed with all three purified allergens and with the major peach LTP allergen, Pru p 3. Results: The natural allergens purified from orange (nCit s 3) and lemon (nCit l 3) showed very similar N-terminal amino acid sequences (18 out of 20 identical residues), typical of LTPs, and molecular masses of 9,610 and 9,618 Da, respectively. The recombinant orange isoform (rCit s 3) expressed in P. pastoris (16 out of 20 residues identical to its natural counterpart in the N-terminal region) presented 92 amino acid residues and 9,463 Da, and 67% sequence identity with rPru p 3. Of the 27 sera analyzed, specific IgE to the purified allergens was found in 54% for nCit l 3, 48% for nCit s 3, 46% for rCit s 3 and 37% for rPru p 3. Positive SPT responses were obtained in 7 out of 26 patients tested for nCit s 3, 3 out of 8 for nCit l 3 and 10 out of 26 for nPru p 3. ELISA-inhibition assays showed an equivalent IgE-binding pattern for the natural and recombinant orange LTPs, and IgE cross-reactivity among the purified orange, lemon and peach LTP allergens. Conclusions: Members of the LTP allergen family are involved in allergy to oranges, displaying positive in vitro and in vivo reactions in 30–50% of the patients studied. Both orange and lemon allergens show cross-reactivity with the major peach allergen Pru p 3.

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Immunological cross‐reactivity between lipid transfer proteins from botanically unrelated plant‐derived foods: a clinical study

Cited by 160 publications

References 37 publications

Cross-Reactivity and 1.4-Å Crystal Structure ofMalassezia sympodialisThioredoxin (Mala s 13), a Member of a New Pan-Allergen Family

Cross-Reactivity and 1.4-Å Crystal Structure ofMalassezia sympodialisThioredoxin (Mala s 13), a Member of a New Pan-Allergen Family

Lettuce Allergy Is a Lipid Transfer Syndrome-Related Food Allergy With a High Risk of Severe Reactions

Lipid Transfer Proteins and Allergy to Oranges

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