The maize major allergen, which is responsible for food-induced allergic reactions, is a lipid transfer protein

Pastorello, Elide A.; Farioli, Laura; Pravettoni, Valerio; Ispano, Marco; Scibola, Elisabetta; Trambaioli, Chiara; Giuffrida, Maria Gabriella; Ansaloni, Raffaella; Godovac‐Zimmermann, Jasminka; Conti, Amedeo; Fortunato, Donatella; Ortolani, Claudio

doi:10.1067/mai.2000.108712

Cited by 177 publications

(146 citation statements)

References 26 publications

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“…Since no IgEreactive epitope could be identified for Phl p 3 and Phl p 2 by peptide mapping, we assume the presence of conformational epitopes in those allergens [35]. Interestingly, we did not identify allergens belonging to the lipid transfer proteins and albumins/globulins, which were determined as major allergens in maize flour [37,38]. Probably, these allergens are not expressed in pollen or they might not have been detected by patients' sera from the northern part of Germany.…”

Section: Discussionmentioning

confidence: 80%

Proteome analysis of maize pollen for allergy-relevant components

et al. 2006

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Over the last few decades, the cultivation of maize (Zea mays) has strongly increased in Central Europe. We therefore decided to study the allergen composition and the allergenic potency of its pollen in comparison with pollen from timothy grass (Phleum pratense), a typical representative of the native grasses. We found that 65% of the sera reactive to timothy pollen also bound to maize pollen proteins. By using 2-DE immunoblotting, followed by incubation with mAbs directed against known allergens or protein sequencing, those IgE-reactive components were further classified. Although novel, maize-specific pollen allergens could not be found, the presence of crossreacting allergens belonging to groups 1 and 13 (Zea m 1 and 13), both having high IgE prevalence, as well as the presence of the less important group 3 and 12 allergens was found. The structural variability of Zea m 1 and Zea m 13 was determined by sequencing clones isolated from a maize pollen cDNA library. This revealed sequence identities of 72 and 70%, respectively, to the corresponding Phl p 1 and Phl p 13 allergens of timothy grass pollen. IgE-crossreactivity was further studied using immunoblot inhibition tests. Here, timothy pollen extract completely blocked IgE binding to maize, whereas maize pollen extract blocked IgE reactivity to only some timothy pollen allergens.

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Section: Discussionmentioning

confidence: 80%

Proteome analysis of maize pollen for allergy-relevant components

et al. 2006

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“…It has recently been confirmed that nsLTPs lack any specificity for fatty acids, phospholipids or the cutin monomers (Douliez et al 2001). With respect to food allergies, most of the nsLTP allergens identified to date belong to the nsLTP1 subfamily, whose members have been identified as major allergens in several Rosaceae fruits, including peach (Pastorello et al 1999b;Ballmer-Weber 2002), apple (Pastorello et al 1999a;Diaz-Perales et al 2002), apricot (Pastorello et al 2000a(Pastorello et al , 2000b, plum ) and cherry (Scheurer et al 2001). The prevalence of allergies to nsLTP-containing fruits is especially high in Mediterranean communities (Ballmer-Weber 2002).…”

Section: Communicated By R Hagemannmentioning

confidence: 99%

Linkage map positions and allelic diversity of two Mal d 3 (non-specific lipid transfer protein) genes in the cultivated apple (Malus domestica)

et al. 2005

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Non-specific lipid transfer proteins (nsLTPs) of Rosaceae fruits, such as peach, apricot, cherry, plum and apple, represent major allergens for Mediterranean atopic populations. As a first step in elucidating the genetics of nsLTPs, we directed the research reported here towards identifying the number and location of nsLTP (Mal d 3) genes in the apple genome and determining their allelic diversity. PCR cloning was initially performed on two cultivars, Prima and Fiesta, parents of a core apple mapping progeny in Europe, based on two Mal d 3 sequences (AF221502 and AJ277164) in the GenBank. This resulted in the identification of two distinct sequences (representing two genes) encoding the mature nsLTP proteins. One is identical to accession AF221502 and has been named Mal d 3.01, and the other is new and has been named Mal d 3.02. Subsequent genome walking in the upstream direction and DNA polymorphism analysis revealed that these two genes are intronless and that they could be mapped on two homoeologous segments of linkage groups 12 and 4, respectively. Further cloning and sequencing of the coding and upstream region of both Mal d 3 genes in eight cultivars was performed to identify allelic variation. Assessment of the deduced nsLTP amino acid sequences gave a total of two variants at the protein level for Mal d 3.01 and three for Mal d 3.02. The consequences of our results for allergen nomenclature and the breeding of low allergenic apple cultivars are discussed.

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“…IE-HPLC with a cationic column was employed for the purification of a major allergen of maize seed responsible for food-induced allergic reactions [55]. The column was eluted with a salt gradient in a sodium citrate buffer at pH 6 and the allergens were detected at 280 nm.…”

Section: Ie-hplcmentioning

confidence: 99%

“…[ 55] tional RP octadecyl silica columns (C-18) were used with IDs ranging from 2.1 to 4.6 mm, although a C-18 capillary column with an ID of 0.3 mm has been employed for the nanogram scale separation of a crude extract of acidsoluble proteins from maize kernels [2]. Replacement of conventional analytical scale chromatography by capillary liquid chromatography (0.05 -0.3 mm ID capillary columns) brings some benefits to the separation process, such as higher sensitivity and lower sample and mobilephase consumption [46].…”

Section: Hplc For the Analysis Of Maize Proteinsmentioning

confidence: 99%

High-performance liquid chromatography and capillary electrophoresis for the analysis of maize proteins

Rodríguez‐Nogales¹,

García²,

Marina³

2006

J. Sep. Science

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ReviewHigh-performance liquid chromatography and capillary electrophoresis for the analysis of maize proteinsMethods for the analysis of maize proteins using HPLC and CE are reviewed. Most of the references cited in this review concern HPLC methods. Size-exclusion HPLC and especially RP-HPLC methods have been developed for characterization of normal and genetically modified maize, cultivar differentiation, and prediction of quality. Few CE methods for the analysis of maize proteins were found in the existing literature. Most of these methods focus on optimization of the separation of maize proteins using CZE and SDS-capillary gel electrophoresis.

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The maize major allergen, which is responsible for food-induced allergic reactions, is a lipid transfer protein

Cited by 177 publications

References 26 publications

Proteome analysis of maize pollen for allergy-relevant components

Proteome analysis of maize pollen for allergy-relevant components

Linkage map positions and allelic diversity of two Mal d 3 (non-specific lipid transfer protein) genes in the cultivated apple (Malus domestica)

High-performance liquid chromatography and capillary electrophoresis for the analysis of maize proteins

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