Role of carbohydrate moieties in IgE binding to allergenic components of <i>Cupressus arizonica </i>pollen extract

Afferni, Claudia; Iacovacci, Patrizia; Barletta, Bianca; Felice, Gabriella Di; Tinghino, Raffaella; Mari, Adriano; Pini, Carlo

doi:10.1046/j.1365-2222.1999.00590.x

Cited by 45 publications

(40 citation statements)

References 42 publications

(53 reference statements)

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“…From the comparison of their Asn-linked carbohydrate structures, the β(1,2)xylose residue and the α(1,3)fucose residue are proposed to be cross-reactive determinants. These carbohydrate residues have already been reported as cross-reactive epitopes on antigens in pollen and vegetable foods [27, 28, 29, 30]. Thus, it can be concluded that the CCDs of the latex β-1,3-glucanase isoenzymes are primarily responsible for the IgE-binding capacity and cross-reactivity observed in in vitro IgE tests.…”

Section: Discussionmentioning

confidence: 70%

Significance of Carbohydrate Epitopes in a Latex Allergen with β-1,3-Glucanase Activity

Yagami

Osuna

Kouno

et al. 2002

Int Arch Allergy Immunol

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Background: One of the latex allergens, Hev b 2, has β-1,3-glucanase activity. The entire sequence of this allergen is already known. There is one potential N-glycosylation site in this molecule (²⁷Asn). Heterogeneous glycosylation of this Asn residue could be a source of the multiplicity of natural Hev b 2. Possible participation of the carbohydrate epitopes of latex β-1,3-glucanase isoenzymes in their IgE-binding capacity and cross-reactivity was investigated in this study. Methods: β-1,3-Glucanase isoenzymes were separated based on their affinities for concanavalin A. IgE-binding capacity and cross-reactivity were examined by immunoblotting and enzyme-linked immunosorbent assay (ELISA). Sequence heterogeneity among the isoenzymes was probed by peptide mass mapping after lysyl endopeptidase digestion. To clarify the relation to Hev b 2, N-terminal sequencing was performed on a fragmented peptide common to the separated isoenzymes. Results: Basic β-1,3-glucanase was subdivided into two glycosylated isoenzymes (GI and GII) and one non-glycosylated isoenzyme (GIII). IgE antibodies in latex-positive sera chiefly recognized the glycosylated isoenzymes. Inhibition ELISA supported the significance of the carbohydrate epitopes for the IgE recognition and cross-reactivity. However, non-glycosylated GIII, as well as GI and GII, produced positive results in a skin prick test. The three β-1,3-glucanase isoenzymes shared a partial sequence in common with Hev b 2. Conclusions: Our results suggest that the carbohydrate epitopes in Hev b 2 homologues are relevant to an in vitro diagnosis of latex allergy and the accompanying cross-reactivity. Carbohydrate epitopes do not necessarily provoke allergic symptoms. Therefore, the actual allergenicity of Hev b 2 and its homologues should be carefully evaluated not only by in vitro IgE tests but also by in vivo tests.

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Section: Discussionmentioning

confidence: 70%

Significance of Carbohydrate Epitopes in a Latex Allergen with β-1,3-Glucanase Activity

Yagami

Osuna

Kouno

et al. 2002

Int Arch Allergy Immunol

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“…Polygalacturonase, pollen-specific protein C13 (Os09g39950), ␤-expansin Os-EXPB13, and ␤-expansin have been well documented as pollen allergens (43)(44)(45). Previous investigations showed that most pollen allergens were glycoproteins, whereas glycan probably contributes to their allergenic activity (46). And Os09g39950 contains the function domain pfam01190 of the Ole e I family, and its homolog Ole e10 from olive pollen tubes has been detected to bind 1,3-␤-glucans preferentially (45).…”

Section: Identification Of Proteins Involved In Pollen Germinationmentioning

confidence: 99%

Proteomics Identification of Differentially Expressed Proteins Associated with Pollen Germination and Tube Growth Reveals Characteristics of Germinated Oryza sativa Pollen

Dai

Chen

Chong

et al. 2007

Molecular & Cellular Proteomics

138

134

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Mature pollen from most plant species is metabolically quiescent; however, after pollination, it germinates quickly and gives rise to a pollen tube to transport sperms into the embryo sac. Because methods for collecting a large amount of in vitro germinated pollen grains for transcriptomics and proteomics studies from model plants of Arabidopsis and rice are not available, molecular information about the germination developmental process is lacking. Here we describe a method for obtaining a large quantity of in vitro germinating rice pollen for proteomics study. Two-dimensional electrophoresis of ϳ2300 protein spots revealed 186 that were differentially expressed in mature and germinated pollen. Most showed a changed level of expression, and only 66 appeared to be specific to developmental stages. Furthermore 160 differentially expressed protein spots were identified on mass spectrometry to match 120 diverse protein species. These proteins involve different cellular and metabolic processes with obvious functional skew toward wall metabolism, protein synthesis and degradation, cytoskeleton dynamics, and carbohydrate/energy metabolism. Wall metabolism-related proteins are prominently featured in the differentially expressed proteins and the pollen proteome as compared with rice sporophytic proteomes. Our study also revealed multiple isoforms and differential expression patterns between isoforms of a protein. These results provide novel insights into pollen function specialization. Pollen of flowering plants, generated in diploid sporophytic plants via meiosis followed by two cycles of mitosis, contains three haploid genomes and is a highly reduced organism. Mature pollen grains from most plant species are metabolically quiescent. However, during pollination, they can quickly germinate and give rise to a polarly growing pollen tube whereby the pollen interacts with pistils and then delivers two sperms into the embryo sac to initiate double fertilization. Besides having biological importance, pollen germination and tube growth have been considered unique developmental processes for studying cell polar establishment, cell differentiation, cell fate determination, and cell-to-cell recognition. Thus, the molecular mechanisms underlining the specific cellular programs have been the focus of investigation over the past 50 years (1). However, until now, only a limited number of genes encoding coat/wall proteins or signal molecules have been shown to be essential for pollen germination, tube growth, and interaction of the tube and stigma (1-7).Recent analyses of mature pollen of Arabidopsis revealed the transcriptome to have reduced complexity and a higher proportion of selectively expressed transcripts than sporophytic tissues (8 -10). As well, about one-third of the genes expressed in vegetative tissues are not expressed in the pollen (8). The observation suggests that the transcriptional characteristics involve pollen function specialization. Furthermore these studies determined that pollen transcriptome has a functiona...

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“…These structures could also explain the presence of specific IgE antibodies to allergens in the sera of patients without evidence of previous exposure to the allergenic source. The presence of CCDs recognised by human IgE has been reported for the purified major allergen of C. japonica, Cry j 1 [43, 44], and for C. arizonica pollen extract [76]and the purified major allergen Cup a 1 [53]. In these cases, deglycosylation treatment of the glycoallergens results in a reduced IgE-binding capability.…”

Section: Allergenic Cross-reactivitymentioning

confidence: 99%

Cupressaceae Pollinosis: Identification, Purification and Cloning of Relevant Allergens

Felice

Barletta

Tinghino

et al. 2001

Int Arch Allergy Immunol

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Allergy to Cupressaceae pollen is a worldwide pollinosis caused by several species. Pollen extracts prepared from allergenic species belonging to this family are characterised by low protein and high carbohydrate content. The allergenic components represented in the pollen extracts from different species of the Cupressaceae family show high levels of cross-reactivity when probed with human IgE from allergic subjects and share a number of common epitopes also identified by polyclonal rabbit antisera and monoclonal antibodies. A close relationship has also been described with the Taxodiaceae and Podocarpaceae families. Although both proteic and carbohydrate epitopes appear to be involved in IgE recognition and allergenic cross-reactivity, a large portion of the IgE reactivity of Cupressaceae-allergic patients seems to be associated with sugar moieties present on the relevant allergenic molecules. From this point of view, Cupressaceae/Taxodiaceae allergens constitute a particularly useful model to study IgE cross-reactivity, as they have been shown to display different levels of homology. Moreover, the availability of the purified allergens, together with their recombinant counterparts, may shed light on the actual role played by carbohydrate in allergic sensitisation, IgE recognition and allergenic cross-reactivity.

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Role of carbohydrate moieties in IgE binding to allergenic components of Cupressus arizonica pollen extract

Cited by 45 publications

References 42 publications

Significance of Carbohydrate Epitopes in a Latex Allergen with β-1,3-Glucanase Activity

Significance of Carbohydrate Epitopes in a Latex Allergen with β-1,3-Glucanase Activity

Proteomics Identification of Differentially Expressed Proteins Associated with Pollen Germination and Tube Growth Reveals Characteristics of Germinated Oryza sativa Pollen

Cupressaceae Pollinosis: Identification, Purification and Cloning of Relevant Allergens

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