Molecular characterization of Api g 2, a novel allergenic member of the lipid‐transfer protein 1 family from celery stalks

Gadermaier, Gabriele; Egger, Matthias; Girbl, Tamara; Erler, Anja; Harrer, Andrea; Vejvar, Eva; Liso, Marina; Richter, Klaus; Zuidmeer, Laurian; Mari, Adriano; Ferreira, Fátima

doi:10.1002/mnfr.201000443

Cited by 28 publications

(40 citation statements)

References 37 publications

(70 reference statements)

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The wide distribution of LTP1 in plant-derived foods, the recent evidence for food allergies induced by LTP1 from a number of botanically unrelated species distinct from Rosaceae (Ciardiello et al, 2010;Gadermaier et al, 2011;Krause et al, 2009;Pastorello et al, 2000;Pastorello et al, 2004;San Miguel-Moncin et al, 2003), and the demonstration of immunological cross-reactivity between LTP1 from such species (Asero et al, 2002(Asero et al, , 2004Tordesillas et al, 2009) indicate that these proteins represent plant pan-allergens. Allergenic LTP1 described so far are small (about 9 kDa) extracellular lipidbinding proteins that are ubiquitous in plants and whose biological function has not yet been precisely clarified.…”

Section: Introductionmentioning

confidence: 96%

Isoform identification, recombinant production and characterization of the allergen lipid transfer protein 1 from pear (Pyr c 3)

Ramazzina

Amato

Passera

et al. 2012

Gene

View full text Add to dashboard Cite

Section: Introductionmentioning

confidence: 96%

Isoform identification, recombinant production and characterization of the allergen lipid transfer protein 1 from pear (Pyr c 3)

Ramazzina

Amato

Passera

et al. 2012

Gene

View full text Add to dashboard Cite

“…We recently identified and characterized an nsLTP1 in celery stalks which was included as Api g 2.0101 in the official I.U.I.S. allergen nomenclature [8]. The natural protein consists of a single isoallergen with a mass of 9024.5 Da.…”

Section: Introductionmentioning

confidence: 99%

Sensitization Prevalence, Antibody Cross-Reactivity and Immunogenic Peptide Profile of Api g 2, the Non-Specific Lipid Transfer Protein 1 of Celery

et al. 2011

Self Cite

View full text Add to dashboard Cite

BackgroundCelery (Apium graveolens) represents a relevant allergen source that can elicit severe reactions in the adult population. To investigate the sensitization prevalence and cross-reactivity of Api g 2 from celery stalks in a Mediterranean population and in a mouse model.Methodology786 non-randomized subjects from Italy were screened for IgE reactivity to rApi g 2, rArt v 3 (mugwort pollen LTP) and nPru p 3 (peach LTP) using an allergen microarray. Clinical data of 32 selected patients with reactivity to LTP under investigation were evaluated. Specific IgE titers and cross-inhibitions were performed in ELISA and allergen microarray. Balb/c mice were immunized with purified LTPs; IgG titers were determined in ELISA and mediator release was examined using RBL-2H3 cells. Simulated endolysosomal digestion was performed using microsomes obtained from human DCs.ResultsIgE testing showed a sensitization prevalence of 25.6% to Api g 2, 18.6% to Art v 3, and 28.6% to Pru p 3 and frequent co-sensitization and correlating IgE-reactivity was observed. 10/32 patients suffering from LTP-related allergy reported symptoms upon consumption of celery stalks which mainly presented as OAS. Considerable IgE cross-reactivity was observed between Api g 2, Art v 3, and Pru p 3 with varying inhibition degrees of individual patients' sera. Simulating LTP mono-sensitization in a mouse model showed development of more congruent antibody specificities between Api g 2 and Art v 3. Notably, biologically relevant murine IgE cross-reactivity was restricted to the latter and diverse from Pru p 3 epitopes. Endolysosomal processing of LTP showed generation of similar clusters, which presumably represent T-cell peptides.ConclusionsApi g 2 represents a relevant celery stalk allergen in the LTP-sensitized population. The molecule displays common B cell epitopes and endolysosomal peptides that encompass T cell epitopes with pollen and plant-food derived LTP.

show abstract

“…A study on four species of Cassia showed that higher level of carbohydrates (11-15%) than lipids (8-12%) (Mondal et al 1998). There have been several reports where glycoproteins, polysaccharides and lipoproteins serve as effective allergens in pollen grains and food stuffs (Nilsen and Paulsen 1990;Batanero et al 1996;Kimura et al 2002;Gómez-Gómez et al 2010;Gadermaier et al 2011, Kuppannan et al 2011.…”

Section: Discussionmentioning

confidence: 98%

Aerobiological, clinical and immunobiochemical studies on Lantana camara pollen and cross-reactivity with other Verbenaceae pollen species

et al. 2011

View full text Add to dashboard Cite

Airborne pollen is an important and potent source of aeroallergens. The aim of the study was to conduct a 2-year aerobiological survey in Calcutta, India, for knowing the concentration and seasonal periodicity of Lantana camara (LC) pollen. The sensitization due to this pollen among seasonal respiratory allergic patients and its chemical composition was studied. An aerobiological survey was conducted with a volumetric Burkard sampler from 2004 to 2006. Protein components of LC pollen were characterized by sodium dodecyl sulfate polyacrylamide gel electrophoresis and IgE immunoblotting. Allergenic activities were determined by in vivo (skin prick test) and in vitro (enzyme-linked immunosorbent assay. In vitro inhibition tests were performed to evaluate crossreactivity. LC pollen was present from March to May and from September to December contributing up to 10.5% to the total aeropollen load during peak month. Horizontal profile showed highest concentration for nearest (0.5 m) rotorod and it was decreased by half in a distance within 4.5-6.5 m from plot edge. LC pollen contained 7.5% carbohydrate, 19.3% lipid with proline and valine as dominant amino acid. Among 1,500 adult respiratory allergic patients tested, 7.93% showed higher level of positive reaction. IgE binding proteins of 22, 42, 45 and 95 kD were revealed. LC pollen showed remarkable cross-reactivity with other local Verbenaceae pollen taxa (Clerodendron viscosum, Tectona grandis and Vitex negundo). This is the first study on LC pollen regarding its aerobiological, clinical and immuno-biochemical aspects; it should be helpful for the diagnosis and therapy of patients susceptible to LC pollen.

show abstract

Molecular characterization of Api g 2, a novel allergenic member of the lipid‐transfer protein 1 family from celery stalks

Cited by 28 publications

References 37 publications

Isoform identification, recombinant production and characterization of the allergen lipid transfer protein 1 from pear (Pyr c 3)

Isoform identification, recombinant production and characterization of the allergen lipid transfer protein 1 from pear (Pyr c 3)

Sensitization Prevalence, Antibody Cross-Reactivity and Immunogenic Peptide Profile of Api g 2, the Non-Specific Lipid Transfer Protein 1 of Celery

Aerobiological, clinical and immunobiochemical studies on Lantana camara pollen and cross-reactivity with other Verbenaceae pollen species

Contact Info

Product

Resources

About