Dataset Information

Low Molecular Weight Allergens from English Walnut (Juglans Regia)

ABSTRACT: Low molecular weight (LMW) proteins were purified from English walnuts (J. regia cv. Chandler). The LMW proteins were separated by anion exchange chromatography. The anion exchange fractions were analyzed by SDS-PAGE, and protein bands were excised. In gel trypsin digestion was conducted (following reduction with DTT and alkylation with iodoacetamide). Peptides were separated by RP-HPLC and analyzed with an LTQ Orbitrap XL. Peptide and protein identifications were obtained with Mascot.

INSTRUMENT(S): LTQ Orbitrap, instrument model

ORGANISM(S): Juglans Regia (english Walnut)

TISSUE(S): Plant Cell, Seed

SUBMITTER: Melanie Downs

LAB HEAD: E.N. Clare Mills

PROVIDER: PXD000634 | Pride | 2019-11-28

REPOSITORIES: Pride

ACCESS DATA

Publications

Characterization of low molecular weight allergens from English walnut (Juglans regia).

Downs Melanie L ML Semic-Jusufagic Aida A Simpson Angela A Bartra Joan J Fernandez-Rivas Montserrat M Rigby Neil M NM Taylor Steve L SL Baumert Joseph L JL Mills E N Clare EN

Journal of agricultural and food chemistry 20141120 48

Although English walnut is a commonly allergenic tree nut, walnut allergens have been poorly characterized to date. The objective of this work was to characterize the natural, low molecular weight (LMW) allergens from walnut. A protocol was developed to purify LMW allergens (specifically 2S albumins) from English walnuts. In addition to 2S albumins, a series of peptides from the N-terminal region of the 7S seed storage globulin proprotein were also identified and characterized. These peptides co ...[more]

PMID: 25388987

Similar Datasets

Project description:Background: Respiratory allergy triggered by pollen allergens is increasing at an alarming rate worldwide. Sunflower pollen is thought to be an important source of inhalant allergens. Present study aims to identify the prevalence of sunflower pollinosis among the Indian allergic population and characterizes the pollen allergens using immuno-proteomic tools. Methodology: Clinico-immunological tests were performed to understand the prevalence of sensitivity towards sunflower pollen among the atopic population. Sera from selected sunflower positive patients were used as probe to detect the IgE-reactive proteins from the one and two dimensionally separated proteome of sunflower pollen. The antigenic nature of the sugar moiety of the glycoprotein allergens was studied by meta-periodate modification of IgE-immunoblot. Finally, these allergens were identified by mass-spectrometry (MALDI TOF/TOF and LC ESI qTOF). MASCOT searching was performed against NCBInr database. However, Helianthus annuus genome is not fully sequenced and partially annotated. So in case of low confidence (p> 0.05) protein identification, searching was performed against EST library of Helianthus annuus. Results: Prevalence of sunflower pollen allergy was observed among 21% of the atopic population and associated with elevated level of specific IgE and histamine in the sera of these patients. Immunoscreening of sunflower pollen proteome with patient serum detected seven IgE-reactive proteins with varying molecular weight and pI. Hierarchical clustering of 2D-immunoblot data highlighted three allergens characterized by a more frequent immuno-reactivity and increased levels of IgE antibodies in the sera of susceptible patients. These allergens were considered as the major allergens of sunflower pollen and were found to have their glycan moiety critical for inducing IgE response. Homology driven search of MS/MS data of these IgE-reactive proteins identified seven previously unreported allergens from sunflower pollen. Three major allergenic proteins were identified as two non-isoformic pectate lyases and a cystein protease. Conclusion: Novelty of the present report is the identification of a panel of seven sunflower pollen allergens for the first time at immuno-biochemical and proteomic level, which substantiated the clinical evidence of sunflower allergy. Further purification and recombinant expression of these allergens will improve component-resolved diagnosis and therapy of pollen allergy.

Dataset Information

Low Molecular Weight Allergens from English Walnut (Juglans Regia)

Publications

Characterization of low molecular weight allergens from English walnut (Juglans regia).

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure