Data on mass spectrometry based identification of allergens from sunflower (Helianthus annuus L.) pollen proteome.

Nandini Ghosh,Gaurab Sircar,Bodhisattwa Saha,Naren Pandey,Swati Gupta Bhattacharya

doi:10.1016/j.dib.2016.03.023

Abstract

Allergy is a type of abnormal immune reactions, which is triggered by environmental antigens or allergens and mediated by IgE antibodies. Now-a-days mass spectrometry is the method of choice for allergen identification based on homology searching. Here, we provide the mass spectrometry dataset associated with our previously published research article on identification of sunflower pollen allergens (Ghosh et al., 2015 [1]). In this study allergenicity of sunflower (Helianthus annuus) pollen grains were primarily investigated by clinical studies followed by detailed immunobiochemical and immunoproteomic analyses. The mass spectrometry data for the identification of allergens were deposited to ProteomeXchange Consortium via PRIDE partner repository with the dataset identifier PXD002397.

Highlights

MALDI-TOF/TOF (Autoflex II, Bruker Daltonics, Germany) and LC-ESI qTOF analysis of in-gel digested proteins Analyzed mass spectrometry data Total pollen proteome of Helianthus annuus was confronted with pooled sera of sunflower pollen-sensitized patients
Allergenic proteins were excised from 2 Dimensional (2D) gel, and in-gel digested spots were identified using a combination of two different mass spectrometric techniques (MALDI TOF/TOF and LC-ESI qTOF) and searching the MS/MS data against NCBInr database and EST library of H. annuus
Using bottom-up proteomic approach we have previously identified sunflower pollen allergens [1]

Summary

Data accessibility

MALDI-TOF/TOF (Autoflex II, Bruker Daltonics, Germany) and LC-ESI qTOF (maXis Impact, Bruker Daltonics, Germany) analysis of in-gel digested proteins Analyzed mass spectrometry data Total pollen proteome of Helianthus annuus was confronted with pooled sera of sunflower pollen-sensitized patients. Allergenic proteins were excised from 2D gel, and in-gel digested spots were identified using a combination of two different mass spectrometric techniques (MALDI TOF/TOF and LC-ESI qTOF) and searching the MS/MS data against NCBInr database and EST library of H. annuus. Unmatched peptides with low significance score were further subjected to similarity searches against the H. annuus EST database Unmatched proteins, after MALDI-TOF/TOF, were subjected to LC-ESI qTOF for better peak resolution, maximum signal, and maximum coverage. Sera from selected sunflower positive patients were used as the probe to detect the IgE-reactive proteins from twodimensional electrophoretic separated proteome of sunflower pollen

Pollen sampling and protein extraction

Patient selection and clinical studies

Sample preparation for mass spectrometry

LC-ESI qTOF analysis

Database search and allergen identification