Method Article

Analysis of N-glycans from Raphanus sativus Cultivars Using PNGase H+

DOI:

10.3791/57979

June 25th, 2018

In This Article

Summary

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We describe a simple and rapid method for the preparation and analysis of N-glycans from different cultivars of radish (Raphanus sativus).

Abstract

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In recent years, the carbohydrate moieties of plants have received considerable attention, as they are a potential source of cross-reactive, allergy-provoking immune responses. In addition, carbohydrate structures also play a critical role in plant metabolism. Here, we present a simple and rapid method for preparing and analyzing N-glycans from different cultivars of radish (Raphanus sativus) using an N-glycanase specific for the release of plant-derived carbohydrate structures. To achieve this, crude trichloroacetic acid precipitates of radish homogenates were treated with PNGase H+, and labeled using 2-aminobenzamide as a fluorescent tag. The labeled N-glycan samples were subsequently analyzed by ultra performance liquid chromatography (UPLC) separation and matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) mass spectrometry for a detailed structural evaluation and to quantify relative abundancies of the radish-derived N-glycan structures. This protocol can also be used for the analysis of N-glycans from various other plant species, and may be useful for further investigation of the function and effects of N-glycans on human health.

Introduction

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N-glycans in plants have drawn increased attention in recent years, as previous research has highlighted N-glycans as a potential source of immunological cross-reactions that may provoke allergic responses1,2. It has been demonstrated previously that N-glycans on plant glycoproteins can affect catalytic activity3,4, thermostability and folding5,6 or subcellular localization and secretion7. In order to correlate the glycan structures with their ....

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Protocol

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1. Sample collection

  1. Purchase different cultivars of fresh radish (Raphanus sativus L.).

2. Isolation of Protein from Radish

  1. Homogenize approximately 100 g of fresh radish with a kitchen blender for 10 min.
  2. Transfer the slurry to a 50 mL centrifuge tube and centrifuge at 14,000 × g at 4 °C for 20 min to remove the insoluble material.
  3. Transfer the supernatant carefully into a new 50 mL centrifuge tube and add an equal volume of 2 M trichloroacetic acid (TCA) solution.
    NOTE: Adding TCA will precipitate soluble (glyco)proteins.
  4. Centrifuge at 14,000 ....

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Results

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Figure 1 shows a schematic overview of the described protocol, including the isolation of (glyco-)proteins from radish, the preparation of N-glycans, the UPLC analysis, and the MALDI-TOF-MS analysis of these components. Figure 2 shows representative UPLC chromatograms of derivatized N-glycans of the analyzed radish cultivars. Figure 3 shows the obtained results of the 2AB-derivatize.......

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Discussion

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The protocol we have presented here allows the comparison of the N-glycan profiles of various cultivars of radish. A significant advantage of this method compared to existing protocols is that no buffer changes between the enzymatic release of N-glycans and the derivatization reaction with 2-AB are required. The most critical step of this procedure is the purification of N-glycans using the SPE column, as failure to remove salts or other impurities in the reaction mixture may negatively impact .......

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Disclosures

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The authors have nothing to disclose.

Acknowledgements

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This work was supported in part by the Natural Science Foundation of China (grant numbers 31471703, A0201300537 and 31671854 to J.V. and L.L., grant number 31470435 to G.Y.), and the 100 Foreign Talents Plan (grant number JSB2014012 to J.V.).

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Materials

List of materials used in this article
NameCompanyCatalog NumberComments
Chemicals:
Trichloroacetic acid SCR, Shanghai80132618
Acetic acid glacialHuada, Guangzhou64-19-7
AcetonitrileGeneral-reagentG80988C
Trifluoroacetic acidEnergy chemicalW810031
2-aminobenzamideHeowns, TianjinA41900
Sodium cyanoborohydrideJ&K Scientific Ltd314162
Dimethyl sulfoxideHuada, Guangzhou67-68-5
2AB-labeled dextran ladder, 200 pmolAgilent TechnologiesAT-5190-6998
6-Aza-2-thiothymine Sigma275514
Tools/Materials:
Kitchen blenderBear, GuangzhouLLJ-A10T1
CentrifugeTechcompCT15RT
Centrifugal EvaporatorHualida, TaicangLNG-T120
SPE columnSupelcoSupelclean ENVI Carb SPE column
MALDI-TOF mass spectrometerBrukerAutoflex
HPLC Analysis:
High-recovery HPLC vialAgilent Technologies # 5188-2788
HPLC SystemShimadzuNexera
Fluorescence Detector for HPLCShimadzuRF-20Axs 
Column ovenHengxinCO-2000
HPLC ColumnWatersAcquity UPLC BEH glycan column2.1 × 150 mm, 1.7 μm particle size
LCMS-grade WaterMerck Millipore#WX00011
LCMS-grade AcetonitrileMerck Millipore# 100029
Formic acidAladdinF112034
Ammonia solutionAladdinA112080

References

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  1. Altmann, F. The Role of Protein Glycosylation in Allergy. International Archives of Allergy and Immunology. 142 (2), 99-115 (2007).
  2. Van Ree, R., et al. β (1, 2)-xylose and α (1, 3)-fucose residues have a strong contribution in IgE binding to plant glycoallergens. Journal of Biological Chemistry<....

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Tags

N Glycan AnalysisRadish CultivarsUPLC SeparationMALDI TOF Mass Spectrometry2 Aminobenzamide LabelingSolid Phase ExtractionTrichloroacetic Acid PrecipitationFluorescence DerivatizationPlant Glycoscience

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