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Author Spotlight: Advancing Protein Glycosylation Research Using a Fully Automated System
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A Quantitative Microtiter Assay for Sialylated Glycoform Analyses Using Lectin Complexes.

Karunya Srinivasan1, Sucharita Roy2, Nathaniel Washburn1

  • 1Momenta Pharmaceuticals, Inc., Cambridge, MA, USA.

Journal of Biomolecular Screening
|April 9, 2015
PubMed
Summary

A novel lectin-based ELISA assay quantifies terminal glycan structures on biotherapeutics, offering sensitivities comparable to mass spectrometry. This method provides a customizable, complementary tool for glycan analysis in biologics like Fc proteins and immunoglobulins.

Keywords:
ELISAIVIGglycoformlectinsialylation

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Area of Science:

  • Biochemistry
  • Analytical Chemistry
  • Biotechnology

Background:

  • Glycan structure fidelity is critical for biotherapeutic efficacy.
  • Existing glycan profiling methods (LC-MS) are data-intensive and require sample preparation.
  • Lectins on microarrays offer in situ glycoprofiling but need analyte labeling.

Purpose of the Study:

  • To develop a lectin-based microtiter assay (lectin-ELISA) for quantifying terminal glycan moieties.
  • To assess the assay's applicability to glycan-engineered Fc proteins and intact immunoglobulins (IVIG).
  • To compare the assay's performance with industry-standard LC-MS profiling.

Main Methods:

  • Development of a lectin-enzyme-linked immunosorbent assay (ELISA).
  • Application of the assay to Fc proteins and IVIG samples.
  • Validation of results using liquid chromatography-mass spectrometry (LC-MS).

Main Results:

  • The lectin-ELISA accurately quantifies terminal glycan moieties.
  • The assay can differentiate single- versus dual-arm glycosylation.
  • Sensitivity is comparable to mass spectrometry, with customizable lectin panels.
  • Results are corroborated by LC-MS profiling.

Conclusions:

  • The developed lectin-ELISA is a versatile tool for quantitative glycan analysis.
  • It can be used independently or alongside MS for biologics.
  • The assay is extendable to various biotherapeutics, enhancing glycan characterization.