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Genetically encoded multivalent liquid glycan array displayed on M13 bacteriophage.

Mirat Sojitra1, Susmita Sarkar1, Jasmine Maghera1

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This summary is machine-generated.

This study introduces a novel liquid glycan array (LiGA) platform for studying glycans using DNA sequencing. LiGA decodes optimal glycan structures and binding profiles for lectins in vitro and in vivo.

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Area of Science:

  • Glycomics and glycobiology
  • Molecular biology and biochemistry
  • Immunology and cell biology

Background:

  • Traditional DNA sequencing methods are incompatible with glycan analysis due to the central dogma of biology.
  • Understanding glycan structures and their interactions is crucial for various biological processes, including immunity.
  • Existing methods for glycan profiling are limited in scope and application.

Purpose of the Study:

  • To develop a novel platform, the liquid glycan array (LiGA), for high-throughput glycan analysis using DNA sequencing.
  • To characterize the glycan-binding profiles of lectins, such as CD22, in complex biological systems.
  • To identify optimal glycan structures and densities for lectin binding in vitro and in vivo.

Main Methods:

  • Construction of a liquid glycan array (LiGA) using DNA-barcoded M13 bacteriophages displaying modified glycans.
  • Synthesis of LiGA via acylation of phage pVIII protein and subsequent ligation of azido-modified glycans.
  • Pulldown assays with lectins, followed by deep sequencing of phage barcodes to decode glycan recognition.

Main Results:

  • The LiGA platform successfully displays a wide range of glycans (30-1,500 copies per phage) with high fidelity.
  • Deep sequencing of bound phages accurately decodes the optimal glycan structures and densities recognized by lectins.
  • LiGA enabled target-agnostic measurement of lectin-binding profiles, including CD22, on cells and immune cells in live mice.

Conclusions:

  • The liquid glycan array (LiGA) platform overcomes limitations in glycan analysis by integrating DNA sequencing.
  • LiGA provides a powerful tool for dissecting glycan-lectin interactions in diverse biological contexts, from cellular assays to in vivo studies.
  • This technology facilitates the identification of glycoconjugates with optimal avidity for lectin binding, advancing glycomics research.