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Dissecting Multivalent Lectin-Carbohydrate Recognition Using Polyvalent Multifunctional Glycan-Quantum Dots.

Yuan Guo, Inga Nehlmeier1, Emma Poole

  • 1Infection Biology Unit, German Primate Center , Kellnerweg 4, Gottingen 37077, Germany.

Journal of the American Chemical Society
|August 9, 2017
PubMed
Summary
This summary is machine-generated.

Quantum dots (QDs) with dense sugar arrays serve as powerful probes for multivalent protein-glycan interactions. These glycan-QDs effectively inhibit viral entry by dissecting lectin binding modes and quantifying affinities, aiding in the design of novel antiviral strategies.

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Area of Science:

  • Biochemistry
  • Nanotechnology
  • Virology

Background:

  • Multivalent protein-carbohydrate interactions are crucial for initial virus/bacteria-cell contact and infection.
  • Designing effective multivalent inhibitors is hindered by a lack of structural data on flexible, complex cell surface proteins.
  • Lectins like DC-SIGN and DC-SIGNR play key roles in viral entry augmentation for HIV and Ebola virus.

Purpose of the Study:

  • To develop quantum dots (QDs) displaying dense arrays of mono-/disaccharides as probes for multivalent protein-glycan interactions.
  • To utilize these glycan-QDs to dissect binding modes and quantify affinities of lectins DC-SIGN and DC-SIGNR.
  • To evaluate the potential of glycan-QDs as inhibitors of DC-SIGN-mediated viral entry.

Main Methods:

  • Synthesis of quantum dots (QDs) functionalized with a dense array of mono-/disaccharides.
  • Employing a combination of Förster resonance energy transfer (FRET), hydrodynamic size measurements, and transmission electron microscopy (TEM) to analyze QD-lectin interactions.
  • Developing a QD-FRET method for quantifying binding affinities between QDs and DC-SIGN/DC-SIGNR.

Main Results:

  • Glycan-QDs successfully differentiated between tetra-, di-, and monovalent binding modes of DC-SIGN and DC-SIGNR.
  • A QD-FRET assay revealed that DC-SIGN binds to the QDs over 100-fold tighter than DC-SIGNR.
  • Glycan-QDs demonstrated potent inhibition of DC-SIGN-mediated enhancement of EBOV-GP transduction, with IC50 values as low as 0.7 nM.

Conclusions:

  • Glycan-displaying QDs are versatile tools for dissecting complex multivalent protein-ligand recognition.
  • The developed QD-FRET method accurately quantifies binding affinities and differentiates lectin binding modes.
  • Glycan-QDs show promise as effective inhibitors of viral infection by targeting specific protein-glycan interactions at the cellular level.