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A Comparative Approach to Characterize the Landscape of Host-Pathogen Protein-Protein Interactions
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A human lectin array for characterizing host-pathogen interactions.

Stefi V Benjamin1, Sabine A F Jégouzo1, Chloe Lieng1

  • 1Department of Life Sciences, Imperial College London, London, United Kingdom.

The Journal of Biological Chemistry
|October 9, 2024
PubMed
Summary
This summary is machine-generated.

A novel human lectin array enables comprehensive screening of innate immune receptor interactions with various microorganisms. This tool reveals previously unknown glycan-binding specificities, advancing our understanding of host-microbe interactions.

Keywords:
array screeningcarbohydrate-binding proteinglycan-binding receptorsglycobiologyhost-pathogen interactioninnate immunitylectin

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Area of Science:

  • Immunology
  • Glycobiology
  • Microbiology

Background:

  • Innate immune receptors, including lectins, play a crucial role in host defense against pathogens.
  • Understanding the specific interactions between lectins and microbial glycans is essential for deciphering immune responses.
  • Existing methods often lack the breadth to screen diverse lectin families and microbial targets simultaneously.

Purpose of the Study:

  • To develop and validate a human lectin array for high-throughput screening of glycan-binding proteins.
  • To investigate the interactions between various human lectin classes and a range of microorganisms.
  • To identify novel and unexpected binding specificities between lectins and microbial glycans.

Main Methods:

  • Construction of a human lectin array featuring C-type carbohydrate-recognition domains (CRDs) and other lectin classes (galectins, siglecs, etc.).
  • Bioti n-tagged CRDs displayed on a streptavidin-coated surface for defined orientation and accessibility.
  • Development of methods for detecting both labeled and unlabeled microbial binding, including viral glycoproteins and polysaccharides.

Main Results:

  • The array successfully screened interactions between multiple human lectin classes and diverse microorganisms.
  • New binding interactions were identified, including high-affinity binding of some galectins to bacterial glycans lacking common motifs.
  • The platform demonstrated an unbiased approach to identifying lectin-glycan interactions.

Conclusions:

  • The human lectin array is a powerful tool for a comprehensive overview of innate immune glycan-binding protein interactions.
  • This array facilitates the discovery of novel host-microbe recognition mechanisms.
  • The findings highlight the complexity of innate immunity and the potential for new therapeutic targets.