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Development and application of a high-content virion display human GPCR array.

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Area of Science:

  • Biochemistry
  • Immunology
  • Microbiology

Background:

  • Human G protein-coupled receptors (GPCRs) are crucial cell surface proteins involved in numerous physiological processes.
  • Studying GPCRs is challenging due to their reliance on membrane environments for proper folding and function.
  • Existing methods for GPCR characterization are often limited in throughput and scope.

Purpose of the Study:

  • To develop a novel platform for the functional characterization of a large number of human GPCRs.
  • To utilize this platform for antibody specificity screening, ligand interaction identification, and drug target discovery.
  • To investigate the role of GPCRs in host-pathogen interactions, specifically with Group B Streptococcus.

Main Methods:

  • Fabrication of a Virion Display (VirD) array presenting 315 non-olfactory human GPCRs on viral envelopes.
  • Screening of anti-GPCR monoclonal antibodies (mAbs) for specificity using the VirD-GPCR array.
  • Identification of GPCR-ligand interactions using peptide ligands on the VirD-GPCR array.
  • Screening the array against Group B Streptococcus to identify novel therapeutic targets.

Main Results:

  • The VirD-GPCR array successfully displayed functional human GPCRs.
  • 10 out of 20 anti-GPCR mAbs demonstrated ultra-specificity.
  • The array identified expected and novel interactions between GPCRs and peptide ligands.
  • A newly identified target, CysLTR1, was found to be involved in Group B Streptococcus infection, with its inhibition reducing bacterial penetration in vitro and in vivo.

Conclusions:

  • The VirD-GPCR array is a powerful tool for high-throughput functional GPCR characterization.
  • This platform facilitates the discovery of specific affinity reagents and the identification of novel drug targets.
  • The study identified CysLTR1 as a potential therapeutic target for Group B Streptococcus infections, offering new avenues for treatment.