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Area of Science:

  • Biochemistry
  • Structural Biology
  • Virology

Background:

  • Cellular processes rely on biomolecular interaction thermodynamics.
  • Most proteins are oligomeric, yet binding affinities are often measured as 1:1 interactions.
  • SARS-CoV-2 entry involves interactions between trimeric spike proteins, dimeric ACE2 receptors, and dimeric antibodies.

Purpose of the Study:

  • To investigate the role of protein oligomerization in biomolecular interactions.
  • To determine if cooperativity, rather than 1:1 binding strength, correlates with infectivity and inhibition.
  • To elucidate antibody mechanisms against oligomeric viral targets.

Main Methods:

  • Thermodynamic analysis of biomolecular interactions.
  • Ensemble measurements of binding affinities.
  • Structural investigations of protein complexes.

Main Results:

  • ACE2 oligomerizes SARS-CoV-2 spike proteins more strongly for infectious variants, despite weaker 1:1 affinity.
  • Antibodies utilize induced oligomerization for inhibition and to enhance receptor-site blocking.
  • Cooperativity in oligomeric interactions correlates with infectivity and inhibition potency.

Conclusions:

  • 1:1 binding affinity is a poor predictor of biological potency for oligomeric targets.
  • Induced oligomerization is a significant mechanism for antibody-mediated inhibition.
  • Oligomerization plays a broader role in controlling biomolecular interactions and cellular processes.