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A complex water network contributes to high-affinity binding in an antibody-antigen interface.

S F Marino1, D Olal1, O Daumke1

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Summary

Structural water molecules play a key role in the high-affinity binding of the J22.9-xi antibody fragment to the CD269 (BCMA) tumor antigen, influencing anti-tumor responses.

Keywords:
BCMABinding interfaceCrystal structureFab fragmentHigh affinityWater molecules

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Area of Science:

  • Structural biology
  • Immunology
  • Biochemistry

Background:

  • Antibody fragments targeting tumor antigens show therapeutic potential.
  • CD269 (B cell maturation antigen, BCMA) is a tumor marker antigen.
  • Understanding antigen-antibody interactions is crucial for drug development.

Purpose of the Study:

  • To analyze the role of structural water molecules in the J22.9-xi antibody fragment and CD269 (BCMA) interaction.
  • To detail the binding interface at an atomic level.

Main Methods:

  • X-ray crystallography at 1.89 Å resolution.
  • Structural analysis of protein-protein interactions.
  • Identification of direct and indirect binding contacts.

Main Results:

  • The binding interface between J22.9-xi and CD269 (BCMA) involves few direct contacts, primarily hydrophobic.
  • Numerous indirect interactions mediated by solvent water molecules are integral to the interface.
  • These buried water molecules contribute significantly to the high-affinity binding.

Conclusions:

  • Structural water molecules are critical components of the J22.9-xi/CD269 (BCMA) binding interface.
  • The detailed structural insights can inform the design of novel antibody-based therapeutics.
  • This analysis provides a foundation for understanding antibody-mediated tumor inhibition mechanisms.