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Related Experiment Videos

Engineering an APRIL-specific B cell maturation antigen.

Darshana R Patel1, Heidi J A Wallweber, JianPing Yin

  • 1Department of Protein Engineering, Genentech, Inc., South San Francisco, California 94080, USA.

The Journal of Biological Chemistry
|February 7, 2004
PubMed
Summary
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B cell maturation antigen (BCMA) preferentially binds a proliferation-inducing ligand (APRIL) over B cell-activating factor (BAFF). Amino acid substitutions can alter BCMA

Area of Science:

  • Immunology
  • Molecular Biology
  • Biochemistry

Background:

  • B cell maturation antigen (BCMA) is a receptor in the tumor necrosis factor receptor superfamily.
  • Its physiological role is unclear, but it's implicated in binding a proliferation-inducing ligand (APRIL) and B cell-activating factor (BAFF).
  • APRIL and BAFF are involved in autoimmune disease and cancer.

Purpose of the Study:

  • To analyze the dual binding of BCMA to APRIL and BAFF.
  • To characterize binding affinities and identify critical residues for ligand specificity.
  • To engineer BCMA variants with modified binding properties.

Main Methods:

  • Characterization of monomeric BCMA binding affinity for APRIL and BAFF.
  • Shotgun alanine scanning to map critical residues for ligand binding.

Related Experiment Videos

  • Phage display experiments to assess single amino acid mutations.

    • Main Results:

    • BCMA exhibits significantly higher affinity for APRIL (IC50 = 11 +/- 3 nm) than for BAFF (IC50 = 8 +/- 5 microm).
    • Specific amino acid residues (Tyr13, Ile22, Gln25, Arg27) were identified as critical for ligand specificity.
    • A BCMA-Fc fusion with an I22K mutation showed specific binding to APRIL with no measurable affinity for BAFF.

    Conclusions:

    • APRIL is the preferred ligand for BCMA.
    • Amino acid substitutions can be used to engineer BCMA specificity towards APRIL or BAFF.
    • Understanding BCMA-ligand interactions is crucial for therapeutic applications in autoimmune diseases and cancer.