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Related Experiment Videos

Interfacial metal and antibody recognition.

Tongqing Zhou1, Dean H Hamer, Wayne A Hendrickson

  • 1Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.

Proceedings of the National Academy of Sciences of the United States of America
|October 1, 2005
PubMed
Summary

Antibodies can use metals for antigen recognition. The Q425 antibody binds CD4 with 55,000-fold higher affinity when complexed with calcium, revealing a novel mechanism for antibody-antigen interaction.

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Area of Science:

  • Immunology
  • Structural Biology
  • Biochemistry

Background:

  • Metalloproteins are abundant, utilizing metal ions for function.
  • Antibody-antigen recognition typically involves protein-protein interactions.
  • A novel antibody, Q425, recognizes CD4 and inhibits HIV entry.

Purpose of the Study:

  • To investigate the mechanism of CD4 recognition by the Q425 antibody.
  • To determine if metal ions play a role in Q425 antibody binding to CD4.
  • To characterize the structural basis of metal-dependent antibody-antigen interaction.

Main Methods:

  • Surface-plasmon resonance (SPR) to measure binding affinity.
  • X-ray crystallography to determine the structure of the antibody-antigen complex.

Related Experiment Videos

  • Computational analysis of binding energy.

    • Main Results:

    • Q425 antibody requires calcium (Ca2+) for high-affinity CD4 binding.
    • Calcium binding enhances Q425 affinity for CD4 by 55,000-fold.
    • X-ray crystallography revealed an exposed metal-binding site in Q425, coordinating calcium and interacting with CD4.

    Conclusions:

    • Antibody Q425 utilizes an interfacial calcium ion for CD4 recognition.
    • This metal-mediated interaction provides a significant binding energy contribution.
    • This study demonstrates a novel mechanism of antigen recognition involving metal ion ligation by antibodies.