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Identification of a CD4 domain required for interleukin-16 binding and lymphocyte activation

Y Liu1, W W Cruikshank, T O'Loughlin

  • 1Pulmonary Center, Boston University School of Medicine, Boston, Massachusetts 02118, USA.

The Journal of Biological Chemistry
|August 7, 1999
PubMed

Insights

Interleukin-16 (IL-16) binds to the D4 domain of CD4, activating immune cells. This interaction, mediated by specific peptides, explains IL-16

Area of Science:

  • Immunology
  • Molecular Biology
  • Cell Biology

Background:

  • Interleukin-16 (IL-16) is known to activate CD4(+) cells, suggesting a direct interaction with the CD4 molecule.
  • The high conservation of IL-16 structure and function across species implies a conserved binding site on CD4.

Purpose of the Study:

  • To identify the specific region on CD4 responsible for IL-16 binding.
  • To elucidate the mechanism by which IL-16 interacts with CD4 and affects immune responses.

Main Methods:

  • Comparative analysis of human and various species' CD4 amino acid sequences to identify conserved regions.
  • Synthesis and testing of murine CD4 domain 4 (D4) oligopeptides for their ability to inhibit IL-16 chemoattractant activity and binding to CD4 in vitro.

Main Results:

  • Immunoglobulin-like domain 4 (D4) of CD4 was identified as the most conserved extracellular region.
  • Three D4 peptides (A, B, and C) inhibited IL-16 chemoattractant activity, with peptide B being most potent.
  • Peptides A and B blocked IL-16 binding to CD4 in vitro, indicating the D4 domain contains the IL-16 binding site.
  • The IL-16 binding site within D4 overlaps with residues involved in CD4 dimerization, explaining IL-16's inhibition of mixed lymphocyte reactions.

Conclusions:

  • CD4 possesses an IL-16 binding site within its D4 domain.
  • This binding interaction provides a mechanistic basis for IL-16's known inhibitory effect on mixed lymphocyte reactions.

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