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Human immunodeficiency virus gp120 binding C'C" ridge of CD4 domain 1 is also involved in interaction with class II

U Moebius1, L K Clayton, S Abraham

  • 1Laboratory of Immunobiology, Dana-Farber Cancer Institute, Boston, MA.

Proceedings of the National Academy of Sciences of the United States of America
|December 15, 1992
PubMed

Insights

The CD4 protein

Area of Science:

  • Immunology
  • Structural Biology
  • Virology

Background:

  • The C'C'' ridge region of human CD4 is known to bind human immunodeficiency virus (HIV) gp120.
  • This region's role in class II major histocompatibility complex (MHC) binding is not fully understood.

Purpose of the Study:

  • To investigate the role of CD4's C'C'' ridge residues in class II MHC binding.
  • To understand the structural basis of CD4 interactions with both HIV and class II MHC.

Main Methods:

  • Site-directed mutagenesis of CD4.
  • Analysis of CD4 structural data.
  • Assessment of class II MHC binding affinity.

Main Results:

  • Specific charged and hydrophobic residues (Lys-35, Lys-46, Arg-59, Phe-43) in the C'C'' ridge significantly contribute to class II MHC binding.
  • Mutations in buried residues (Trp-62, Ser-49) disrupt class II MHC interaction.
  • The HIV binding site on CD4 is a smaller subset of the larger class II MHC binding site.

Conclusions:

  • The C'C'' ridge of CD4 is crucial for both HIV gp120 and class II MHC binding.
  • Drug design targeting CD4-HIV interactions must account for the overlapping binding surfaces with class II MHC.

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