Thermodynamic and Kinetic Analysis of sCD4 Binding to HIV-1 Virions and of gp120 Dissociation

AIDS Res Hum Retroviruses. 1992 Apr;8(4):443-50. doi: 10.1089/aid.1992.8.443.


Kinetic and thermodynamic aspects of the binding of sCD4 to intact virions of human immunodeficiency virus type 1 (HIV-1 RF), and of the subsequent induction of gp120 dissociation were studied. sCD4 binding to virions at 4 and 37 degrees C is half-maximal at approximately 40 and 10 nM, respectively. The transition between low-affinity and high-affinity binding of sCD4 to virions occurs over a narrow temperature range between 20 and 25 degrees C. Shedding of gp120 from virions after sCD4 binding is also temperature dependent, being initiated above approximately 20 degrees C. The minimum temperatures for the sCD4 affinity transition and gp120 shedding are, therefore, similar and we suggest how the two processes might be related mechanistically.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • CD4 Antigens / metabolism*
  • Cell Line
  • HIV Envelope Protein gp120 / metabolism*
  • HIV Envelope Protein gp41 / metabolism
  • HIV-1 / metabolism*
  • Humans
  • Kinetics
  • Solubility
  • Thermodynamics
  • Virion / metabolism


  • CD4 Antigens
  • HIV Envelope Protein gp120
  • HIV Envelope Protein gp41