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CD4 binding site antibodies inhibit human immunodeficiency virus gp120 envelope glycoprotein interaction with CCR5

Aarti Raja1, Miro Venturi, Peter Kwong

  • 1Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, Boston, Massachusetts 02115, USA.

Journal of Virology
|December 13, 2002
PubMed

Insights

CD4-binding-site antibodies block HIV-1 entry by preventing the virus from binding to host cell coreceptors. These antibodies inhibit the conformational changes in the gp120 protein necessary for viral entry.

Area of Science:

  • Virology
  • Immunology
  • Structural Biology

Background:

  • The human immunodeficiency virus type 1 (HIV-1) exterior glycoprotein gp120 is conformationally flexible.
  • HIV-1 uses CD4 as a receptor and CCR5 or CXCR4 as coreceptors for cell entry.
  • CD4-binding-site (CD4BS) antibodies target epitopes overlapping the CD4 binding site on gp120.

Purpose of the Study:

  • To investigate whether CD4BS antibodies inhibit coreceptor binding and viral entry.
  • To determine if CD4BS antibodies recognize distinct gp120 conformations.

Main Methods:

  • Using Fab fragments and complete immunoglobulin molecules of CD4BS antibodies.
  • Assessing inhibition of CD4-independent gp120 binding to CCR5.
  • Evaluating inhibition of cell-cell fusion mediated by CD4-independent HIV-1 envelope glycoproteins.

Main Results:

  • CD4BS antibodies inhibited CD4-independent gp120 binding to CCR5.
  • CD4BS antibodies blocked cell-cell fusion mediated by CD4-independent HIV-1 envelope glycoproteins.
  • These findings suggest CD4BS antibodies interfere with gp120 conformational changes required for coreceptor engagement.

Conclusions:

  • CD4BS antibodies effectively inhibit HIV-1 entry by preventing coreceptor binding.
  • The mechanism involves limiting gp120's ability to adopt a conformation necessary for coreceptor interaction.
  • This provides insight into neutralizing antibody mechanisms against HIV-1.

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