HIV-1 gp120: a novel viral B cell superantigen

Int Rev Immunol. 1997;14(4):325-38. doi: 10.3109/08830189709116523.


The envelope glycoprotein of the human immunodeficiency virus (HIV-1), gp120, has recently been characterized as a novel immunoglobulin superantigen (Ig-SAg) [1,2]. Analogous to the interaction of SAgs with T cells, gp120 binds to an unusually large proportion of immunoglobulins (lgs) from HIV-uninfected individuals; most, if not all of these Igs are members of the VH3 family [3]. Functionally, gp120 preferentially stimulates VH3 B cells in vitro. This stimulation correlates with an in vivo VH3 activation during HIV infection. Curiously, this initial activation is followed by a subsequent depletion of VH3-expressing B cells as individuals progress to AIDS. In this article we will review our current understanding of the superantigenic properties of HIV gp120. Specifically we will focus on structural aspects of the binding interaction. on the ontological development of these superantigen-binding antibodies, and on potential roles that this unconventional Ig-pathogen interaction might play in the pathogenesis of HIV-induced disease.

Publication types

  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • B-Lymphocytes / immunology*
  • Binding Sites
  • Complement System Proteins / metabolism
  • HIV Antibodies / metabolism
  • HIV Envelope Protein gp120 / chemistry
  • HIV Envelope Protein gp120 / immunology*
  • HIV Envelope Protein gp120 / metabolism
  • HIV Infections / epidemiology
  • HIV Infections / etiology
  • HIV Infections / transmission
  • HIV-1 / immunology*
  • Humans
  • Molecular Structure
  • Superantigens* / metabolism


  • HIV Antibodies
  • HIV Envelope Protein gp120
  • Superantigens
  • Complement System Proteins