Structural basis of the gp120 superantigen-binding site on human immunoglobulins.

@article{Karray1998StructuralBO,
  title={Structural basis of the gp120 superantigen-binding site on human immunoglobulins.},
  author={Saoussen Karray and Laure Juompan and Rachid C. Maroun and David Isenberg David Isenberg and Gregg J Silverman and Moncef Zouali},
  journal={Journal of immunology},
  year={1998},
  volume={161 12},
  pages={6681-8}
}
B cell superantigens (SAg) interact with normal human nonimmune Igs (Igs), independently of the light chain isotype, and activate a large proportion of the B cell repertoire. Recently, the major envelope protein of HIV-1, gp120, was found to exhibit SAg-like properties for B cells with potential pathologic consequences for the infected host. This unconventional mode of interaction contrasts with its binding to immunization-induced Abs, which requires the tertiary structure of the heavy and… CONTINUE READING

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