HIV-1 Envelope gp120 and Viral Particles Block Adenosine Deaminase Binding to Human CD26

  • Agustin Valenzuela
  • Julià Blanco
  • Christian Callebaut
  • Etienne Jacotot
  • Carmen Lluis
  • Ara G. Hovanessian
  • Rafael Franco
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 421)

Abstract

CD26, known to be the adenosine deaminase (ADA) binding protein, has been implicated in HIV infection. In human B and T cell lines we show that, irrespective of CD4 expression, 125I-labeled ADA binding to CD26 is inhibited by recombinant soluble HIV-1 envelope glycoprotein gp120 and by HIV-1 infectious particles. Overlapping synthetic peptides covering the entire gp120 sequence were tested to map the region in gp120 responsible for ADA binding inhibition. Only peptides in the C3 region significantly inhibited the binding of ADA to CD26. These results indicate that a specific function of gp120 is the inhibition of ADA binding to CD26 in both CD4+ and CD4 cells. Since the interaction ecto-ADA/CD26 is required for the activation of T cells, it remains possible that HIV particle-mediated blockade of ecto-ADA/CD26 interaction may have significant consequences in the pathogenesis of AIDS disease.

Keywords

Jurkat Cell Adenosine Deaminase Severe Combine Immunodeficiency Cell Surface CD26 High CD26 Level 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1997

Authors and Affiliations

  • Agustin Valenzuela
    • 1
  • Julià Blanco
    • 2
  • Christian Callebaut
    • 2
  • Etienne Jacotot
    • 2
  • Carmen Lluis
    • 1
  • Ara G. Hovanessian
    • 2
  • Rafael Franco
    • 1
  1. 1.Departament de Bioquímica i Biologia Molecular Facultad de QuímicaUniversidad de BarcelonaBarcelonaSpain
  2. 2.Unité de Virologie et d’ImmunologieCellulaire UA CNRS 1157, Institut PasteurParis Cedex 15France

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