Human immunodeficiency virus induces phosphorylation of its cell surface receptor

AIDS is an immunoregulatory disorder characterized by depletion of the CD4+, helper/inducer lymphocyte population. The causative agent of this disease is the human immunodeficiency virus, HIV, which infects CD4+ cells and leads to cytopathic effects characterized by syncytia formation and cell death. Recent studies have demonstrated that binding of HIV to its cellular receptor CD4 is necessary for viral entry. We find that binding of HIV to CD4 induces rapid and sustained phosphorylation of CD4 which could involve protein kinase C. HIV-induced CD4 phosphorylation can be blocked by antibody against CD4 and monoclonal antibody against the HIV envelope glycoprotein gp120, indicating that a specific interaction between CD4 and gp120 is required for phosphorylation. Electron microscopy shows that a protein kinase C inhibitor does not impair binding of HIV to CD4+ cells, but causes an apparent accumulation of virus particles at the cell surface, at the same time inhibiting viral infectivity. These results indicate a possible role for HIV-induced CD4 phosphorylation in viral entry and identify a potential target for antiviral therapy.     

On the radioactivity of certain stable isotope-enriched substances

Résumé Des mesures de radioactivité de nombreux échantillons d'eau lourde et de substances deutérées de provenances les plus diverses ont montré que les substances de teneur élevée en deutérium (>99%) présentent une radioactivité spécifique de l'ordre de 5 µCi par gramme de deutérium, due au tritium d'origine naturelle concentré en meme temps que le deutérium. Le phénomène ne se limite pas aux isotopes de l'hydrogène. Il est de caractère général et comporte d'importances conséquences théoriques et pratiques.

---

---

Financial support by the Swiss National Foundation for Scientific Research is acknowledged.