Abstract
INFECTION by the human immunodeficiency virus (HIV) is initiated by the binding of its extracellular envelope glycoprotein, gp120, to the CD4 antigen on target cells1-3. To map the residues of the HIV-1 glycoprotein that are critical for binding and to analyse the effects of binding on viral infectivity, we created 15 mutations in a region of gp!20 that is important for binding to CD4 (refs 4,5). We find that substitution of a single amino acid (tryptophan at position 432) can abrogate CD4 binding and that virus carrying this mutation is non-infectious. By contrast, other amino-acid changes in the same region do not affect CD4 binding but restrict viral tropism: virions containing isoleucine substitutions at position 425 lose their ability to infect a monocyte cell line (U937 cells) but can still infect T-lymphocyte cell lines (CEM, SUP-T1) and activated human peripheral blood lymphocytes. These results indicate that cellular tropism of HIV can be influen-ced by a single amino-acid change in gp120.
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Cordonnier, A., Montagnier, L. & Emerman, M. Single amino-acid changes in HIV envelope affect viral tropism and receptor binding. Nature 340, 571–574 (1989). https://doi.org/10.1038/340571a0
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DOI: https://doi.org/10.1038/340571a0
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