Abstract
The T-cell surface glycoprotein, CD4 (T4), acts as the cellular receptor for human immunodeficiency virus, type 1 (HIV-1), the first member of the family of viruses that cause acquired immunodeficiency syndrome1–4. HIV recognition of CD4 is prob-ably mediated through the virus envelope glycoprotein (gp!20) as shown by co-immunoprecipitation of CD4 and gp!20 (ref. 5) and by experiments using recombinant gp!20 as a binding probe6. Here we demonstrate that recombinant soluble CD4 (rsT4) purified from the conditioned medium of a stably transfected Chinese hamster ovary cell line is a potent inhibitor of both virus replication and virus-induced cell fusion (syncytium formation). These results suggest that rsT4 is sufficient to bind HIV, and that it represents a potential anti-viral therapy for HIV infection.
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Fisher, R., Bertonis, J., Meier, W. et al. HIV infection is blocked in vitro by recombinant soluble CD4. Nature 331, 76–78 (1988). https://doi.org/10.1038/331076a0
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DOI: https://doi.org/10.1038/331076a0
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