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Science 23 November 1990: Vol. 250. no. 4984, pp. 1139 - 1142 DOI: 10.1126/science.2251501
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Articles
Science, Vol 250, Issue 4984, 1139-1142
Copyright © 1990 by American Association for the Advancement of Science
Dissociation of gp120 from HIV-1 virions induced by soluble CD4
JP Moore,
JA McKeating,
RA Weiss,
and
QJ Sattentau
Chester Beatty Laboratories, Institute of Cancer Research, London, United Kingdom.
The CD4 antigen is the high affinity cellular receptor for the human immunodeficiency virus type-1 (HIV-1). Binding of recombinant soluble CD4 (sCD4) or the purified V1 domain of sCD4 to the surface glycoprotein gp120 on virions resulted in rapid dissociation of gp120 from its complex with the transmembrane glycoprotein gp41. This may represent the initial stage in virus-cell and cell-cell fusion. Shedding of gp120 from virions induced by sCD4 may also contribute to the mechanism by which these soluble receptor molecules neutralize HIV-1.
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