A soluble CD4 protein selectively inhibits HIV replication and syncytium formation

Rebecca E. Hussey, Neil E. Richardson, Mark Kowalski, Nicholas R. Brown, Hsiu Ching Chang, Robert F. Siliciano, Tatyana Dorfman, Bruce Walker, Joseph Sodroski, Ellis L. Reinherz

Research output: Contribution to journalArticlepeer-review

Abstract

The CD4 (T4) molecule is expressed on a subset of T lymphocytes involved in class II MHC recognition1,2, and is probably the physiological receptor for one or more monomorphic regions of class II MHC (refs 1-3). CD4 also functions as a receptor for the human immunodeficiency virus (HIV) exterior envelope glycoprotein (gp120) (refs 4-9), being essential for virus entry into the host cell and for membrane fusion, which contributes to cell-to-cell transmission of the virus and to its cytopathic effects10,11. We have used a baculovirus expression system to generate mg quantities of a hydrophilic extracellular segment of CD4. Concentrations of soluble CD4 in the nanomolar range, like certain anti-CD4 monoclonal antibodies, inhibit syncytium formation and HIV infection by binding gp120-expressing cells. Perhaps more importantly, class II specific T-cell interactions are uninhibited by soluble CD4 protein, whereas they are virtually abrogated by equivalent amounts of anti-T4 antibody. This may reflect substantial differences in CD4 affinity for gp120 and class II MHC.

Original languageEnglish (US)
Pages (from-to)78-81
Number of pages4
JournalNature
Volume331
Issue number6151
DOIs
StatePublished - 1988
Externally publishedYes

ASJC Scopus subject areas

  • General

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