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Journal of Virology, January 2007, p. 532-538, Vol. 81, No. 2
0022-538X/07/$08.00+0 doi:10.1128/JVI.01079-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.
Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, Boston, Massachusetts 02115,1 Department of Pathology, Division of AIDS, Harvard Medical School, Boston, Massachusetts 02115,2 Department of Immunology and Infectious Diseases, Harvard School of Public Health, Boston, Massachusetts 02115,3 Department of Biochemical Immunology, Merck & Co., Inc., Rahway, New Jersey 070654
Received 25 May 2006/ Accepted 17 August 2006
The coexpression of human immunodeficiency virus type 1 (HIV-1) envelope glycoproteins and receptors leads to the lysis of single cells by a process that is dependent upon membrane fusion. This cell lysis was inhibited by low-molecular-weight compounds that interfere with receptor binding or with receptor-induced conformational transitions in the envelope glycoproteins. A peptide, T20, potently inhibited cell-cell fusion but had no effect on single cell lysis mediated by the HIV-1 envelope glycoproteins. Thus, critical events in the lysis of single cells by the HIV-1 envelope glycoproteins occur in intracellular compartments accessible only to small inhibitory compounds.
Published ahead of print on 30 August 2006.
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