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Extracellular addition of a domain of HIV-1 Vpr containing the amino acid sequence motif H(S/F)RIG causes cell membrane permeabilization and death
Article first published online: 6 OCT 2006
DOI: 10.1111/j.1365-2958.1996.tb02464.x
1365-2958/asset/cover.gif?v=1&s=75254d9e3ae6a0f08085f34cc6e5bd65d8e3d52e "Molecular Microbiology")
Additional Information
How to Cite
Macreadie, I. G., Arunagiri, C. K., Hewish, D. R., White, J. F. and Azad, A. A. (1996), Extracellular addition of a domain of HIV-1 Vpr containing the amino acid sequence motif H(S/F)RIG causes cell membrane permeabilization and death. Molecular Microbiology, 19: 1185–1192. doi: 10.1111/j.1365-2958.1996.tb02464.x
Publication History
- Issue published online: 6 OCT 2006
- Article first published online: 6 OCT 2006
- Received 14 August, 1995; revised 24 October, 1995; accepted 27 October, 1995
- Abstract
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Summary
Vpr is a virion-associated protein of human immuno-deficiency virus type 1 (HIV-1) whose function in acquired immune deficiency syndrome (AIDS) has been uncertain. We previously employed yeast as a model to examine the effects of Vpr on basic cellular functions; intracellular Vpr was shown to cause cell-growth arrest and structural defects, and these effects were caused by a region of Vpr containing the sequence HFRIGCRHSRIG. Here we show that peptides containing the H(S/F)RIG amino acid sequence motif cause death when added externally to a variety of yeast including Saccharomyces cerevisiae, Kluyveromyces lactis, Candida glabrata, Candida albicans and Schizosaccharomyces pombe. Such peptides rapldly entered the cell from the time of addition, resulting in cell death. Elevated levels of ions, particularly magnesium and calcium ions, abrogated the cytotoxic effect by preventing the Vpr peptides from entering the cells. Extracellular Vpr found in the serum, or breakdown products of extracellular Vpr, may have similar effects to the Vpr peptides described here and could explain the death of uninfected by-stander cells during AIDS.