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Amphipathic Domains in the C Terminus of the Transmembrane Protein (gp41) Permeabilize HIV-1 Virions: A Molecular Mechanism Underlying Natural Endogenous Reverse Transcription

Hui Zhang, Geethanjali Dornadula, Prasad Alur, Mark A. Laughlin and Roger J. Pomerantz
Proceedings of the National Academy of Sciences of the United States of America
Vol. 93, No. 22 (Oct. 29, 1996), pp. 12519-12524
Stable URL: http://www.jstor.org/stable/40650
Page Count: 6
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Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Amphipathic Domains in the C Terminus of the Transmembrane Protein (gp41) Permeabilize HIV-1 Virions: A Molecular Mechanism Underlying Natural Endogenous Reverse Transcription
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Abstract

Reverse transcription of HIV-1, without detergent or amphipathic peptide-induced permeability of the viral envelope, has been demonstrated to occur in the intact HIV-1 virion. In this report, we demonstrate that the amphipathic domains in the C terminus of the transmembrane glycoprotein (gp41) account for the natural permeability of the HIV-1 envelope to deoxyribonucleoside triphosphates, the substrates for DNA polymerization. In addition, nonphysiological deoxyribonucleoside triphosphates, such as 3$^{\prime}$-azido-3$^{\prime}$-deoxythymidine 5$^{\prime}$-triphosphate and 3$^{\prime}$-deoxythymidine 5$^{\prime}$-triphosphate, can also penetrate the viral envelope, incorporate into, and irreversibly terminate reverse transcripts. As a result, viral infectivity is potently inhibited. Since the lentiviral envelope with these newly demonstrated characteristics can serve as a delivery pathway for anti-reverse transcription agents, we propose a unique strategy to prevent HIV-1 interand, possibly, intrahost transmission.

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