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IP6 Regulation of HIV Capsid Assembly, Stability, and Uncoating

Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853-2703, USA
Protein and Nucleic Acid Chemistry Division, Medical Research Council, Laboratory of Molecular Biology, Cambridge CB2 0QH, UK
Authors to whom correspondence should be addressed.
Viruses 2018, 10(11), 640;
Received: 17 October 2018 / Revised: 12 November 2018 / Accepted: 13 November 2018 / Published: 15 November 2018
(This article belongs to the Special Issue Breakthroughs in Viral Replication)
The mechanisms that drive formation of the HIV capsid, first as an immature particle and then as a mature protein shell, remain incompletely understood. Recent discoveries of positively-charged rings in the immature and mature protein hexamer subunits that comprise them and their binding to the cellular metabolite inositol hexakisphosphate (IP6) have stimulated exciting new hypotheses. In this paper, we discuss how data from multiple structural and biochemical approaches are revealing potential roles for IP6 in the HIV-1 replication cycle from assembly to uncoating. View Full-Text
Keywords: HIV; IP6; capsid; infection; uncoating; AIDS HIV; IP6; capsid; infection; uncoating; AIDS
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MDPI and ACS Style

Dick, R.A.; Mallery, D.L.; Vogt, V.M.; James, L.C. IP6 Regulation of HIV Capsid Assembly, Stability, and Uncoating. Viruses 2018, 10, 640.

AMA Style

Dick RA, Mallery DL, Vogt VM, James LC. IP6 Regulation of HIV Capsid Assembly, Stability, and Uncoating. Viruses. 2018; 10(11):640.

Chicago/Turabian Style

Dick, Robert A.; Mallery, Donna L.; Vogt, Volker M.; James, Leo C. 2018. "IP6 Regulation of HIV Capsid Assembly, Stability, and Uncoating" Viruses 10, no. 11: 640.

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