Journal
VIRUSES-BASEL
Volume 10, Issue 11, Pages -Publisher
MDPI
DOI: 10.3390/v10110640
Keywords
HIV; IP6; capsid; infection; uncoating; AIDS
Categories
Funding
- Medical Research Council [MC_U105181010, U105181010] Funding Source: Medline
- NCI NIH HHS [R01 CA020081] Funding Source: Medline
- NCRR NIH HHS [P41 RR001777] Funding Source: Medline
- NIAID NIH HHS [R01 AI150454] Funding Source: Medline
- NIGMS NIH HHS [R01 GM107013] Funding Source: Medline
- Wellcome Trust Funding Source: Medline
- MRC [MC_U105181010] Funding Source: UKRI
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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.
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