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The molecular basis of HIV capsid assembly - five years of progress

Adamson, C. S. and Jones, I. M. (2004) The molecular basis of HIV capsid assembly - five years of progress. Reviews in Medical Virology, 14 (2). pp. 107-121. ISSN 1052-9276

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To link to this article DOI: 10.1002/rmv.418

Abstract/Summary

The assembly of HIV is relatively poorly investigated when compared with the process of virus entry. Yet a detailed understanding of the mechanism of assembly is fundamental to our knowledge of the complete life cycle of this virus and also has the potential to inform the development of new antiviral strategies. The repeated multiple interaction of the basic structural unit, Gag, might first appear to be little more than concentration dependent self-assembly but the precise mechanisms emerging for HIV are far from simple. Gag interacts not only with itself but also with host cell lipids and proteins in an ordered and stepwise manner. It binds both the genomic RNA and the virus envelope protein and must do this at an appropriate time and place within the infected cell. The assembled virus particle must successfully release from the cell surface and, whilst being robust enough for transmission between hosts, must nonetheless be primed for rapid disassembly when infection occurs. Our current understanding of these processes and the domains of Gag involved at each stage is the subject of this review. Copyright (C) 2004 John Wiley Sons, Ltd.

Item Type:Article
Refereed:Yes
Divisions:Faculty of Life Sciences > School of Biological Sciences
ID Code:10409
Uncontrolled Keywords:HUMAN-IMMUNODEFICIENCY-VIRUS, TYPE-1 GAG PROTEIN, ROUS-SARCOMA-VIRUS, VESICULAR STOMATITIS-VIRUS, CELL-FREE SYSTEM, LATE DOMAIN FUNCTION, PROLINE-RICH MOTIF, TSG101 UEV DOMAIN, MATRIX PROTEIN, MEMBRANE-BINDING

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