The molecular basis of HIV capsid assembly--five years of progress.
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.
Adamson
Catherine S
CS
School of Animal and Microbial Sciences, The University of Reading, Reading RG6 6AJ, UK. c.s.adamson@rdg.ac.uk
Jones
Ian M
IM
D002213:Capsid / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism / Q000821:virology; D015683:Gene Products, gag / Q000096:biosynthesis / Q000737:chemistry / Q000378:metabolism*; D006678:HIV / Q000235:genetics* / Q000502:physiology*; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000378:metabolism; D012367:RNA, Viral / Q000378:metabolism; D019065:Virus Assembly / Q000502:physiology*
D015683:Gene Products, gag; D011506:Proteins; D012367:RNA, Viral