Structural organization of authentic, mature HIV‐1 virions and cores

Structural organization of authentic, mature HIV‐1 virions and cores Mature, infectious HIV‐1 particles contain a characteristic cone‐shaped core that encases the viral RNA and replication proteins. The architectures of mature virions and isolated cores were studied using cryo‐electron microscopy. The average size (∼145 nm) of the virion was unchanged during maturation. Most virions contained a single core but roughly one‐third contained two or more cores. Consideration of the capsid protein concentration during core assembly indicated that core formation in vivo is template‐mediated rather than concentration‐driven. Although most cores were conical, 7% were tubular. These displayed a stacked‐disc arrangement with 7‐, 8‐, 9‐ or 10‐fold axial symmetry. Layer line filtration of these images showed that the capsid subunit arrangement is consistent with a 9.6 nm hexamer resembling that previously seen in the helical tubes assembled from purified capsid protein. A common reflection (1/3.2 nm) shared between the tubular and conical cores suggested they share a similar organization. The extraordinary flexibility observed in the assembly of the mature core appears to be well suited to accommodating variation and hence there may be no single structure for the infectious virion. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png The EMBO Journal Wiley

Structural organization of authentic, mature HIV‐1 virions and cores

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Publisher
Wiley
Copyright
Copyright © 2013 Wiley Periodicals, Inc
ISSN
0261-4189
eISSN
1460-2075
DOI
10.1093/emboj/cdg143
Publisher site
See Article on Publisher Site

Abstract

Mature, infectious HIV‐1 particles contain a characteristic cone‐shaped core that encases the viral RNA and replication proteins. The architectures of mature virions and isolated cores were studied using cryo‐electron microscopy. The average size (∼145 nm) of the virion was unchanged during maturation. Most virions contained a single core but roughly one‐third contained two or more cores. Consideration of the capsid protein concentration during core assembly indicated that core formation in vivo is template‐mediated rather than concentration‐driven. Although most cores were conical, 7% were tubular. These displayed a stacked‐disc arrangement with 7‐, 8‐, 9‐ or 10‐fold axial symmetry. Layer line filtration of these images showed that the capsid subunit arrangement is consistent with a 9.6 nm hexamer resembling that previously seen in the helical tubes assembled from purified capsid protein. A common reflection (1/3.2 nm) shared between the tubular and conical cores suggested they share a similar organization. The extraordinary flexibility observed in the assembly of the mature core appears to be well suited to accommodating variation and hence there may be no single structure for the infectious virion.

Journal

The EMBO JournalWiley

Published: Jan 1, 2003

Keywords: ; ; ; ;

References

  • Structural analysis of membrane bound retrovirus capsid proteins
    Barklis, E
  • Assembly of recombinant human immunodeficiency virus type 1 capsid protein in vitro
    Ehrlich, LS; Agresta, BE; Carter, CA
  • SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields
    Frank, J; Radermacher, M; Penczek, P; Zhu, J; Li, Y; Ladjadj, M; Leith, A
  • A morphological and immunolabelling study of freeze‐substituted human and simian immunodeficiency viruses
    Grief, C; Nermut, MV; Hockley, DJ
  • Image reconstructions of helical assemblies of the HIV‐1 CA protein
    Li, S; Hill, CP; Sundquist, WI; Finch, JT
  • Supplanting crystallography or supplementing microscopy? A combined approach to the study of an enveloped virus
    Mancini, EJ; Fuller, SD
  • Hexagonal organization of Moloney murine leukemia virus capsid proteins
    Mayo, K; McDermott, J; Barklis, E
  • Molecular organization of Mason–Pfizer monkey virus capsids assembled from Gag polyprotein in Escherichia coli
    Nermut, MV; Bron, P; Thomas, D; Rumlova, M; Ruml, T; Hunter, E

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