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Cited by 45Advanced Electron Microscopy Techniques and ApplicationsT-cell and Retrovirus StudiesHIV Research and Treatment

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The Organization of Mature Rous Sarcoma Virus as Studied by Cryoelectron Microscopy

Kingston, Richard L, Olson, Norman H, Vogt, Volker M·2001·Journal of Structural Biology
DOI 10.1006/jsbi.2001.4423
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Abstract

We have studied the organization of mature infectious Rous sarcoma virus (RSV), suspended in vitreous ice, using transmission electron microscopy. The enveloped virions are spherical in shape, have a mean diameter of 127 nm, and vary significantly in size. Image processing reveals the presence of the viral matrix protein underlying the lipid bilayer and the viral envelope proteins external to the lipid bilayer. In the interior of the virus, the characteristic mature retroviral core is clearly imaged. In contrast to lentiviruses, such as human immunodeficiency virus, the core of RSV is essentially isometric. The capsid, or external shell of the core, has a faceted, almost polygonal appearance in electron micrographs, but many capsids also exhibit continuous surface curvature. Cores are not uniform in size or shape. Serrations observed along the projected faces of the core suggest a repetitive molecular structure. Some isolated cores were observed in the sample, confirming that cores are at least transiently stable in the absence of the viral envelope. Using an approach grounded in geometric probability, we estimate the size of the viral core from the projection data. We show that the size of the core is not tightly controlled and that core size and virion size are positively correlated. From estimates of RNA packing density we conclude that either the RNA within the core is loosely packed or, more probably, that it does not fill the core.

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  • Different retroviruses adopt distinct core geometries, and the cores within a single virus preparation can also vary in morphology.

    “Different retroviruses adopt distinct core geometries, and the cores within a single virus preparation can also vary in morphology”

    From Retrovirus maturation-an extraordinary structural transformation (2016) · cites this paper as [59]

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Metadata

Authors
Kingston, R. L., Olson, N. H., & Vogt, V. M.
Affiliations
  • Howard Hughes Medical Institute (US)
  • Purdue University West Lafayette (US)
  • Cornell University (US)
Corresponding author
Kingston, Richard L
ORCID
Kingston, Richard L
Venue
Journal of Structural Biology
Publisher
Elsevier BV
Published
2001-10
Volume
136
Issue
1
Pages
67-80
ISSN
1047-8477 (ISSN-L)
DOI
10.1006/jsbi.2001.4423
OpenAlex
W2088302274
Cited by
45
References
3
Citations by year
2020: 1 · 2017: 3 · 2016: 4 · 2015: 1 · 2012: 1
FWCI
3.82
Type
journal article
Language
en
Open access
closed
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations
  • Journal of Structural Biology (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • National Institutes of Health (5r01ai034216-08)
  • National Institute of General Medical Sciences (GM-33050)
  • National Institute of Allergy and Infectious Diseases (AI34216)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Advanced Electron Microscopy Techniques and Applications
  • Life Sciences › Immunology and Microbiology › Immunology › T-cell and Retrovirus Studies
  • Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
Keywords
Rous sarcoma virus, viral capsid, viral matrix protein, viral envelope proteins, virion morphology, geometric probability
MeSH terms
Animals, Avian Sarcoma Viruses, Fibroblasts, Image Processing, Computer-Assisted, Microscopy, Electron, RNA, Turkeys, Viral Envelope Proteins, Models, Statistical, Cryoelectron Microscopy

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