Supramolecular organization of immature and mature murine leukemia virus revealed by electron cryo-microscopy: Implications for retroviral assembly mechanisms
Open accessAbstract
We have used electron cryo-microscopy and image analysis to examine the native structure of immature, protease-deficient (PR − ) and mature, wild-type (WT) Moloney murine leukemia virus (MuLV). Maturational cleavage of the Gag polyprotein by the viral protease is associated with striking morphological changes. The PR − MuLV particles exhibit a rounded central core, which has a characteristic track-like shell on its surface, whereas the WT MuLV cores display a polygonal surface with loss of the track-like feature. The pleomorphic shape and inability to refine unique orientation angles suggest that neither the PR − nor the WT MuLV adheres to strict icosahedral symmetry. Nevertheless, the PR − MuLV particles do exhibit paracrystalline order with a spacing between Gag molecules of ≈45 Å and a length of ≈200 Å. Because of the pleomorphic shape and paracrystalline packing of the Gag–RNA complexes, we raise the possibility that assembly of MuLV is driven by protein–RNA, as well as protein–protein, interactions. The maturation process involves a dramatic reorganization of the packing arrangements within the ribonucleoprotein core with disordering and loosening of the individual protein components.
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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 [50]
The mature CA lattice has a hexamer-hexamer spacing larger than that seen in the immature virus particle.
“The mature CA lattice has a hexamer-hexamer spacing larger than that seen in the immature virus particle”
From Retrovirus maturation-an extraordinary structural transformation (2016) · cites this paper as [50]
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Structure of Full-Length HIV-1 CA: A Model for the Mature Capsid Lattice
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Self-citationOn the Role of the SP1 Domain in HIV-1 Particle Assembly: a Molecular Switch?
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Self-citationRetrovirus maturation-an extraordinary structural transformation
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“The mature CA lattice has a hexamer-hexamer spacing larger than that seen in the immature virus particle [47,50,51].”
BackgroundHadravová, R., de Marco, A., Ulbrich, P., Štokrová, J., Doležal, M., Pichová, I., Ruml, T., Briggs, J. A. G., & Rumlová, M. (2012) · Journal of Virology · doi:10.1128/jvi.05564-11 · Cited by 26 · see citing works
- Authors
- Yeager, M., Wilson-Kubalek, E. M., Weiner, S. G., Brown, P. O., & Rein, A.
- Affiliations
- Scripps Research Institute (US)
- Department of Cell Biology, The Scripps Research Institute, La Jolla, CA 92037; Laboratory of Molecular Virology and Carcinogenesis, Advanced BioScience Laboratories–Basic Research Program, National Cancer Institute–Frederick Cancer Research Facility, Frederick, MD 21702-1201; and Department of Biochemistry, Howard Hughes Medical Institute, Stanford University Medical Center, Stanford, CA 94305
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1998-06-23
- Volume
- 95
- Issue
- 13
- Pages
- 7299-7304
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC22596
- OpenAlex
- W2073178398
- Cited by
- 189
- References
- 7
- Citations by year
- 2026: 4 · 2024: 1 · 2023: 2 · 2022: 8 · 2021: 1 · 2020: 3 · 2019: 4 · 2018: 4 · 2017: 5 · 2016: 6 · 2015: 3 · 2014: 7 · 2013: 4 · 2012: 9
- FWCI
- 4.08
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Howard Hughes Medical Institute
- U.S. Department of Health and Human Services
- American Heart Association
- Gustavus and Louise Pfeiffer Research Foundation
- Bristol-Myers Squibb
- National Institutes of Health (5r01ai031535-05)
- National Heart, Lung, and Blood Institute (R01HL048908, R01HL48908)
- National Cancer Institute
- National Institute of Allergy and Infectious Diseases (R01AI31535)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › T-cell and Retrovirus Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Advanced Electron Microscopy Techniques and Applications
- Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
- Keywords
- Moloney murine leukemia virus, retroviral assembly, virus maturation, Gag protein, icosahedral symmetry, RNA-protein interactions, immature virus particles, particle morphology
- MeSH terms
- Animals, Cricetinae, Image Processing, Computer-Assisted, Microscopy, Electron, Models, Molecular, Moloney murine leukemia virus, Endopeptidases, CHO Cells, Virus Assembly
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