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Updated: Dec 11, 2025

Structure of HIV-1 Capsid Assemblies by Cryo-electron Microscopy and Iterative Helical Real-space Reconstruction
Published on: August 9, 2011
3D structure of three jumbo phage heads
Emmanuelle Neumann1, Takeru Kawasaki2, Grégory Effantin1
1Université Grenoble Alpes, CNRS, CEA, Institute for Structural Biology (IBS), F-38000, Grenoble, France.
Abstract:
Jumbo phages are bacteriophages that carry more than 200 kbp of DNA. In this study we characterized two jumbo phages (ΦRSL2 and ΦXacN1) and one semi-jumbo phage (ΦRP13) at the structural level by cryo-electron microscopy. Focusing on their capsids, three-dimensional structures of the heads at resolutions ranging from 16 to 9 Å were calculated. Based on these structures we determined the geometrical basis on which the icosahedral capsids of these phages are constructed, which includes the accessory and decorative proteins that complement them. A triangulation number novel to Myoviridae (ΦRP13; T=21) was discovered as well as two others, which are more common for jumbo phages (T=27 and T=28). Based on one of the structures we also provide evidence that accessory or decorative proteins are not a prerequisite for maintaining the structural integrity of very large capsids.
Insights
Jumbo phages, large viruses infecting bacteria, were structurally analyzed using cryo-electron microscopy. Researchers revealed the geometric principles of their icosahedral capsids and found accessory proteins may not be essential for large capsid integrity.
Area of Science:
- Structural biology
- Virology
- Microbiology
Background:
- Jumbo phages are bacteriophages with large DNA genomes (>200 kbp).
- Understanding their structure is key to comprehending their replication and evolution.
- Cryo-electron microscopy provides high-resolution insights into viral architecture.
Purpose of the Study:
- To characterize the three-dimensional structures of jumbo phage capsids.
- To elucidate the geometric principles underlying their icosahedral capsid construction.
- To investigate the role of accessory proteins in capsid stability.
Main Methods:
- Cryo-electron microscopy was used to determine the structures of two jumbo phages (ΦRSL2, ΦXacN1) and one semi-jumbo phage (ΦRP13).
- Three-dimensional reconstructions of phage heads were calculated at 9–16 Å resolution.
- Analysis of the structures focused on capsid geometry and protein composition.
Main Results:
- Determined the 3D structures of ΦRSL2, ΦXacN1, and ΦRP13 capsids.
- Identified the geometrical basis of icosahedral capsid assembly, including accessory proteins.
- Discovered a novel triangulation number (T=21) for Myoviridae (ΦRP13) and common numbers (T=27, T=28) for jumbo phages.
- Provided evidence that accessory proteins are not essential for the structural integrity of very large capsids.
Conclusions:
- The study reveals the structural basis of jumbo phage capsid formation.
- Novel triangulation numbers were identified, expanding our understanding of viral evolution.
- The findings challenge the necessity of accessory proteins for maintaining the stability of large bacteriophage capsids.
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