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Open-source Single-particle Analysis for Super-resolution Microscopy with VirusMapper
Published on: April 9, 2017
Structure of simian virus 40 at 3.8-A resolution
R C Liddington1, Y Yan, J Moulai
1Howard Hughes Medical Institute, Harvard University, Cambridge, Massachusetts 02138.
Nature
|November 28, 1991
Summary
The simian virus 40 structure reveals that viral protein VP1 pentamers form the outer shell. C-terminal arms link these pentamers, enabling flexible yet specific viral assembly.
Area of Science:
- Structural biology
- Virology
- Biochemistry
Background:
- Simian virus 40 (SV40) is a small DNA tumor virus with an icosahedral capsid.
- The capsid is primarily composed of 72 pentamers of the viral protein VP1.
Purpose of the Study:
- To elucidate the detailed atomic structure of simian virus 40.
- To understand the molecular mechanisms underlying viral capsid assembly and stability.
Main Methods:
- X-ray crystallography was employed to determine the high-resolution structure of SV40.
- Computational analysis was used to examine the interactions between VP1 subunits and pentamers.
Main Results:
- The structure shows 72 identical VP1 pentamers forming the viral capsid.
- A key finding is the role of C-terminal arms of VP1 subunits in inter-pentamer interactions.
- These arms extend from one pentamer and insert into adjacent pentamers, creating a 'tying together' effect.
Conclusions:
- The C-terminal arms provide a mechanism for specific yet flexible capsid assembly.
- This structural feature allows for precise packing geometry while maintaining the integrity of the viral shell.
- The findings offer insights into the assembly principles of icosahedral viruses.
