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Structure of HIV-1 Capsid Assemblies by Cryo-electron Microscopy and Iterative Helical Real-space Reconstruction

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Published on: August 9, 2011

Herpesvirus capsid assembly: insights from structural analysis.

Jay C Brown¹, William W Newcomb

¹Department of Microbiology, University of Virginia Health System, Charlottesville, 22908, USA. JCB2G@VIRGINIA.EDU

Current Opinion in Virology

|September 20, 2011

Summary

This summary is machine-generated.

Herpesvirus capsid assembly shares similarities with double-stranded DNA bacteriophages. Structural studies reveal a pathway involving scaffolding proteins and a portal complex, crucial for viral DNA packaging and transport.

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Area of Science:

Structural virology
Molecular biology
Cryo-electron microscopy

Background:

Herpesviruses possess highly uniform icosahedral capsids assembled in the host cell nucleus.
Capsid structure is critical for viral DNA packaging and subsequent cytoplasmic morphogenetic events.
Previous studies highlight the utility of cryo-electron microscopy for herpesvirus structural analysis.

Purpose of the Study:

To elucidate the structural characteristics and assembly mechanisms of herpesvirus capsids.
To emphasize the role of structural studies, particularly on herpes simplex virus.
To compare herpesvirus capsid assembly pathways with those of double-stranded DNA bacteriophages.

Main Methods:

Analysis of existing structural data on herpesvirus capsids.
Comparative analysis with established models for double-stranded DNA bacteriophage assembly.
Focus on contributions from cryo-electron microscopy and three-dimensional image reconstruction.

Main Results:

Herpesvirus capsid assembly follows a pathway analogous to double-stranded DNA bacteriophages (e.g., P22, HK97).
Assembly involves a transient scaffolding protein absent in the mature virion.
A procapsid intermediate, spherical and fragile, is formed during assembly.
A portal complex is incorporated at a unique vertex of the capsid.

Conclusions:

Herpesvirus capsid assembly is a conserved process, sharing key features with bacteriophage assembly.
The identified pathway provides insights into the fundamental mechanisms of viral capsid formation.
Structural studies are instrumental in understanding herpesvirus morphogenesis and could inform antiviral strategies.