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Three-dimensional localization of the smallest capsid protein in the human cytomegalovirus capsid
Xuekui Yu1, Sanket Shah, Ivo Atanasov
1Department of Pathology and Laboratory Medicine, University of Texas Medical School at Houston, 6431 Fannin St., MSB 2.280, Houston, TX 77030, USA.
Abstract:
The smallest capsid proteins (SCPs) of the human herpesviruses differ substantially in size and sequence and are thought to impart some unique aspects of infection to their respective viruses. We used electron cryomicroscopy and antibody labeling to show that the 8-kDa SCP of human cytomegalovirus is attached only to major capsid protein subunits of the hexons, not the pentons. Thus, the SCPs of different herpesviruses illustrate that a protein can evolve significantly in sequence, structure, and function, while preserving its role in the architecture of the virus by binding to a specific partner in a specific oligomeric state.
Insights
Smallest capsid proteins (SCPs) in human cytomegalovirus bind only to hexons, not pentons. This shows how viral proteins can evolve while maintaining their structural role in virus architecture.
Area of Science:
- Virology
- Structural Biology
- Molecular Biology
Background:
- Smallest capsid proteins (SCPs) of human herpesviruses vary in size and sequence.
- These SCPs are believed to confer unique infection characteristics to their respective viruses.
Purpose of the Study:
- To investigate the binding interactions of the smallest capsid protein (SCP) from human cytomegalovirus (HCMV).
- To understand the role of SCPs in the structural architecture of herpesviruses.
Main Methods:
- Electron cryomicroscopy was employed to visualize the structure of the viral capsid.
- Antibody labeling was used to identify the location and binding partners of the SCP.
Main Results:
- The 8-kDa SCP of human cytomegalovirus was found to exclusively attach to major capsid protein subunits known as hexons.
- Binding of the HCMV SCP was not observed with penton subunits.
Conclusions:
- The study demonstrates that viral SCPs can undergo significant evolutionary changes in sequence, structure, and function.
- Despite evolutionary divergence, SCPs maintain their essential role in virus architecture by binding to specific partners in defined oligomeric states.
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