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Three-dimensional structure of poliovirus at 2.9 A resolution
Science (New York, N.Y.)
|September 27, 1985
Summary
The poliovirus capsid structure reveals a shared protein fold with plant viruses, despite distinct surface features. These structural insights inform understanding of viral assembly and antigenic sites.
Area of Science:
- Structural Biology
- Virology
- Biochemistry
Background:
- Poliovirus is a significant human pathogen.
- Understanding the three-dimensional structure of viruses is crucial for developing antiviral strategies.
Purpose of the Study:
- To determine the high-resolution three-dimensional structure of poliovirus.
- To compare the structural features of poliovirus capsid proteins with those of other viruses.
Main Methods:
- X-ray crystallography at 2.9 A resolution.
- Analysis of the capsid protein folding and subunit packing.
Main Results:
- Poliovirus capsid proteins share a common beta-barrel core structure with icosahedral plant viruses.
- Distinct connecting loops and terminal extensions create unique surface features and protein-protein contacts.
- Subunit packing differs from T=3 plant viruses, leading to prominent surface peaks.
Conclusions:
- Poliovirus capsid structure shares evolutionary links with plant viruses.
- Surface features, including antigenic sites, are determined by variable loop and terminal strand interactions.
- Structural findings provide insights into poliovirus assembly mechanisms.