Membrane-containing viruses with icosahedrally symmetric capsids
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Updated: Jul 16, 2026

Generation and Assembly of Virus-Specific Nucleocapsids of the Respiratory Syncytial Virus
Published on: July 27, 2021
Juha T Huiskonen1, Sarah J Butcher
1Institute of Biotechnology and Department of Biological and Environmental Sciences, PO Box 65 (Viikinkaari 1), University of Helsinki, Finland.
Abstract:
Viruses with an icosahedrally symmetric protein capsid and a membrane infect hosts from all three domains of life. Similar architectural principles are shared by different viral families, as exemplified by double-stranded DNA viruses such as PRD1 and STIV. During virus assembly, the membrane lipids are selectively acquired from the host cell. The X-ray structure of bacteriophage PRD1 revealed that the lipids are asymmetrically distributed between the two leaflets and facet length is controlled by a tape-measure protein. In most membrane-containing viruses, viral and host membranes fuse during viral entry. In the best-understood systems of the alphaviruses, flaviviruses and herpes viruses, fusion is mediated by viral glycoproteins. Recent structural advances reveal how very different protein architectures can be used to form trimeric extensions that extend into the target cell membrane and then fold back to mediate fusion of the target and viral membranes.
Insights
This study explores viral structure and assembly, revealing how membrane-containing viruses acquire host lipids and mediate membrane fusion through viral glycoproteins. Key findings include lipid asymmetry and tape-measure protein roles in bacteriophage PRD1.
Area of Science:
- Virology
- Structural Biology
- Biochemistry
Background:
- Many viruses possess icosahedral capsids and membranes, infecting all domains of life.
- Viral families like PRD1 and STIV share architectural principles in double-stranded DNA virus assembly.
- Membrane-containing viruses selectively acquire host lipids during assembly and fuse with host membranes during entry.
Purpose of the Study:
- To elucidate the structural mechanisms of viral assembly and membrane fusion.
- To understand the role of viral glycoproteins in mediating membrane fusion.
- To investigate lipid acquisition and distribution in viruses like bacteriophage PRD1.
Main Methods:
- X-ray crystallography of bacteriophage PRD1.
- Structural analysis of viral glycoproteins involved in membrane fusion.
- Comparative analysis of viral architecture across different families.
Main Results:
- Bacteriophage PRD1 exhibits asymmetric lipid distribution and tape-measure proteins controlling facet length.
- Viral glycoproteins form trimeric extensions that interact with and fuse target cell membranes.
- Diverse viral protein architectures can achieve membrane fusion.
Conclusions:
- Viral assembly involves selective lipid acquisition and precise structural organization.
- Viral glycoproteins are crucial for mediating membrane fusion, a conserved mechanism across various virus types.
- Understanding these viral mechanisms provides insights into host-pathogen interactions and potential antiviral strategies.
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