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The papillomavirus major capsid protein L1
Christopher B Buck1, Patricia M Day, Benes L Trus
1Lab of Cellular Oncology, Center for Cancer Research, NCI, USA.
Virology
|June 27, 2013
Summary
Papillomavirus L1 protein self-assembles into virus-like particles, forming the basis for effective human papillomavirus (HPV) vaccines. This review explores conserved features of L1 protein structure and function.
Area of Science:
- Structural biology
- Virology
- Vaccine development
Background:
- The papillomavirus virion surface is composed of the L1 protein, which can self-assemble into virus-like particles (VLPs).
- These recombinant L1 VLPs mimic native papillomavirus virions and are highly immunogenic.
- VLPs form the foundation for successful vaccines against cancer-causing human papillomaviruses (HPVs).
Purpose of the Study:
- To review conserved sequence and structural features of the papillomavirus L1 protein.
- To elucidate how these features enable critical viral life cycle functions.
Main Methods:
- Literature review focusing on structural and sequence analysis of papillomavirus L1 proteins.
- Analysis of published data on L1 protein self-assembly and VLP formation.
- Review of studies detailing viral capsid conformational changes during infection.
Main Results:
- The L1 protein's icosahedral structure is conserved across papillomaviruses.
- Conserved regions within L1 are crucial for self-assembly into VLPs.
- Structural plasticity of the capsid facilitates viral DNA encapsidation, maturation, cell attachment, and DNA release.
Conclusions:
- Conserved sequence and structural attributes of the papillomavirus L1 protein are fundamental to its functional versatility.
- Understanding these features is key to advancing VLP-based vaccine design and antiviral strategies.
- The L1 protein's ability to undergo conformational changes is central to the papillomavirus life cycle.
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