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Quantifying Human Norovirus Virus-like Particles Binding to Commensal Bacteria Using Flow Cytometry
Published on: April 29, 2020
Noroviral P particle: structure, function and applications in virus-host interaction.
Ming Tan1, Pingan Fang, Teepanis Chachiyo
1Division of Infectious Diseases, Cincinnati Children's Hospital Medical Center, 3333 Burnet Avenue, Cincinnati, OH 45229-3039, USA.
Virology
|October 18, 2008
Summary
Noroviruses cause epidemic gastroenteritis by binding to human histo-blood group antigens (HBGAs). Subviral P particles retain this binding function and show potential for norovirus vaccine development.
Area of Science:
- Virology
- Structural Biology
- Immunology
Background:
- Noroviruses are a major cause of epidemic acute gastroenteritis.
- These viruses utilize human histo-blood group antigens (HBGAs) as cellular receptors.
- The protruding (P) domain of the norovirus capsid contains the receptor-binding site and can form subviral particles (P particles) in vitro.
Purpose of the Study:
- To characterize the structure and HBGA-binding function of norovirus P particles.
- To evaluate the potential of P particles for vaccine development.
Main Methods:
- Cryo-electron microscopy (cryo-EM) for structural reconstruction.
- Biochemical assays to assess HBGA-binding.
- Immunogenicity studies.
- Production of P particles in E. coli and yeast.
Main Results:
- P particles are composed of 12 P dimers arranged in octahedral symmetry.
- The dimeric packing resembles that of the norovirus capsid, with the receptor-binding interface exposed.
- P particles are immunogenic and share antigenic and HBGA-binding profiles with virus-like particles.
- P particles are stable and readily produced in microbial systems.
Conclusions:
- Norovirus P particles possess a defined structure mimicking the viral capsid's surface.
- P particles effectively bind to HBGAs and are immunogenic.
- Their stability and ease of production suggest significant potential for norovirus vaccine development.
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