Structure and Assembly of Poxvirus Scaffolding Protein D13
Author Information
Author(s): Hyun Jae-Kyung, Accurso Cathy, Hijnen Marcel, Schult Philipp, Pettikiriarachchi Anne, Mitra Alok K., Coulibaly Fasséli
Primary Institution: School of Biological Sciences, the University of Auckland, Auckland, New Zealand; School of Biomedical Sciences, Monash University, Clayton, Australia
Hypothesis
The study investigates the structure and assembly mechanisms of the D13 protein in poxviruses.
Conclusion
The findings reveal that poxviruses utilize an ancestral lipid-remodeling strategy common to DNA viruses for their morphogenesis.
Supporting Evidence
- The crystal structure of D13 was determined at 2.6 Å resolution.
- D13 assembles into trimers that are homologous to capsid proteins of other large DNA viruses.
- D13 forms a honeycomb lattice when tethered to artificial membranes.
Takeaway
Poxviruses use a special protein called D13 to help them build their virus particles, which is different from how most other viruses do it.
Methodology
The study used X-ray crystallography and electron microscopy to analyze the D13 protein's structure and assembly.
Digital Object Identifier (DOI)
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