Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 110, Issue 50, Pages 20105-20110Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1316681110
Keywords
X-ray crystallography; cryoelectron tomography; virology
Categories
Funding
- National Institutes of Health [AI-095366]
- National Science Foundation [MCB-1014547]
- Canadian Institutes of Health Research (CIHR)
- CIHR
- Alberta Innovates Health Solutions
- DOE [DE-AC02-06CH11357]
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [1014547] Funding Source: National Science Foundation
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Rubella virus (RV) is a leading cause of birth defects due to infectious agents. When contracted during pregnancy, RV infection leads to severe damage in fetuses. Despite its medical importance, compared with the related alphaviruses, very little is known about the structure of RV. The RV capsid protein is an essential structural component of virions as well as a key factor in virus-host interactions. Here we describe three crystal structures of the structural domain of the RV capsid protein. The polypeptide fold of the RV capsid protomer has not been observed previously. Combining the atomic structure of the RV capsid protein with the cryoelectron tomograms of RV particles established a low-resolution structure of the virion. Mutational studies based on this structure confirmed the role of amino acid residues in the capsid that function in the assembly of infectious virions.
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