Researchers are exploring whether these ubiquitous fluorinated molecules might worsen infections or hamper vaccine effectiveness.
Image credit: Shutterstock/Dmitry Naumov.
Edited by Stephen C. Harrison, Children’s Hospital, Harvard Medical School, and Howard Hughes Medical Institute, Boston, MA, and approved November 4, 2013 (received for review September 3, 2013)
Significance
Rubella virus (RV) is a human pathogen that causes serious birth defects when contracted during pregnancy. However, due to its variable shape and size, little is known about the RV structure. The RV capsid protein is an essential component of the virus and a key factor for successful replication of the virus in host cells. Here we describe the atomic structure of the RV capsid protein. This structure, along with electron microscopic data on the virus, has provided a three-dimensional picture of the virion. The capsid protein structure has also helped to identify amino acid residues that are required for virus assembly. This information can be used for the development of antiviral therapies that target the viral capsid protein.
Abstract
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.
Footnotes
↵1Present address: Central European Institute of Technology, Masaryk University, Kamenice 5, 625 00 Brno, Czech Republic.
- ↵2To whom correspondence should be addressed. E-mail: mr{at}purdue.edu.
Author contributions: V.M.P., S.D.W., T.C.H., and M.G.R. designed research; V.M.P. and S.D.W. performed research; V.M.P., A.F., A.J.B., S.S., and P.P. analyzed data; and V.M.P., A.F., T.C.H., and M.G.R. wrote the paper.
The authors declare no conflict of interest.
This article is a PNAS Direct Submission.
Data deposition: The atomic coordinates and structure factors reported here have been deposited in the Protein Data Bank, www.pdb.org (PDB codes 4HAR, 4HBE, and 4HBO).
This article contains supporting information online at www.pnas.org/lookup/suppl/doi:10.1073/pnas.1316681110/-/DCSupplemental.
Rubella virus capsid structure and organization
Sign up for Article Alerts
Jump to section
You May Also be Interested in
Recent experiments and simulations are starting to answer some fundamental questions about how life came to be.
Image credit: Shutterstock/Radoslaw Lecyk.
Archaeologists have long tried to define the transition between the two time periods.
Image credit: Ceri Shipton.
Jonathon Yuly, David Beratan, and Peng Zhang investigate how electron bifurcation reactions work.
A study finds that giant pandas roll in horse manure to increase their cold tolerance.
Image credit: Fuwen Wei.