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Rubella virus capsid protein structure and its role in virus assembly and infection
Autoři | |
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Rok publikování | 2013 |
Druh | Článek v odborném periodiku |
Časopis / Zdroj | Proceedings of the National Academy of Sciences of the United States of America |
Fakulta / Pracoviště MU | |
Citace | |
Doi | http://dx.doi.org/10.1073/pnas.1316681110 |
Obor | Biochemie |
Klíčová slova | X-ray crystallography; cryoelectron tomography; virology |
Popis | 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. |