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PRASAD, Vidya Mangala, Steven D. WILLOWS, Andrei FOKINE, Anthony J. BATTISTI, Siyang SUN, Pavel PLEVKA, Tom C. HOBMAN and Michael G. ROSSMANN. Rubella virus capsid protein structure and its role in virus assembly and infection. Proceedings of the National Academy of Sciences of the United States of America. WASHINGTON: National Academy of Sciences, 2013, vol. 110, No 50, p. 20105-20110. ISSN 0027-8424. Available from: https://dx.doi.org/10.1073/pnas.1316681110.

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Basic information
Original name	Rubella virus capsid protein structure and its role in virus assembly and infection
Authors	PRASAD, Vidya Mangala, Steven D. WILLOWS, Andrei FOKINE, Anthony J. BATTISTI, Siyang SUN, Pavel PLEVKA, Tom C. HOBMAN and Michael G. ROSSMANN.
Edition	Proceedings of the National Academy of Sciences of the United States of America, WASHINGTON, National Academy of Sciences, 2013, 0027-8424.

Other information
Original language	English
Type of outcome	Article in a journal
Field of Study	10600 1.6 Biological sciences
Country of publisher	United States of America
Confidentiality degree	is not subject to a state or trade secret
Impact factor	Impact factor: 9.809
Organization unit	Central European Institute of Technology
Doi	http://dx.doi.org/10.1073/pnas.1316681110
UT WoS	000328061700043
Keywords in English	X-ray crystallography; cryoelectron tomography; virology
Tags	neMU
Changed by	Changed by: Mgr. Eva Špillingová, učo 110713. Changed: 29/3/2017 11:05.

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.

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.