BATTISTI, Anthony J., Geng MENG, Dennis C. WINKLER, Lori W. MCGINNES, Pavel PLEVKA, Alasdair C. STEVEN, Trudy G. MORRISON and Michael G. ROSSMANN. Structure and assembly of a paramyxovirus matrix protein. Proceedings of the National Academy of Sciences of the United States of America. WASHINGTON: National Academy of Sciences, 2012, vol. 109, No 35, p. 13996-14000. ISSN 0027-8424. Available from: https://dx.doi.org/10.1073/pnas.1210275109.
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Basic information
Original name Structure and assembly of a paramyxovirus matrix protein
Authors BATTISTI, Anthony J., Geng MENG, Dennis C. WINKLER, Lori W. MCGINNES, Pavel PLEVKA, Alasdair C. STEVEN, Trudy G. MORRISON and Michael G. ROSSMANN.
Edition Proceedings of the National Academy of Sciences of the United States of America, WASHINGTON, National Academy of Sciences, 2012, 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: 9.737
Organization unit Central European Institute of Technology
Doi http://dx.doi.org/10.1073/pnas.1210275109
UT WoS 000308565300031
Keywords in English NEWCASTLE-DISEASE VIRUS; RESPIRATORY SYNCYTIAL VIRUS; CRYSTAL-STRUCTURE; SENDAI-VIRUS; PARTICLES; REVEALS; NUCLEOCAPSIDS; GLYCOPROTEINS; ECTODOMAIN; EVOLUTION
Tags neMU
Changed by Changed by: Mgr. Eva Špillingová, učo 110713. Changed: 29/3/2017 14:41.
Abstract
Many pleomorphic, lipid-enveloped viruses encode matrix proteins that direct their assembly and budding, but the mechanism of this process is unclear. We have combined X-ray crystallography and cryoelectron tomography to show that the matrix protein of Newcastle disease virus, a paramyxovirus and relative of measles virus, forms dimers that assemble into pseudotetrameric arrays that generate the membrane curvature necessary for virus budding. We show that the glycoproteins are anchored in the gaps between the matrix proteins and that the helical nucleocapsids are associated in register with the matrix arrays. About 90% of virions lack matrix arrays, suggesting that, in agreement with previous biological observations, the matrix protein needs to dissociate from the viral membrane during maturation, as is required for fusion and release of the nucleocapsid into the host's cytoplasm. Structure and sequence conservation imply that other paramyxovirus matrix proteins function similarly.
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