Informace o publikaci

Structure and assembly of a paramyxovirus matrix protein

Autoři	BATTISTI Anthony J. MENG Geng WINKLER Dennis C. MCGINNES Lori W. PLEVKA Pavel STEVEN Alasdair C. MORRISON Trudy G. ROSSMANN Michael G.
Rok publikování	2012
Druh	Článek v odborném periodiku
Časopis / Zdroj	Proceedings of the National Academy of Sciences of the United States of America
Fakulta / Pracoviště MU	Středoevropský technologický institut
Citace
Doi	http://dx.doi.org/10.1073/pnas.1210275109
Obor	Biochemie
Klíčová slova	NEWCASTLE-DISEASE VIRUS; RESPIRATORY SYNCYTIAL VIRUS; CRYSTAL-STRUCTURE; SENDAI-VIRUS; PARTICLES; REVEALS; NUCLEOCAPSIDS; GLYCOPROTEINS; ECTODOMAIN; EVOLUTION
Popis	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.