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Publication Abstract from PubMed

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.

Structure and assembly of a paramyxovirus matrix protein.,Battisti AJ, Meng G, Winkler DC, McGinnes LW, Plevka P, Steven AC, Morrison TG, Rossmann MG Proc Natl Acad Sci U S A. 2012 Aug 13. PMID:22891297^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.