Electron cryotomography of measles virus reveals how matrix protein coats the ribonucleocapsid within intact virions.

ABSTRACT: Measles virus is a highly infectious, enveloped, pleomorphic virus. We combined electron cryotomography with subvolume averaging and immunosorbent electron microscopy to characterize the 3D ultrastructure of the virion. We show that the matrix protein forms helices coating the helical ribonucleocapsid rather than coating the inner leaflet of the membrane, as previously thought. The ribonucleocapsid is folded into tight bundles through matrix-matrix interactions. The implications for virus assembly are that the matrix already tightly interacts with the ribonucleocapsid in the cytoplasm, providing a structural basis for the previously observed regulation of RNA transcription by the matrix protein. Next, the matrix-covered ribonucleocapsids are transported to the plasma membrane, where the ma

SUBMITTER: Liljeroos L 

PROVIDER: S-EPMC3207687 | biostudies-literature | 2011 Nov

REPOSITORIES: biostudies-literature