Intracellular transport of the measles virus ribonucleoprotein complex is mediated by Rab11A-positive recycling endosomes and drives virus release from the apical membrane of polarized epithelial cells.

ABSTRACT: Many viruses use the host trafficking system at a variety of their replication steps. Measles virus (MV) possesses a nonsegmented negative-strand RNA genome that encodes three components of the ribonucleoprotein (RNP) complex (N, P, and L), two surface glycoproteins, a matrix protein, and two nonstructural proteins. A subset of immune cells and polarized epithelial cells are in vivo targets of MV, and MV is selectively released from the apical membrane of polarized epithelial cells. However, the molecular mechanisms for the apical release of MV remain largely unknown. In the present study, the localization and trafficking mechanisms of the RNP complex of MV were analyzed in detail using recombinant MVs expressing fluorescent protein-tagged L proteins. Live cell imaging analyses demonstrate

SUBMITTER: Nakatsu Y 

PROVIDER: S-EPMC3624359 | biostudies-literature | 2013 Apr

REPOSITORIES: biostudies-literature