Myosin Va enhances secretion of herpes simplex virus 1 virions and cell surface expression of viral glycoproteins.

ABSTRACT: The final step in the egress of herpes simplex virus (HSV) virions requires virion-laden vesicles to bypass cortical actin and fuse with the plasma membrane, releasing virions into the extracellular space. Little is known about the host or viral proteins involved. In the current study, we noted that the conformation of myosin Va (myoVa), a protein known to be involved in melanosome and secretory granule trafficking to the plasma membrane in melanocytes and neuroendocrine cells, respectively, was altered by 4 h after infection with HSV-1 such that an N-terminal epitope expected to be masked in its inactive state was rendered immunoreactive. Wild-type myoVa localized throughout the cytoplasm and to a limited extent in the nuclei of HSV-infected cells. Two different dominant negative myoVa mo

SUBMITTER: Roberts KL 

PROVIDER: S-EPMC2937760 | biostudies-literature | 2010 Oct

REPOSITORIES: biostudies-literature