Membrane Anchors of the Structural Flavivirus Proteins and Their Role in Virus Assembly.

ABSTRACT:

Unlabelled

The structural proteins of flaviviruses carry a unique set of transmembrane domains (TMDs) at their C termini that are derived from the mode of viral polyprotein processing. They function as internal signal and stop-transfer sequences during protein translation, but possible additional roles in protein interactions required during assembly and maturation of viral particles are ill defined. To shed light on the role of TMDs in these processes, we engineered a set of tick-borne encephalitis virus mutants in which these structural elements were replaced in different combinations by the homologous sequences of a distantly related flavivirus (Japanese encephalitis virus). The effects of these modifications were analyzed with respect to protein synthesis, viral particle secret

SUBMITTER: Blazevic J 

PROVIDER: S-EPMC4936158 | biostudies-literature | 2016 Jul

REPOSITORIES: biostudies-literature