Identification of conserved amino acids in pUL34 which are critical for function of the pseudorabies virus nuclear egress complex.

ABSTRACT:

Unlabelled

Nuclear egress of herpesvirus capsids is mediated by a conserved heterodimeric complex of two viral proteins, designated pUL34 and pUL31 in herpes simplex virus and pseudorabies virus (PrV). pUL34, a tail-anchored membrane protein, is targeted to the nuclear envelope and recruits pUL31 to the inner nuclear membrane (INM) to provide the docking and envelopment machinery for the nascent capsid. While the less conserved C-terminal part of pUL34 is required for correct positioning of the nuclear egress complex (NEC) at the INM, the conserved N-terminal part functions as a docking site for pUL31. Since no crystal structure of NEC is available yet, structure-function studies depend on mutational analyses, with several approaches already being performed for different herpesviru

SUBMITTER: Paßvogel L 

PROVIDER: S-EPMC4093891 | biostudies-literature | 2014 Jun

REPOSITORIES: biostudies-literature