The nuclear phase of herpesvirus replication is regulated through the formation of regulatory multi-component protein complexes. Viral genomic replication is followed by nuclear capsid assembly, DNA encapsidation and nuclear egress.
Jens Milbradt +11 more
doaj +3 more sources
Highly Basic Clusters in the Herpes Simplex Virus 1 Nuclear Egress Complex Drive Membrane Budding by Inducing Lipid Ordering [PDF]
During replication of herpesviruses, capsids escape from the nucleus into the cytoplasm by budding at the inner nuclear membrane. This unusual process is mediated by the viral nuclear egress complex (NEC) that deforms the membrane around the capsid by ...
Michael K. Thorsen +6 more
doaj +2 more sources
The universal suppressor mutation restores membrane budding defects in the HSV-1 nuclear egress complex by stabilizing the oligomeric lattice. [PDF]
Nuclear egress is an essential process in herpesvirus replication whereby nascent capsids translocate from the nucleus to the cytoplasm. This initial step of nuclear egress-budding at the inner nuclear membrane-is coordinated by the nuclear egress ...
Elizabeth B Draganova +8 more
doaj +2 more sources
During viral replication, herpesviruses utilize a unique strategy, termed nuclear egress, to translocate capsids from the nucleus into the cytoplasm. This initial budding step transfers a newly formed capsid from within the nucleus, too large to fit through nuclear pores, through the inner nuclear membrane to the perinuclear space.
Draganova EB, Thorsen MK, Heldwein EE.
europepmc +5 more sources
The HSV1 Tail-Anchored Membrane Protein pUL34 Contains a Basic Motif That Supports Active Transport to the Inner Nuclear Membrane Prior to Formation of the Nuclear Egress Complex [PDF]
Herpes simplex virus type 1 nucleocapsids are released from the host nucleus by a budding process through the nuclear envelope called nuclear egress. Two viral proteins, the integral membrane proteins pUL34 and pUL31, form the nuclear egress complex at ...
Christina Funk +4 more
doaj +2 more sources
Exploring the Human Cytomegalovirus Core Nuclear Egress Complex as a Novel Antiviral Target: A New Type of Small Molecule Inhibitors [PDF]
Nuclear egress is an essential process in the replication of human cytomegalovirus (HCMV), as it enables the migration of newly formed viral capsids from the nucleus into the cytoplasm.
Sewar Alkhashrom +7 more
doaj +2 more sources
pUL21 regulation of pUs3 kinase activity influences the nature of nuclear envelope deformation by the HSV-2 nuclear egress complex. [PDF]
It is well established that the herpesvirus nuclear egress complex (NEC) has an intrinsic ability to deform membranes. During viral infection, the membrane-deformation activity of the NEC must be precisely regulated to ensure efficient nuclear egress of ...
Jamil H Muradov +4 more
doaj +2 more sources
Autographa californica multiple nucleopolyhedrovirus e18 is essential for the formation of normal intranuclear membrane microvesicles and intranuclear envelopment and nuclear egress of nucleocapsids [PDF]
Autographa californica multiple nucleopolyhedrovirus (AcMNPV) E18 (AC143, ODV-E18) is an envelope protein common to both occlusion-derived virions (ODVs) and budded virions (BVs).
Lingqian Wang +4 more
doaj +2 more sources
HSV-1 exploits host heterochromatin for nuclear egress. [PDF]
Herpes simplex virus (HSV-1) progeny form in the nucleus and exit to successfully infect other cells. Newly formed capsids navigate complex chromatin architecture to reach the inner nuclear membrane (INM) and egress. Here, we demonstrate by transmission electron microscopy (TEM) that HSV-1 capsids traverse heterochromatin associated with trimethylation
Lewis HC +8 more
europepmc +4 more sources
Membrane deformation and scission by the HSV-1 nuclear egress complex [PDF]
The nuclear egress complex (NEC) of herpesviruses such as HSV-1 is essential for the exit of nascent capsids from the cell nucleus. The NEC drives nuclear envelope vesiculation in cells, but the precise budding mechanism and the potential involvement of cellular proteins are unclear.
Bigalke, Janna M. +3 more
openaire +4 more sources

