Nuclear entry and egress of parvoviruses
AbstractParvoviruses are small non‐enveloped single‐stranded DNA viruses, which depend on host cell nuclear transcriptional and replication machinery. After endosomal exposure of nuclear localization sequence and a phospholipase A2 domain on the capsid surface, and escape into the cytosol, parvovirus capsids enter the nucleus.
Mattola, Salla +5 more
core +7 more sources
Functional Identification and Characterization of the Nuclear Egress Complex of a Gammaherpesvirus. [PDF]
Increasing amounts of knowledge indicate that the nuclear egress complex (NEC) is critical for the nuclear egress of herpesvirus capsids, which can be viewed as a vesicle-mediated transport pathway through the nuclear membrane. In this study, we identified open reading frame 67 (ORF67) and ORF69 as components of the NEC in murine gammaherpesvirus 68 ...
Hongyu Deng, Dacheng Wang
exaly +5 more sources
Autographa californica multiple nucleopolyhedrovirus Ac51 interacts with Ac66 and facilitates its nuclear localization to promote the nuclear egress of nucleocapsids [PDF]
Autographa californica multiple nucleopolyhedrovirus is a large DNA virus that replicates within host nuclei. The mechanism underlying the nuclear egress of viral nucleocapsids is not fully understood.
Jianxiang Qiu +10 more
doaj +2 more sources
The nuclear egress complex of Epstein-Barr virus buds membranes through an oligomerization-driven mechanism. [PDF]
During replication, herpesviral capsids are translocated from the nucleus into the cytoplasm by an unusual mechanism, termed nuclear egress, that involves capsid budding at the inner nuclear membrane.
Michael K Thorsen +2 more
doaj +2 more sources
GRWD1 enhances HSV-1 replication by facilitating nuclear egress [PDF]
Herpes simplex virus 1 (HSV-1) depends on host factors for its replication. Here, we identify glutamate-rich WD40 repeat-containing 1 (GRWD1) as a novel pro-viral host factor that facilitates HSV-1 nuclear egress. GRWD1 knockdown trapped nucleocapsids in
Zimeng Kong +7 more
doaj +2 more sources
NECing goes: flexibility of the herpesvirus nuclear egress complex [PDF]
Abstract The nuclear egress complex (NEC) allows herpesvirus capsids to escape from the nucleus without breaking the nuclear envelope barrier. It assembles into a lattice on the inner nuclear membrane enveloping newly assembled nucleocapsids, which bud into the perinuclear space.
Pražák V +12 more
europepmc +3 more sources
Phenotypical Characterization of the Nuclear Egress of Recombinant Cytomegaloviruses Reveals Defective Replication upon ORF-UL50 Deletion but Not pUL50 Phosphosite Mutation [PDF]
Nuclear egress is a common herpesviral process regulating nucleocytoplasmic capsid release. For human cytomegalovirus (HCMV), the nuclear egress complex (NEC) is determined by the pUL50-pUL53 core that regulates multicomponent assembly with NEC ...
Sigrun Häge +11 more
doaj +2 more sources
The Complex Regulatory Role of Cytomegalovirus Nuclear Egress Protein pUL50 in the Production of Infectious Virus [PDF]
The regulation of the nucleocytoplasmic release of herpesviral capsids is defined by the process of nuclear egress. Due to their large size, nuclear capsids are unable to traverse via nuclear pores, so that herpesviruses evolved to develop a vesicular ...
Sigrun Häge +10 more
doaj +2 more sources
Herpesviruses show consistency in their nuclear egress-associated induction of lamina-depleted areas as measured in an autofluorescent reporter cell model [PDF]
Human herpesvirus infections span a wide variety of pathogenic outcomes, with individual representatives comprising a huge clinical relevance on human health.
Kishore Dhotre +3 more
doaj +2 more sources
Nuclear egress of TDP-43 and FUS occurs independently of Exportin-1/CRM1 [PDF]
TDP-43 and FUS are nuclear proteins with multiple functions in mRNA processing. They play key roles in ALS (amyotrophic lateral sclerosis) and FTD (frontotemporal dementia), where they are partially lost from the nucleus and aggregate in the cytoplasm of
Helena Ederle +7 more
doaj +3 more sources

