The role of the trans-Golgi network in varicella zoster virus biology 2004
Papers VZV receptor
Papers VZV paralysis
Papers VZV endosomes
J Virol. 1994 Oct;68(10):6372-90.
Intracellular transport of newly synthesized varicella-zoster virus: final envelopment in the trans-Golgi network.
Gershon AA, Sherman DL, Zhu Z, Gabel CA, Ambron RT, Gershon MD.
Department of Pediatrics, Columbia University College of Physicians and Surgeons, New York, New York 10032.
The maturation and envelopment of varicella-zoster virus (VZV) was studied in infected human embryonic lung fibroblasts. Transmission electron microscopy confirmed that nucleocapsids acquire an envelope from the inner nuclear membrane as they enter the perinuclear-cisterna-rough endoplasmic reticulum (RER). Tegument is not detectable in these virions; moreover, in contrast to the mature VZV envelope, the envelope of VZV in the RER is not radioautographically labeled in pulse-chase experiments with [3H]mannose, and it lacks gpI immunoreactivity and complex oligosaccharides. This primary envelope fuses with the RER membrane (detected in cells incubated at 20 degrees C), thereby releasing nucleocapsids to the cytosol. Viral glycoproteins, traced by transmission electron microscopy radioautography in pulse-chase experiments with [3H]mannose, are transported to the trans-Golgi network (TGN) by a pathway that runs from the RER through an intermediate compartment and the Golgi stack. At later chase intervals, [3H]mannose labeling becomes associated with enveloped virions in post-Golgi locations (prelysosomes and plasma membrane). Nucleocapsids appear to be enveloped by wrapping in specialized cisternae, identified as the TGN with specific markers. Tegument-like material adheres to the cytosolic face of the concave surface of TGN sacs; nucleocapsids adhere to this protein, which is thus trapped between the nucleocapsid and the TGN-derived membrane that wraps around it. Experiments with brefeldin A suggest that tegument may bind to the cytosolic tails of viral glycoproteins. Fusion and fission convert the TGN-derived wrapping sacs into an inner enveloped virion and an outer transport vesicle that carries newly enveloped virions to cytoplasmic vacuoles. These vacuoles are acidic and were identified as prelysosomes. It is postulated that secreted virions are partially degraded by their exposure to the prelysosomal internal milieu and rendered noninfectious. This process explains the cell-associated nature of VZV in vitro; however, the mechanism by which the virus escapes diversion from the secretory pathway to the lysosomal pathway in vivo remains to be determined.
Does varicella-zoster virus infection of the peripheral ganglia cause Chronic Fatigue Syndrome? 2009
Human herpesvirus-7 (HHV-7): current status. 1995
Following this report, an independent isolation of HHV-7 was reported from the mononuclear cells (PBMC) of a chronic fatigue syndrome patient.
[Detection of active varicella-zoster virus (VZV) infection in patients with neurological complications]. 2007
RESULTS Intrathecal antibodies against VZV were detected in 19.6 of the studied patients, VZV-specific IgM antibodies were present in serum of 17.3 of the patients and VZV DNA was recorded in CSF of 9.4 % of the patients.