PubMed · 2848210
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J Frankl. 1988-06-19. [A regrettable lapse].. https://pubmed.ncbi.nlm.nih.gov/2848210/
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Plasmids containing the varicella zoster virus (VZV) open reading frames (ORFs) 61 and 62 were used in a transient co-transfection assay to test for trans-activation of the VZV and herpes simplex virus type 1 (HSV-1) thymidine kinase (tk) promoters. The trans-activating potential of the polypeptides encoded by these VZV ORFs, designated p51 and p140, was compared to that of their HSV-1 homologs ICP0 and ICP4, respectively. VZV p51 was functionally inactive in this system while p140 appeared to be a much stronger transcriptional activator than ICP4. Co-transfection of plasmids encoding VZV p140 and HSV-1 ICP0 resulted in a synergistic activation of the reporter gene as has been shown for the combination of ICP4 and ICP0.
Soluble class I antigens (sHLA) are secreted by lymphocytes upon activation in vitro. The intrathecal synthesis (ITS) of these molecules has been studied in patients with the varicella-zoster virus (VZV) meningitis. In this paper we describe a sHLA index IH = (CSF sHLA/serum sHLA): (CSF albumin/serum albumin) which is expected to increase only when sHLA is synthesised within the central nervous system (CNS). The IH is elevated in the first week of meningitis, when antibody synthesis is still low, and decreases thereafter. We think IH is an index of early lymphocyte activation within the CNS. The relation of these findings with previous in vitro studies is also discussed.
gpI, the predominant varicella-zoster virus (VZV) envelope glycoprotein, was shown to be phosphorylated exclusively on serine and threonine residues, and phosphorylated gpI was detected in isolated virions. In cells infected with herpes simplex virus type 1 (HSV-1), a related neurotropic alpha-herpesvirus, HSV gE, the homolog to VZV gpI, and HSV gB, the homolog to VZV gpII, were also phosphorylated. The phosphate on gB and gE was alkali labile and resistant to endo H, suggesting linkage to serine and/or threonine. Although VZV gpI and HSV gE share sequence homology and similar post-translational modifications, no Fc-binding activity similar to that associated with gE was detected for gpI or any of the VZV glycoproteins.