Regulation of Expression of the Glycoprotein Genes of Herpes Simplex Virus Type 1 (HSV-1)

Levine, Fred; Krikos, Alexandra; Homa, Fred L.

doi:10.1007/978-1-4684-5853-4_16

Cited by 5 publications

(2 citation statements)

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“…We also repeated many of the studies herein with the commonly used but non-sequenced VZV-Ellen strain; the results were very similar (data not shown). In HSV-1 infection, the true late gC gene product is the last major glycoprotein to be expressed; its mRNA is relatively abundant by 5 hpi and the protein is expressed at high levels within a single HSV replication cycle of about 14 hours (Levine et al, 1990; Swain, Peet, and Galloway, 1985; Zhang et al, 1987). …”

Section: Discussionmentioning

confidence: 99%

Discordant varicella-zoster virus glycoprotein C expression and localization between cultured cells and human skin vesicles

Storlie¹,

Carpenter²,

Jackson³

et al. 2008

Virology

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Because of its very low titer, varicella-zoster virus (VZV) infectivity is usually transferred by passage of trypsin dispersed infected cells. Previously, we observed that gC biosynthesis was markedly delayed in monolayers inoculated with cell free virus. In this report, we investigated the kinetics of gC expression in more detail and included studies of monolayers inoculated with trypsin dispersed infected cells, the more traditional method of VZV infection. Extensive imaging analyses disclosed that gC was detectable in some inoculum cells, but little gC biosynthesis occurred during the first 48 hpi in the newly infected underlying monolayer. In contrast, during the first 24–48 hpi, expression of VZV gE and gB was easily detectable. Using real-time RT-PCR, we found a delay in accumulation of VZV gC transcripts that paralleled the delay in expression of VZV gC protein. Treatment with hexamethylene bisacetamide (HMBA) increased expression of both gC protein and gC mRNA. HMBA treatment also increased virus titer by 4-fold, but paradoxically reduced plaque size in the titration assay. Finally, we examined skin vesicles from cases of chickenpox and zoster in humans and observed abundant amounts of gC expression. In short, this report documents an unexpected delay in both gC mRNA and protein production under all conditions of VZV infection of cultured cells.

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Section: Discussionmentioning

confidence: 99%

Discordant varicella-zoster virus glycoprotein C expression and localization between cultured cells and human skin vesicles

Storlie¹,

Carpenter²,

Jackson³

et al. 2008

Virology

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“…In HeLa cells infected with HSV-1 (5 PFU/cell), the transcript for the γ 2 gC was present from 2 to 8 hpi and the relative increase in gC transcript was detected by 8-h RNA hybridization[48]. Levine M[49] reported that gC protein was expressed at high levels within a single HSV replication cycle of about 10 to 14 h. From our data, the level of DPV gC mRNA had been increasing since 4 hpi, with maximal amounts between 28 and 36 hpi and the maximum gC expression was achieved by 48 hpi. These results demonstrated that the expression of this gene occurred at the late stage of infection, which was to some extent consistent with the results from the previous observations.…”

Section: Discussionmentioning

confidence: 99%

Identification and characterization of duck plague virus glycoprotein C gene and gene product

Cheng

Wang

et al. 2010

Virol J

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BackgroundViral envelope proteins have been proposed to play significant roles in the process of viral infection.ResultsIn this study, an envelope protein gene, gC (NCBI GenBank accession no. EU076811), was expressed and characterized from duck plague virus (DPV), a member of the family herpesviridae. The gene encodes a protein of 432 amino acids with a predicted molecular mass of 45 kDa. Sequence comparisons, multiple alignments and phylogenetic analysis showed that DPV gC has several features common to other identified herpesvirus gC, and was genetically close to the gallid herpervirus.Antibodies raised in rabbits against the pET32a-gC recombinant protein expressed in Escherichia coli BL21 (DE3) recognized a 45-KDa DPV-specific protein from infected duck embryo fibroblast (DEF) cells. Transcriptional and expression analysis, using real-time fluorescent quantitative PCR (FQ-PCR) and Western blot detection, revealed that the transcripts encoding DPV gC and the protein itself appeared late during infection of DEF cells. Immunofluorescence localization further demonstrated that the gC protein exhibited substantial cytoplasm fluorescence in DPV-infected DEF cells.ConclusionsIn this work, the DPV gC protein was successfully expressed in a prokaryotic expression system, and we presented the basic properties of the DPV gC product for the first time. These properties of the gC protein provided a prerequisite for further functional analysis of this gene.

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Overview of Varicella-Zoster Virus Glycoproteins gC, gH and gL

Grose

Carpenter

Jackson

et al. 2010

Current Topics in Microbiology and Immunology

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The VZV genome is smaller than the HSV genome and only encodes nine glycoproteins. This chapter provides an overview of three VZV glycoproteins: gH (ORF37), gL (ORF60), and gC (ORF14). All three glycoproteins are highly conserved among the alpha herpesviruses. However, VZV gC exhibits unexpected differences from its HSV counterpart gC. In particular, both VZV gC transcription and protein expression are markedly delayed in cultured cells. These delays occur regardless of the virus strain or the cell type, and may account in part for the aberrant assembly of VZV particles. In contrast to VZV gC, the general properties of gH and gL more closely resemble their HSV homologs. VZV gL behaves as a chaperone protein to facilitate the maturation of the gH protein. The mature gH protein in turn is a potent fusogen. Its fusogenic activity can be abrogated when infected cultures are treated with monoclonal anti-gH antibodies.

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Regulation of Expression of the Glycoprotein Genes of Herpes Simplex Virus Type 1 (HSV-1)

Cited by 5 publications

References 46 publications

Discordant varicella-zoster virus glycoprotein C expression and localization between cultured cells and human skin vesicles

Discordant varicella-zoster virus glycoprotein C expression and localization between cultured cells and human skin vesicles

Identification and characterization of duck plague virus glycoprotein C gene and gene product

Overview of Varicella-Zoster Virus Glycoproteins gC, gH and gL

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