Glycoprotein K Specified by Herpes Simplex Virus Type 1 Is Expressed on Virions as a Golgi Complex-Dependent Glycosylated Species and Functions in Virion Entry

Foster, Timothy P.; Rybachuk, Galena V.; Kousoulas, Konstantin G.

doi:10.1128/jvi.75.24.12431-12438.2001

Cited by 54 publications

(88 citation statements)

References 45 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Indeed, Loret et al confirmed the presence of 12 of these proteins in mature virions (68). Some reports have detected UL53 in mature virions (69,70), whereas others did not (71). UL3 was identified in our data at the late time points of HSV-1 infection (9 -15 hpi).…”

Section: Fig 1 Proteome Characterization During Hsv-1 Infection By mentioning

confidence: 91%

Time-resolved Global and Chromatin Proteomics during Herpes Simplex Virus Type 1 (HSV-1) Infection

Kulej

Avgousti

Sidoli

et al. 2017

Molecular & Cellular Proteomics

View full text Add to dashboard Cite

Herpes simplex virus (HSV-1) lytic infection results in global changes to the host cell proteome and the proteins associated with host chromatin. We present a system level characterization of proteome dynamics during infection by performing a multi-dimensional analysis during HSV-1 lytic infection of human foreskin fibroblast (HFF) cells. Our study includes identification and quantification of the host and viral proteomes, phosphoproteomes, chromatin bound proteomes and post-translational modifications (PTMs) on cellular histones during infection. We analyzed proteomes across six time points of virus infection (0, 3, 6, 9, 12 and 15 h post-infection) and clustered trends in abundance using fuzzy c-means. Globally, we accurately quantified more than 4000 proteins, 200 differently modified histone peptides and 9000 phosphorylation sites on cellular proteins. In addition, we identified 67 viral proteins and quantified 571 phosphorylation events (465 with high confidence site localization) on viral proteins, which is currently the most comprehensive map of HSV-1 phosphoproteome. We investigated chromatin bound proteins by proteomic analysis of the high-salt chromatin fraction and identified 510 proteins that were significantly different in abundance during infection. We found 53 histone marks significantly regulated during virus infection, including a steady increase of histone H3 acetylation (H3K9ac and H3K14ac). Our data provide a resource of unprecedented depth for human and viral proteome dynamics during infection. Collectively, our results indicate that the proteome composition of the chromatin of HFF cells is highly affected during HSV-1 infection, and that phosphorylation events are abundant on viral proteins. We propose that our epi-proteomics approach will prove to be important in the characterization of other model infectious systems that involve changes to chromatin composition. Molecular & Cellular Proteomics 16: 10.1074/mcp.M116.065987, S92-S107, 2017. Herpes simplex virus (HSV-1)1 leads to a contagious and persistent infection that affects about 95% of the human population. The HSV-1 genome is a double-stranded DNA molecule that replicates in the host cell nucleus (1). HSV-1 initially infects epithelial cells as a lytic infection, and then enters peripheral neurons where it establishes latency (2, 3). Processes such as viral transcription, viral DNA synthesis, virion assembly and DNA packaging take place in discrete virus-induced structures within the nucleus called replication compartments (1, 4). These processes are temporally regulated by the viral cascades of immediate-early (IE), early (E), and late (L) gene expression. The IE proteins are primarily responsible for counteracting intrinsic host defenses and for activating expression of early-phase genes (1). Early viral pro-

show abstract

Section: Fig 1 Proteome Characterization During Hsv-1 Infection By mentioning

confidence: 91%

Time-resolved Global and Chromatin Proteomics during Herpes Simplex Virus Type 1 (HSV-1) Infection

Kulej

Avgousti

Sidoli

et al. 2017

Molecular & Cellular Proteomics

View full text Add to dashboard Cite

show abstract

“…Virus HSV-1 (KOS) d27-1, which has a 1.6-kb BamHI-StuI deletion of the ICP27 gene, was kindly provided by D. M. Knipe, Harvard Medical School, and was propagated in complementing V27 cells (39). The UL53-gK protC epitope-tagged virus (gKprotC) was propagated in Vero cells and was as described previously (14).…”

Section: Cells and Virusesmentioning

confidence: 99%

“…1). The recombinant gK genes coding for the epitope-tagged gKs were constructed by using PCR-based splice-overlap extension methodology as described previously except that either HSV-1 KOS gK or HSV-1 KOS gKsyn20 DNA was used as a template (14). The KOS gKsyn20 DNA specifies a single amino acid substitution at amino acid 40 of gK (Ala to Val) that results in extensive virus-induced cell-to-cell fusion.…”

Section: Cells and Virusesmentioning

confidence: 99%

“…The plasmids that specified the V5 epitope tag and the gK-flanking sequences corresponding to the UL52 and UL54 (ICP27) genes were used to facilitate homologous recombination with viral DNA. Recombinant viruses gKV5DI, gKV5DII, gKV5DIII, and gKV5DIV specifying tags within domains I, II, III, and IV, respectively, were constructed by rescuing the mutant virus d27-1 (KOS) as shown previously (14,22). Recombinant viruses gKsyn20V5DI, gKsyn20V5DII, gKsyn20V5DIII, and gKsyn20V5DIV were as described above except that they contained the syn20 gK mutation.…”

Section: Cells and Virusesmentioning

confidence: 99%

“…Importantly, HSV-1 gK, like other alphaherpesviruses, was shown to be a structural component of purified virions and to function in virion entry (14). In the present study, we expanded upon these studies by constructing a panel of recombinant viruses expressing gK containing epitope tags within different domains of gK.…”

mentioning

confidence: 99%

See 2 more Smart Citations

Plasma Membrane Topology of Syncytial Domains of Herpes Simplex Virus Type 1 Glycoprotein K (gK): the UL20 Protein Enables Cell Surface Localization of gK but Not gK-Mediated Cell-to-Cell Fusion

Foster

Álvarez

Kousoulas

2003

J Virol

Self Cite

117

View full text Add to dashboard Cite

Most spontaneously occurring mutations that cause extensive herpes simplex virus type 1 (HSV-1)-induced cell fusion are single amino acid changes within glycoprotein K (gK). Despite the strong genetic association of gK with virus-induced cell fusion, its direct involvement in cellular membrane fusion has been controversial, largely due to previously unsuccessful efforts to detect gK expression on virion and cellular surfaces. Recently, we showed that gK is expressed on HSV-1 virions and functioned in virus entry (T. P. Foster, G. V. Rybachuk, and K. G. Kousoulas, J. Virol. 75:12431-12438, 2001). To determine whether gK is expressed on cellular surfaces, as well as its membrane topology, we generated the recombinant viruses gKV5DI, gKV5DII, gKV5DIII, and gKV5DIVcontaining insertions of the V5 antigenic epitope within each of four domains of gK predicted to localize either in the cytoplasmic side or in the extracytoplasmic side of cellular membranes. Immunohistochemical and confocal microscopy analyses of infected cells showed that both wild-type and syncytial forms of gK were expressed on cell surfaces. Analysis of the topology of the V5-tagged gK revealed that gK domains I and IV were located extracellularly, whereas domains II and III were localized intracellularly. Transiently expressed gK failed to localize in cellular plasma membranes. In contrast, infection of gKtransfected cells with the gK-null virus ⌬gK enabled expression of gK on cell surfaces, as well as gK-mediated membrane fusion. Transient-coexpression experiments revealed that the UL20 protein enabled cell surface expression of gK, but not gK-mediated cell-to-cell fusion, indicating that additional viral proteins are required for expression of the gK syncytial phenotype.Viral glycoproteins are key determinants of membrane fusion events throughout the life cycle of herpesviruses. Herpes simplex viruses (HSVs) specify at least 11 glycoproteins:

show abstract

Herpes simplex virus type 1 shows multiple interactions with sulfonated compounds at binding, penetration, and cell-to-cell passage

2007

View full text Add to dashboard Cite

Herpes simplex virus type 1 (HSV-1) uses multicomponent mechanisms for binding, penetration, and cell-to-cell passage. These processes are affected by polysulfonated compounds. In this paper we have addressed the question of whether the same or different interactions of HSV-1 with polysulfonated compounds are involved in binding, penetration, and passage. For this, we have compared the inhibitory dose-response for a series of polysulfonated and cationic compounds known to block HSV-1 infections. These comparisons were done at the level of binding, penetration, and cell-to-cell passage. Variations in the parameters of the dose-response curves - IC(50) and Hill coefficients (n (H)) - are consistent with HSV-1 having multiple interactions with sulfonated cellular components in all these processes. Some of the interactions seem to be common to the three processes, while others are particular for each one.

show abstract

Glycoprotein K Specified by Herpes Simplex Virus Type 1 Is Expressed on Virions as a Golgi Complex-Dependent Glycosylated Species and Functions in Virion Entry

Abstract: Herpes simplex virus type 1 (HSV-1) specifies at least 12

Cited by 54 publications

References 45 publications

Time-resolved Global and Chromatin Proteomics during Herpes Simplex Virus Type 1 (HSV-1) Infection

Time-resolved Global and Chromatin Proteomics during Herpes Simplex Virus Type 1 (HSV-1) Infection

Plasma Membrane Topology of Syncytial Domains of Herpes Simplex Virus Type 1 Glycoprotein K (gK): the UL20 Protein Enables Cell Surface Localization of gK but Not gK-Mediated Cell-to-Cell Fusion

Herpes simplex virus type 1 shows multiple interactions with sulfonated compounds at binding, penetration, and cell-to-cell passage

Contact Info

Product

Resources

About