Effects of Targeting Herpes Simplex Virus Type 1 gD to the Endoplasmic Reticulum and
            <i>trans</i>
            -Golgi Network

Whiteley, Alison; Bruun, Birgitte; Minson, Tony; Browne, Helena

doi:10.1128/jvi.73.11.9515-9520.1999

Cited by 88 publications

(31 citation statements)

References 44 publications

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“…5 are consistent with the behavior of mutant gH molecules in fusion and rescue assays and suggest that the assembly of gH into virions is not dependent on specific sequences in the transmembrane or cytoplasmic domains. The same conclusion has been drawn for gD (12,42).…”

Section: Characterization Of Gh Chimeric Constructs In Cell-cell Fusionsupporting

confidence: 82%

“…This construct contains EcoRV and AflII sites immediately 5Ј and 3Ј, respectively, of the predicted transmembrane coding sequence. The coding sequence of HSV-1 gD (nucleotides 138419 to 139601) was cloned into pCDNA3 from the parental plasmid pING-HincIIgD (42). HpaI and AflII sites were introduced 5Ј and 3Ј, respectively, of the predicted transmembrane coding sequence (nucleotides 139439 to 139508) by site-directed mutagenesis.…”

Section: Cells and Virusesmentioning

confidence: 99%

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The Transmembrane Domain and Cytoplasmic Tail of Herpes Simplex Virus Type 1 Glycoprotein H Play a Role in Membrane Fusion

Harman

Browne

Minson

2002

J Virol

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Herpes simplex virus glycoprotein H (gH) is one of the four virion envelope proteins which are required for virus entry and for cell-cell fusion in a transient system. In this report, the role of the transmembrane and cytoplasmic tail domains of gH in membrane fusion was investigated by generating chimeric constructs in which these regions were replaced with analogous domains from other molecules and by introducing amino acid substitutions within the membrane-spanning sequence. gH molecules which lack the authentic transmembrane domain or cytoplasmic tail were unable to mediate cell-cell fusion when coexpressed with gB, gD, and gL and were unable to rescue the infectivity of a gH-null virus as efficiently as a wild-type gH molecule. Many amino acid substitutions of specific amino acid residues within the transmembrane domain also affected cell-cell fusion, in particular, those introduced at a conserved glycine residue. Some gH mutants that were impaired in cell-cell fusion were nevertheless able to rescue the infectivity of a gH-negative virus, but these pseudotyped virions entered cells more slowly than wild-type virions. These results indicate that the fusion event mediated by the coexpression of gHL, gB, and gD in cells shares common features with the fusion of the virus envelope with the plasma membrane, they point to a likely role for the membrane-spanning and cytoplasmic tail domains of gH in both processes, and they suggest that a conserved glycine residue in the membrane-spanning sequence is crucial for efficient fusion.Herpes simplex viruses (HSVs) enter cells by fusion of the virus envelope with the host cell plasma membrane at a neutral pH (reviewed by Spear [37]), and four of the HSV envelope glycoproteins, gB, gD, gH, and gL, are not only essential for virus entry (7, 13, 24) but can also induce the fusion of cellular membranes when coexpressed from plasmid vectors in the absence of any other virus components (30,40). Efficient fusion induction with this system is dependent on the presence of a gD receptor on the plasma membrane of recipient cells (4, 34), but the means by which gB, gD, gH, and gL interact with each other or with other components of the plasma membrane to induce polykaryocyte formation and virus entry remain unclear. It is also uncertain whether the cell-cell fusion induced by the coexpression of gB, gD, gH, and gL mirrors the events which take place when the virion envelope fuses with the plasma membrane during virus entry.Homologues of HSV type 1 (HSV-1) gB and the gHL heterodimer have been identified in herpesviruses of all subfamilies and are likely to play a direct role in the fusion process. Indeed, studies with pseudorabies virus and human herpesvirus 8 have shown that the expression of gB and gHL is sufficient to induce cell fusion (17, 33) and, in varicella-zoster virus, the expression of gHL alone or gB in combination with gE has been reported to induce fusion (11,25). Despite the compelling evidence for the activity of gB and gHL as fusion proteins, these molecules have n...

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Section: Characterization Of Gh Chimeric Constructs In Cell-cell Fusionsupporting

confidence: 82%

Section: Cells and Virusesmentioning

confidence: 99%

The Transmembrane Domain and Cytoplasmic Tail of Herpes Simplex Virus Type 1 Glycoprotein H Play a Role in Membrane Fusion

Harman

Browne

Minson

2002

J Virol

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“…Moreover, SBP1 over-accumulation leads to an increase in the late (docking and fusion) intra-Golgi transport [48]. In fact, in vertebrates, herpesviruses exploit several host compartments for envelopment [49][50][51]. Herpesvirus nucleocapsids assemble in the nuclei of infected cells and acquire an envelope by budding through the inner nuclear membrane.…”

Section: Accepted Manuscriptmentioning

confidence: 99%

“…The virus undergoes de-envelopment and re-envelopment steps during virus egress and its final envelopment is observed in the late Golgi compartment [52]. Indeed, the enveloped proteins of alphaherpesvirus accumulate in the Golgi compartment or in Golgi-derived vesicles [50].…”

Section: Accepted Manuscriptmentioning

confidence: 99%

Proteomic signatures of the oyster metabolic response to herpesvirus OsHV-1 μVar infection

Corporeau

Tamayo

Pernet

et al. 2014

Journal of Proteomics

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This study is the first 2-DE proteomic analysis dedicated to the pathogenesis of ostreid herpesvirus 1 (OsHV-1 μVar) in oyster Crassostrea gigas, the most important bivalve produced in the world. OsHV-1 has affected oysters every year since 2008. All the proteins identified in this paper are key targets involved in OsHV-1 infection processes. We presented evidence that the metabolic changes during infection in oyster somehow resemble the Warburg effect occurring in cancer cells. This work constitutes a real advance in the comprehension of the host metabolic pathways affected during OsHV-1 disease. Overall, this work contributes to a better understanding of disease mortalities in aquatic ecosystems which could guide management actions to mitigate their impacts.

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“…Virus production is sensitive to the endoplasmic reticulum (ER)-to-Golgi inhibitor Brefeldin A (BFA) (17,18), and is inhibited by the depletion of Rab1, a Rab known to be involved in ER-to-Golgi transport (19)(20)(21)(22), suggesting that virus glycoproteins must access the Golgi/TGN prior to envelopment. Virus glycoproteins also localize to the plasma membrane (PM) in advance of any capsid accumulation in the cytoplasm (23)(24)(25)(26).…”

mentioning

confidence: 99%

Rab6 Dependent Post‐Golgi Trafficking of HSV1 Envelope Proteins to Sites of Virus Envelopment

Johns

Lopez

Sayers

et al. 2013

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Herpes simplex virus 1 (HSV1) is an enveloped virus that uses undefined transport carriers for trafficking of its glycoproteins to envelopment sites. Screening of an siRNA library against 60 Rab GTPases revealed Rab6 as the principal Rab involved in HSV1 infection, with its depletion preventing Golgi-to-plasma membrane transport of HSV1 glycoproteins in a pathway used by several integral membrane proteins but not the luminal secreted protein Gaussia luciferase. Knockdown of Rab6 reduced virus yield to 1% and inhibited capsid envelopment, revealing glycoprotein exocytosis as a prerequisite for morphogenesis. Rab6-dependent virus production did not require the effectors myosin-II, bicaudal-D, dynactin-1 or rabkinesin-6, but was facilitated by ERC1, a factor involved in linking microtubules to the cell cortex. Tubulation and exocytosis of Rab6-positive, glycoprotein-containing membranes from the Golgi was substantially augmented by infection, resulting in enhanced and targeted delivery to cell tips. This reveals HSV1 morphogenesis as one of the first biological processes shown to be dependent on the exocytic activity of Rab6.

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Effects of Targeting Herpes Simplex Virus Type 1 gD to the Endoplasmic Reticulum and trans -Golgi Network

Cited by 88 publications

References 44 publications

The Transmembrane Domain and Cytoplasmic Tail of Herpes Simplex Virus Type 1 Glycoprotein H Play a Role in Membrane Fusion

The Transmembrane Domain and Cytoplasmic Tail of Herpes Simplex Virus Type 1 Glycoprotein H Play a Role in Membrane Fusion

Proteomic signatures of the oyster metabolic response to herpesvirus OsHV-1 μVar infection

Rab6 Dependent Post‐Golgi Trafficking of HSV1 Envelope Proteins to Sites of Virus Envelopment

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