Herpes simplex virus glycoprotein D is sufficient to induce spontaneous pH-independent fusion in a cell line that constitutively expresses the glycoprotein

Campadelli-Fiume, Gabriella; Avitabile, Elisa; Fini, Sergio; Stirpe, Daniela; Arsenakis, Minas; Roizman, Bernard

doi:10.1016/0042-6822(88)90533-8

Cited by 51 publications

(29 citation statements)

References 32 publications

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“…We hypothesize that gI interferes with a cellular protein responsible for fusion or other cytopathic effects to the cell. Interference with a cellular protein necessary for fusion has been hypothesized for another HSV-1 fusion protein, gD (Campadelli-Fiume et al, 1988). Cell lines expressing glII were fully susceptible to BHV-1 infection as shown by normal plaque size, number and morphology.…”

Section: Short Communicationmentioning

confidence: 94%

The Effect of Bovine Herpesvirus Type 1 Glycoproteins gI and gIII on Herpesvirus Infections

Chase

Carter-Allen²,

Letchworth³

1989

Journal of General Virology

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SUMMARYWe expressed the bovine herpesvirus type 1 (BHV-1) glycoproteins, gI and gIII, in bovine cells using a bovine papillomavirus vector. The proteins expressed by these cells had the same Mr as the native BHV-1 proteins and monoclonal antibodies detected no differences in their antigenic structure. Cells expressing gI were infected with either BHV-1 or herpes simplex virus type 1 (HSV-1). The number of plaques in gI-expressing cells was similar to that seen with normal fibroblasts infected with BHV-1 or HSV-1. However, BHV-1 or HSV-1 plaques produced in gI-expressing cells were smaller and darker than those seen in normal fibroblasts indicating an interference with cell-to-cell transmission or cellular lysis. Virus growth curves and [3SS]methionine labelling of BHV-l-infected gI-expressing cells showed no difference in virus production, virus protein synthesis or cellular protein shutdown when compared to BHV-l-infected normal cells. This led us to conclude that the gI protein may interfere with a cellular protein(s) responsible for the cytopathic effects of BHV-1 infection. Cells expressing gIII were fully susceptible to BHV-1 infection.

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Section: Short Communicationmentioning

confidence: 94%

The Effect of Bovine Herpesvirus Type 1 Glycoproteins gI and gIII on Herpesvirus Infections

Chase

Carter-Allen²,

Letchworth³

1989

Journal of General Virology

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“…during entry. Nonetheless, with few exceptions (1,4), the bulk of the evidence indicates that HSV-induced fusion of cultured cells does not require an acid pH (7,41,44,52,56). In this regard, HSV is similar to viruses such as HIV.…”

Section: Discussionmentioning

confidence: 99%

Roles for Endocytosis and Low pH in Herpes Simplex Virus Entry into HeLa and Chinese Hamster Ovary Cells

Nicola

McEvoy

Straus

2003

J Virol

317

448

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Herpes simplex virus (HSV) infection of many cultured cells, e.g., Vero cells, can be initiated by receptor binding and pH-neutral fusion with the cell surface. Here we report that a major pathway for HSV entry into the HeLa and CHO-K1 cell lines is dependent on endocytosis and exposure to a low pH. Enveloped virions were readily detected in HeLa or receptor-expressing CHO cell vesicles by electron microscopy at <30 min postinfection. As expected, images of virus fusion with the Vero cell surface were prevalent. Treatment with energy depletion or hypertonic medium, which inhibits endocytosis, prevented uptake of HSV from the HeLa and CHO cell surface relative to uptake from the Vero cell surface. Incubation of HeLa and CHO cells with the weak base ammonium chloride or the ionophore monensin, which elevate the low pH of organelles, blocked HSV entry in a dose-dependent manner. Noncytotoxic concentrations of these agents acted at an early step during infection by HSV type 1 and 2 strains. Entry mediated by the HSV receptor HveA, nectin-1, or nectin-2 was also blocked. As analyzed by fluorescence microscopy, lysosomotropic agents such as the vacuolar H ؉ -ATPase inhibitor bafilomycin A1 blocked the delivery of virus capsids to the nuclei of the HeLa and CHO cell lines but had no effect on capsid transport in Vero cells. The results suggest that HSV can utilize two distinct entry pathways, depending on the type of cell encountered.

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“…Virus mutants lacking glycoprotein gB, gD, gH, or gL are unable to penetrate target cells, a defect which can be at least partially overcome by treatment with an artificial fusogen, polyethylene glycol, indicating that these proteins are involved in the fusion process (reviewed in references 27 and 37). However, no classical viral fusion protein has been identified for any member of the herpesviruses, although there are reports that constitutive expression of gB or gD in transgenic cells does increase polykaryocyte formation (4,5). Glycoprotein gB, a highly conserved protein present in all subfamilies of the herpesviruses, is one of the most abundant proteins in the viral membrane and exhibits many features described for fusion proteins: it is a homodimeric type I N-glycosylated membrane protein, which in most herpesviruses is cleaved by a cellular protease into two disulfide-linked subunits (33).…”

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confidence: 99%

Pseudorabies Virus Glycoprotein M Inhibits Membrane Fusion

Klupp

Nixdorf

Mettenleiter

2000

J Virol

136

166

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A transient transfection-fusion assay was established to investigate membrane fusion mediated by pseudorabies virus (PrV) glycoproteins. Plasmids expressing PrV glycoproteins under control of the immediate-early 1 promoter-enhancer of human cytomegalovirus were transfected into rabbit kidney cells, and the extent of cell fusion was quantitated 27 to 42 h after transfection. Cotransfection of plasmids encoding PrV glycoproteins B (gB), gD, gH, and gL resulted in formation of polykaryocytes, as has been shown for homologous proteins of herpes simplex virus type 1 (HSV-1) (A. Turner, B. Bruun, T. Minson, and H. Browne, J. Virol. 72:873-875, 1998). However, in contrast to HSV-1, fusion was also observed when the gD-encoding plasmid was omitted, which indicates that PrV gB, gH, and gL are sufficient to mediate fusion. Fusogenic activity was enhanced when a carboxy-terminally truncated version of gB (gB-008) lacking the C-terminal 29 amino acids was used instead of wild-type gB. With gB-008, only gH was required in addition for fusion. A very rapid and extended fusion was observed after cotransfection of plasmids encoding gB-008 and gDH, a hybrid protein consisting of the N-terminal 271 amino acids of gD fused to the 590 C-terminal amino acids of gH. This protein has been shown to substitute for gH, gD, and gL function in the respective viral mutants (B. G. Klupp and T. C. Mettenleiter, J. Virol. 73:3014-3022, 1999). Cotransfection of plasmids encoding PrV gC, gE, gI, gK, and UL20 with gB-008 and gDH had no effect on fusion. However, inclusion of a gM-expressing plasmid strongly reduced the extent of fusion. An inhibitory effect was also observed after inclusion of plasmids encoding gM homologs of equine herpesvirus 1 or infectious laryngotracheitis virus but only in conjunction with expression of the gM complex partner, the gN homolog. Inhibition by PrV gM was not limited to PrV glycoprotein-mediated fusion but also affected fusion induced by the F protein of bovine respiratory syncytial virus, indicating a general mechanism of fusion inhibition by gM.

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Herpes simplex virus glycoprotein D is sufficient to induce spontaneous pH-independent fusion in a cell line that constitutively expresses the glycoprotein

Cited by 51 publications

References 32 publications

The Effect of Bovine Herpesvirus Type 1 Glycoproteins gI and gIII on Herpesvirus Infections

The Effect of Bovine Herpesvirus Type 1 Glycoproteins gI and gIII on Herpesvirus Infections

Roles for Endocytosis and Low pH in Herpes Simplex Virus Entry into HeLa and Chinese Hamster Ovary Cells

Pseudorabies Virus Glycoprotein M Inhibits Membrane Fusion

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