Summary
Two and a half hours after infection with a high dose of different strains of HSV-1 which induce rounding of cells, breakdown of actin containing microfilaments can be observed. At the periphery of the cell, actin containing knob-like protuberances were visible. Later on, actin seems to be located exclusively on the surface of cells. Observations were done by immunofluorescence microscopy, scanning electron-microscopy and immunoperoxidase staining of ultrathin sections. The envelope of HSV appears to be stained by anti-actin. Strain IES produces rounding of cells at a high dose of infection before fusion proceeds at 37°C. Similar alterations were not observed with the fusing strains MP and HFEM. Incubation of infected cells at 39°C revealed strain dependent differences of the fusion activity. At 41°C no “fusion from within” of cells but only rounding was detectable. Application of tunicamycin resulted in complete inhibition of fusion by all strains. The fusion activity of some strains of HSV-1 (ANG, HFEM, and MP) was not inhibited by addition of 2-deoxy-D-glucose and 2-fluoro-deoxy-D-glucose. A variant from strain MP could be isolated, which is sensitive to the effects of 2-deoxy-D-glucose. Inhibitors of processing of glycoproteins did not affect fusion of cells.
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Bedows E, Rao KMK, Welsh MJ (1983) Fate of microfilaments in Vero cells infected with measles, virus and Herpes simplex virus type 1. Mol Cell Biol 3: 712–719
Boschek CB, Jokisch BM, Friis RR, Back R, Grundmann E, Bauer H (1981) Early changes in the distribution and organization of microfilament proteins during cell transformation. Cell 24: 175–184
Bzik DJ, Person S (1981) Dependence of herpes simplex virus type-1 cell fusion on cell type. Virology 110: 35–42
Campadelli-Fiume G, Poletti L, Dall'Olio F, Serafini-Cessi F (1982) Infectivity and glycoprotein processing of Herpes simplex virus type 1 grown in a ricin-resistant cell line deficient in N-acetylgucosaminly transferase I. J Virol 43: 1061–1071
Dienes HP, Knoblich A, Falke D (1985) The loss of fibronectin in HSV-infected cells. Arch Virol 85: 223–237
Elbein AD (1981) The tunicamycins-useful tools for studies on glycoproteins. TIBS 6: 219–221
Falke D (1970) Wechselseitige Dissoziierbarkeit von DNS-Synthese und Riesenzell-bildung bei Herpesvirus hominis durch Cytosin-Arabinosid und durch Cpd 48/80. Zbl Parasitenkunde I Orig 212: 390–395
Falke D, Knoblich A, Müller S (1985) Fusion from without induced by HSV. Intervirology 24: 211–219
Franklin RM, Emmons LR, Emmons RP, Kai O, Gommen A, Piuk JR, Rigubeek AM, Schnetzler M, Tudermann L, Vainio E (1984) A monoclonal antibody recognizes an epitope common to an avian-specific nuclear antigen and to cytokeratins. J Cell Biochem 24: 1–14
Fujinami RS, Oldstone MBA, Wroblewska Z, Frankel ME, Koprowski H (1983) Molecular mimicry in virus infection: Crossreaction of measles virus phosphoprotein or of herpes simplex virus protein with human intermediate filaments. Proc Natl Acad Sci USA 80: 2346–2350
Gallaher WR, Levitan DB, Blough HA (1973) Effect of 2-deoxy-D-glucose on cell fusion induced by Newcastle disease and herpes simplex virus. Virology 55: 193–201
Görtz J, Brake B, Härile-Grupp V, Falke D (1984) Replication of HSV-1 in murine peritoneal macrophages: Comparison of various virus strains with different properties. Arch Virol 79: 173–198
Halliburton I (1980) Intertypic recombinants of Herpes simplex viruses. J Gen Virol 48: 1–23
Heeg U, Haase W, Brauer D, Falke D (1981) Microtubules and microfilaments in HSV-infected rabbit-kidney cells. Arch Virol 70: 233–246
Heeg U, Hiller G, Härle-Grupp V, Falke D (1983) Alterations of the cytoskeleton after infection with HSV. Tagung der DGHM, 17.–19. 3. 1983, Würzburg. Zbl Bakt I Orig A 255: 171
Heifetz A, Keenan RW, Elbein AD (1979) Mechanism of action of Tunicamycin on the UDP-GlcNAc: dolicholpyrophosphate GlcNAc-1-phosphate transferase. Biochemistry 18: 2186–2192
Kaerner GH, Schröder CH, Ott-Hastmann A, Kümel G, Kirchner H (1983) Genetic variability of herpes simplex virus: Development of a pathogenic variant during passaging of a nonpathogenic herpes simplex virus type 1 strain in mouse brain. J Virol 46: 83–93
Kohlhage H, Siegert R (1962) Zwei genetisch determinierte Varianten eines HSV-Stammes. Arch Ges Virusforsch 12: 273–286
Kousoulas KG, Person S, Holland TC (1978) Timing of some of the molecular events required for cell fusion induced by herpes simplex virus type 1. J Virol 27: 505–512
Krempien U, Jockusch BM, Jungwirth C (1984) Herpes simplex virus induced cell surface protrusions. Intervirology 22: 156–163
Ludwig H, Becht H, Rott R (1974) Inhibition of herpes virus-induced cell fusion by concanavalin A, antisersa and 2-deoxy-D-glucose. J Virol 14: 307–314
McGinnes LW, Semerjan A, Morrison T (1985) Conformational changes in New-castle Disease Virus Fusion glycoprotein during intracellular transport. J Virol 56: 341–348
Norrild B, Pedersen B (1982) Effect of tunicamycin on the synthesis of herpes simplex virus type 1 glycoproteins and their expression on the cell surface. J Virol 43: 395–401
Pogue-Geile KL, Lee GYT, Shapira SK, Spear PG (1984) Fine mapping of mutations in the fusion-inducing MP strain of Herpes simplex virus type 1. Virology 136: 100–109
Richter IE, Falke D (1974) Scanning electron microscopic observations on the inhibition of Herpes-induced giant cell formation by Cpd 48/80 and Cytochalasin B. Eur J Pathol 4: 59–73
Roizman B (1962) Polykaryocytosis. Cold Spring Harbor Symp Quant Biol 27: 327–342
Romero PA, Datema R, Schwarz RT (1983) N-methyl-1-deoxynojirimycin, a novel inhibitor of glycoprotein processing and its effect on fowl plague virus maturation. Virology 130: 238–242
Schmidt MF, Schwarz RT, Ludwig H (1976) Fluorosugars inhibit biological properties of different enveloped viruses. J Virol 18: 819–823
Schwarz RT, Datema R (1984) Inhibitors of trimming: new tools in glycoprotien research. TIBS 9: 32–34
Spear PG, Roizman B (1982) Herpes simplex viruses. In:Tooze J (ed) DNA tumor viruses, 2nd edn, part 2. Cold Spring Harbor Laboratory, pp 615–746
Weber K, Rathke PC, Osborn M, Franke WW (1976) Distribution of actin and tubulin in cells and in glycerinated cell models after treatment with cytochalasin B (CB). Exptl Cell Res 102: 285–297
Wenske EA, Courtney RJ (1983) Glycosylation of herpes simplex virus type 1 gC in the presence of tunicamycin. J Virol 46: 297–301
Winkler M, Dawson GJ, Elizan TS, Berl S (1982) Distribution of actin and myosin in a rat neuronal cell line infected with Herpes simplex virus. Arch Virol 72: 95–103
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With 8 Figures
In part presented at the meeting of the DGMH, Würzburg, March 17–19, 1983.
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Heeg, U., Dienes, H.P., Müller, S. et al. Involvement of actin-containing microfilaments in HSV-induced cytopathology and the influence of inhibitors of glycosylation. Archives of Virology 91, 257–270 (1986). https://doi.org/10.1007/BF01314285
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DOI: https://doi.org/10.1007/BF01314285