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Characterization of fusion from without induced by herpes simplex virus

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Summary

The process of fusion from without (FFWO) induced by herpes simplex virus (HSV) was analyzed by using various inhibitors and compared to fusion from within (FFWI). The fate of certain elements of the cytoskeleton after FFWO was also investigated. Our experiments demonstrate FFWO as a very suitable system for study of early virus-cell interactions.

Zn++ ions proved inhibitory for penetration whilst pretreatment of cells with Ca++ ions before infection enhanced FFWO activity. Dissociation of penetration from the fusion process itself was possible by use of Zn++ ions, low pH-treatment and antiserum on the one hand and N-ethylmaleimide and cytochalasin D on the other. Penetration itself needs only 6 min or less to proceed. FFWO is independent of inhibitors of glycosylation (tunicamycin) and intracellular vesicular traffic (monensin), protein-synthesis (cycloheximide) and energy-delivery (2.4 dinitrophenol and Na-azide). Analyzed strains of HSV-1 and -2 producing FFWI could be subgrouped into three categories: Strain ANG with high, strain HFEM and Lux with low and strains IES, Len, MP, US with no FFWO activity. The results of these experiments indicate that the property of FFWO is not purely a consequence of the number of PFU but depends on certain inherent properties of the virus particles. Addition of heparin as well as treatment of cells with heparitinase effectively prevented FFWO, indicating identical virus receptors for entrance of virus into cells and FFWO.

During our studies several calf sera were found to inhibit FFWO-activity. Inhibition of FFWO by a glycoconjugate (ferritin coupled with oleic acid) indicates specific stereochemical hindrance of FFWO by this compound. Shortly after FFWO the actin filaments rearrange to form long fibres and surface fibronectin is being lost from the cell membrane.

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References

  1. Bachmann M, Falke D, Müller WEG (1990) Is La protein involved in autoimmunization and inflammatory events during disease? Characterization of La protein as an unwinding enzyme. Mol Biol Rep 14: 49–50

    Google Scholar 

  2. Barrett AJ (1977) Introduction to the history and classification of tissue proteinases. In: Barrett AJ (ed) Proteinases in mammalian cells and tissues. Elsevier, Amsterdam, pp 1–55

    Google Scholar 

  3. Beckers CJM, Block MR, Glick BS, Rothman JE, Balch WE (1989) Vesicular transport between the endoplasmic reticulum and the Golgi stack requires the NEM-sensitive fusion protein. Nature 339: 397–398

    Google Scholar 

  4. Chatterjee S, Kogo J, Whitley RJ (1989) A role of herpes simplex virus type 1 glycoprotein E in induction of cell fusion. J Gen Virol 70: 2157–2161

    Google Scholar 

  5. Couch CB, Strittmacher WJ (1983) Rat myoblast fusion requires metallo-endoprotease activity. Cell 32: 257–265

    Google Scholar 

  6. Dienes HP, Knoblich A, Falke D (1985) Loss of surface fibronectin after infection of cultured cells by HSV-1 and -2. Arch Virol 86: 223–237

    Google Scholar 

  7. Diaz R, Mayorgo LS, Weidman PJ, Rothman JE, Stahl PD (1989) Vesicle fusion following receptor-mediated endocytosis requires a protein active in Golgi transport. Nature 339: 398–400

    Google Scholar 

  8. Falke D (1967) Ca++, Histidin und Zn++ bei der Riesenzellbildung durch Herpes simplex Virus. Z Med Mikrobiol Immunol 153: 175–189

    Google Scholar 

  9. Falke D, Knoblich A, Müller S (1985) Fusion from without induced by herpes simplex virus type 1. Intervirology 24: 211–219

    Google Scholar 

  10. Fridlender B, Chejanovsky N, Becker Y (1978) Selective inhibition of herpes simplex virus type 1 DNA polymerase by zinc ions. Virology 84: 551–554

    Google Scholar 

  11. Heeg U, Dienes HP, Müller S, Falke D (1986) Involvement of actin-containing microfilaments in HSV-induced cytopathology and the influence of inhibitors of glycosilation. Arch Virol 91: 257–270

    Google Scholar 

  12. Heeg U, Haase W, Brauer D, Falke D (1981) Microtubules and microfilaments in HSV-infected rabbit kidney cells. Arch Virol 70: 233–246

    Google Scholar 

  13. Holland TC, Person S (1977) Ammoniumchloride inhibits cell fusion by syn mutants of herpes simplex virus type 1. J Virology 23I: 213–215

    Google Scholar 

  14. Huang RTC (1982) Myxovirus induced membrane fusion mediated by phospholipids and neutral glycolipids. In: Makita S, Hando T, Taketomi M, Nagai R (eds) New vistas in glycolipid research. Plenum, New York, pp 393–400

    Google Scholar 

  15. Huang RTC (1983) Involvement of glycolipids in myxovirus-induced membrane fusion. J Gen Virol 64: 221–224

    Google Scholar 

  16. Huang AS, Wagner RR (1964) Penetration of herpes simplex virus into human epidermoid cells. Proc Soc Exp Biol Med 116: 863–869

    Google Scholar 

  17. Huemer HP, Menzel HJ, Potratz D, Brake B, Falke D, Utermann G, Dierich MP (1988) Herpes simplex virus binds to human serum lipoprotein. Intervirology 29: 68–76

    Google Scholar 

  18. Kaner RJ, Bird A, Mansukhani A, Basilico C, Summers BD, Florkiewicz RZ, Hajjar DP (1990) Fibroblast growth factor receptor is a portal of cellular entry for herpes simplex virus type 1. Science 248: 1410–1412

    Google Scholar 

  19. Koyama AH, Uchido T (1989) The effect of ammoniumchloride on the multiplication of herpes simplex virus type 1 in Vero cells. Virus Res 13: 271–282

    Google Scholar 

  20. Kühn JE, Kramer MD, Willenbacher W, Wieland U, Lorentzen EU, Braun RW (1990) Identification of herpes simplex virus type 1 glycoproteins interacting with the cell surface. J Virol 64: 2491–2497

    Google Scholar 

  21. Prasad AS (1979) Clinical, biochemical and pharmacological role of zinc. Am Rev Pharmacol Toxicol 20: 393–426

    Google Scholar 

  22. Ross DS, Choppin PW (1985) Biochemical studies on cell fusion. I. Lipid composition of fusion resistant cells. J Cell Biol 101: 1578–1590

    Google Scholar 

  23. Roos DS, Choppin PW (1985) Biochemical studies on cell fusion. II. Control of fusion response by lipid alteration. J Cell Biol 101: 1591–1598

    Google Scholar 

  24. Roos DS, Duchala CS, Stephensen CB, Holmes KV, Choppin PW (1990) Control of virus-induced cell fusion by host cell lipid composition. Virology 175: 345–357

    Google Scholar 

  25. Rosenthal KS, Perez R, Hodmichak C (1985) Inhibition of herpes simplex virus type 1 penetration by cytochalasin B and D. J Gen Virol 66: 1601–1605

    Google Scholar 

  26. Spear PG (1987) Virus induced cell fusion. In: Sowers AE (ed) Cell fusion. Plenum, New York, pp 3–32

    Google Scholar 

  27. Stannard LM, Fuller AO, Spear PG (1987) Herpes simplex virus glycoproteins associated with different morphological entities projecting from the virion envelope. J Gen Virol 68: 715–725

    Google Scholar 

  28. Tartakoff AM (1983) Perturbation of vesicular traffic with the carboxylic ionophore monensin. Cell 32: 1026–1028

    Google Scholar 

  29. Tennican P, Carl G, Frey J, Thies C, Chvapil M (1980) Topical zinc in the treatment of mice infected intravaginally with herpes genitalis virus. Proc Soc Exp Biol Med 164: 593–597

    Google Scholar 

  30. Tognon M, Manservigi R, Romanelli MG, Rotola A, Gatti R, Foà-Tomasi L, Campadelli-Fiume S (1988) A herpes simplex virus type 1 mutant resistant to benzhydrazone, an inhibitor of glycoprotein synthesis in herpes-infected cells. Preliminary mapping of benzhydrazone-resistance and of a novel syncytical mutant. Arch Virol 98: 199–212

    Google Scholar 

  31. Tokumaru T (1968) The nature of toxins of herpes simplex virus. I. Syncytical giant cell producing components in tissue culture. Arch Virol 24: 104–122

    Google Scholar 

  32. Wilson DW, Wilcox CA, Flynn GC, Chen E, Kuang WJ, Henzel WJ, Block MR, Ullrich A, Rothman JE (1989) A fusion protein required for vesicle-mediated transport in both mammalian cells and yeast. Nature 339: 355–359

    Google Scholar 

  33. WuDunn D, Spear PG (1989) Initial interaction of herpes simplex virus with cells is binding to heparansulfate. J Virol 63: 52–58

    Google Scholar 

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Walev, I., Wollert, K.C., Weise, K. et al. Characterization of fusion from without induced by herpes simplex virus. Archives of Virology 117, 29–44 (1991). https://doi.org/10.1007/BF01310490

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  • DOI: https://doi.org/10.1007/BF01310490

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