1887

Abstract

Purified porcine monocytes, the natural carrier cells of pseudorabies virus (PrV) in the pig, were inoculated in vitro with PrV. At different time-points post-inoculation (p.i.) (from 7 to 17 h p.i.), the cells were washed and incubated with fluorescein isothiocyanate-labelled porcine PrV-specific polyclonal antibodies (IgG) at 37 degrees C. At all time-points tested p.i., 1 h of antibody incubation induced passive patching and subsequent internalization of the plasma membrane-anchored viral glycoproteins in approximately 65% of the infected monocytes. This endocytosis process is antibody-dependent, since biotinylated glycoproteins did not undergo spontaneous endocytosis. The process is fast and efficient, since only very low amounts of viral glycoproteins on the plasma membrane (7 h p.i.) and a minimal concentration of antibodies (0.04 mg IgG/ml) were needed to induce endocytosis. Experiments with PrV strains carrying deletions in the genes encoding the 11 different viral glycoproteins showed that viral glycoproteins gB and gD play a very important role in endocytosis (80% reduction with deletion mutants, P < 0.001), while the gE:gI Fc receptor complex, but not gE or gI alone, has a significant but lesser effect (45% reduction, P < 0.05). Double staining of viral glycoproteins and major histocompatibility complex class I (MHC I) showed a clear co-localization and co-endocytosis of MHC I with the viral glycoproteins, suggesting a possible role of the process in immune evasion of the virus.

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1999-05-01
2022-05-19
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References

  1. Alberts B., Bray D., Lewis J., Raff M., Roberts K., Watson J. D. 1994 Molecular Biology of the Cell 3rd edn New York: Garland Publishing;
    [Google Scholar]
  2. Banks T. A., Rouse B. T. 1992; Herpesviruses – immune escape artists?. Clinical Infectious Diseases 14:933–941
    [Google Scholar]
  3. Collins K. L., Chen B. K., Kalams S. A., Walker B. D., Baltimore D. 1998; HIV-1 Nef protein protects infected primary cells against killing by cytotoxic T lymphocytes. Nature 391:397–401
    [Google Scholar]
  4. Dijkstra J. M., Visser N., Mettenleiter T. C., Klupp B. G. 1996; Identification and characterization of pseudorabies virus glycoprotein gM as a nonessential virion component. Journal of Virology 70:5684–5688
    [Google Scholar]
  5. Favoreel H. W., Nauwynck H. J., Van Oostveldt P., Mettenleiter T. C., Pensaert M. B. 1997; Antibody-induced and cytoskeleton-mediated redistribution and shedding of viral glycoproteins, expressed on pseudorabies virus-infected cells. Journal of Virology 71:8254–8261
    [Google Scholar]
  6. Jöns A., Granzow H., Kuchling R., Mettenleiter T. C. 1996; The UL49.5 gene of pseudorabies virus codes for an O-glycosylated structural protein of the viral envelope. Journal of Virology 70:1237–1241
    [Google Scholar]
  7. Kaplan A. S., Vatter A. E. 1959; A comparison of herpes simplex and pseudorabies virus. Virology 7:394–407
    [Google Scholar]
  8. Kärre K. 1997; How to recognize a foreign submarine. Immunological Reviews 155:5–9
    [Google Scholar]
  9. Kimman T. G. 1994; Immunological protection against pseudorabies virus. pp 11–22 Proceedings of the Office International des Epizooties Aujeszky’s Disease Symposium (Bangkok, Thailand, June 1994)
    [Google Scholar]
  10. Kimman T. G., De Bruin T. G. M., Voermans J. J. M., Bianchi A. T. J. 1996; Cell-mediated immunity to pseudorabies virus: cytolytic effector cells with characteristics of lymphokine-activated killer cells lyse virus-infected and glycoprotein gB- and gC-transfected L14 cells. Journal of General Virology 77:987–990
    [Google Scholar]
  11. Klupp B. G., Visser N., Mettenleiter T. C. 1992; Identification and characterization of pseudorabies virus glycoprotein gH. Journal of Virology 66:3048–3055
    [Google Scholar]
  12. Klupp B. G., Fuchs W., Weiland E., Mettenleiter T. C. 1997; Pseudorabies virus glycoprotein L is necessary for virus infectivity but dispensable for virion localization of glycoprotein gH. Journal of Virology 71:7687–7695
    [Google Scholar]
  13. Klupp B. G., Baumeister J., Dietz P., Granzow H., Mettenleiter T. C. 1998; Pseudorabies virus glycoprotein gK is a virion structural component involved in virus release but is not required for entry. Journal of Virology 72:1949–1958
    [Google Scholar]
  14. Martin S., Wardley R. C. 1984; Natural cytotoxicity detected in swine using Aujeszky′s disease virus infected cells. Research in Veterinary Science 37:211–218
    [Google Scholar]
  15. Mettenleiter T. C., Schreurs C., Zuckermann F., Ben-Porat T. 1987a; Role of pseudorabies virus glycoprotein gl in virus release from infected cells. Journal of Virology 61:2764–2769
    [Google Scholar]
  16. Mettenleiter T. C., Zsak L., Kaplan A. S., Ben-Porat T., Lomniczi B. 1987b; Role of a structural glycoprotein of pseudorabies virus in virus virulence. Journal of Virology 61:4030–4032
    [Google Scholar]
  17. Mettenleiter T. C., Schreurs C., Zuckermann F., Ben-Porat T., Kaplan A. S. 1988; Role of glycoprotein gIII of pseudorabies virus in virulence. Journal of Virology 62:2712–2717
    [Google Scholar]
  18. Nauwynck H. J., Pensaert M. B. 1992; Abortion induced by cell- associated pseudorabies virus in vaccinated sows. American Journal of Veterinary Research 53:489–493
    [Google Scholar]
  19. Nauwynck H. J., Pensaert M. B. 1994; Interactions of Aujeszky’s disease virus and porcine blood mononuclear cells in vivo and in vitro. Acta Veterinaria Hungarica 42:301–308
    [Google Scholar]
  20. Nauwynck H. J., Pensaert M. B. 1995; Effect of specific antibodies on the cell-associated spread of pseudorabies virus in monolayers of different cell types. Archives of Virology 140:1137–1146
    [Google Scholar]
  21. Olson J. K., Grose C. 1997; Endocytosis and recycling of varicella- zoster virus Fc receptor glycoprotein gE: internalization mediated by a YXXL motif in the cytoplasmic tail. Journal of Virology 71:4042–4054
    [Google Scholar]
  22. Pescovitz M. D., Lunney J. K., Sachs D. H. 1984; Preparation and characterization of monoclonal antibodies reactive with porcine PBL. Journal of Immunology 13:368–375
    [Google Scholar]
  23. Ploegh H. L. 1998; Viral strategies of immune evasion. Science 280:248–253
    [Google Scholar]
  24. Rauh I., Mettenleiter T. C. 1991; Pseudorabies virus glycoprotein gII and gp50 are essential for virus penetration. Journal of Virology 65:5348–5356
    [Google Scholar]
  25. Rauh I., Weiland F., Fehler F., Keil G. M., Mettenleiter T. C. 1991; Pseudorabies virus mutants lacking the essential glycoprotein gII can be complemented by glycoprotein gI of bovine herpesvirus 1. Journal of Virology 65:621–631
    [Google Scholar]
  26. Reth M. 1989; Antigen receptor tail clue. Nature 338:383–384
    [Google Scholar]
  27. Sandoval I. V., Bakke O. 1994; Targeting of membrane proteins to endosomes and lysosomes. Trends in Cell Biology 4:292–296
    [Google Scholar]
  28. Tirabassi R. S., Enquist L. W. 1998; Role of envelope protein gE endocytosis in the pseudorabies virus life cycle. Journal of Virology 72:4571–4579
    [Google Scholar]
  29. Wittmann G., Jakubik J., Ahl R. 1980; Multiplication and distribution of Aujeszky’s disease (pseudorabies) virus in vaccinated and non-vaccinated pigs after intranasal infection. Archives of Virology 66:227–240
    [Google Scholar]
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