1887

Abstract

Vaccinia virus infection dramatically affects the host actin cytoskeleton by inducing disassembly of actin stress fibres and formation of actin tails which propel the virus intra- and intercellularly. The viral factors responsible for these actin rearrangements remain unknown. Sequence analysis reveals significant homology between the vaccinia F8L ORF and the proline repeats of iActA, the protein which initiates actin tail assembly and motility in the bacterial pathogen . We characterized the F8L gene product to examine its possible role in vaccinia rearrangements of the host actin cytoskeleton. F8L is a ~ 8 kDa protein expressed early during infection and is found throughout the cytoplasm, with no discernible association with viral or cellular structures. Furthermore, the F8L deletion strain, WR∆F8L, forms particles and actin tails indistinguishable from WR. Our observations demonstrate that F8L is not required for vaccinia virus morphogenesis or the actin rearrangements observed during infection.

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1997-10-01
2024-04-25
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References

  1. Cudmore S., Cossart P., Griffiths G., Way M. 1995; Actin-based motility of vaccinia virus. Nature 378:636–638
    [Google Scholar]
  2. Cudmore S., Reckmann I., Griffiths G., Way M. 1996; Vaccinia virus: a model system for actin-membrane interactions. Journal of Cell Science 109:1739–1747
    [Google Scholar]
  3. Cudmore S., Reckmann I., Way M. 1997; Viral manipulations ofthe actin cytoskeleton. Trends in Microbiology 5:142–148
    [Google Scholar]
  4. Gerstel B., Grobe L., Pistor S., Chakraborty T., Wehland J. 1996; The ActA polypeptides of Listeria ivanovii and Listeria monocytogenes harbor related binding sites for host microfilament proteins. Infection and Immunity 64:1929–1936
    [Google Scholar]
  5. Goldberg M. B., Theriot J. A. 1995; Shigella flexneri surface protein IcsA is sufficient to direct actin-based motility. Proceedings of the National Academy of Sciences USA: 926572–6576
    [Google Scholar]
  6. Gouin E., Dehoux P., Mengaud J., Kocks C., Cossart P. 1995; iactA of Listeria ivanovii, although distantly related to Listeria monocytogenes actA, restores actin tail formation in an L monocytogenes actA mutant. Infection and Immunity 63:2729–2737
    [Google Scholar]
  7. Higley S., Way M. 1997; Actin and cell pathogenesis. Current Opinion in Cell Biology 9:62–69
    [Google Scholar]
  8. Hiller G., Jungwirth C., Weber K. 1981; Fluorescence microscopical analysis of the life cycle of vaccinia virus in the chick embryo fibroblasts. Experimental Cell Research 132:81–87
    [Google Scholar]
  9. Hiller G., Weber K., Schneider L., Parajsz C., Jungwirth C. 1979; Interaction of assembled progeny pox viruses with the cellular cyto- skeleton. Virology 98:142–153
    [Google Scholar]
  10. Jensen O. N., Houthaeve T., Shevchenko A., Cudmore S., Ashford T., Mann M., Griffiths G., Krijnse Locker J. 1996; Identification of the major membrane and core proteins of vaccinia virus by twodimensional electrophoresis. Journal of Virology 70:7485–7497
    [Google Scholar]
  11. Kocks C., Marchand J.-B., Gouin E., D’Hauteville H., Sansonetti P. J., Carlier M.-F., Cossart P. 1995; The unrelated surfaces proteins ActA of Listeria monocytogenes and IcsA of Shigella flexneri are sufficient to confer actin-based motility on Listeria innocua and Escherichia coli respectively. Molecular Microbiology 18:413–423
    [Google Scholar]
  12. Kreft J., Dumbsky M., Theiss S. 1995; The actin-polymerization protein from Listeria ivanovii is a large repeat protein which shows only limited amino acid sequence homology to ActA from Listeria mono cytogenes. FEMS Microbiology Letters 132:181–182
    [Google Scholar]
  13. Lasa I., David V., Gouin E., Marchand J.-B., Cossart P. 1995; The amino-terminal part of ActA is critical for the actin-based motility of Listeria monocytogenes ; the central proline-rich region acts as a stimulator. Molecular Microbiology 18:425–436
    [Google Scholar]
  14. Pistor S., Chakraborty T., Walter U., Wehland J. 1995; The bacterial actin nucleator protein ActA of Listeria monocytogenes contains multiple binding sites for host microfilament proteins. Current Biology 5:517–525
    [Google Scholar]
  15. Rodriguez J. F., Janeczko R., Esteban M. 1985; Isolation and characterization of neutralizing monoclonal antibodies to vaccinia virus. Journal of Virology 56:482–488
    [Google Scholar]
  16. Schmelz M., Sodeik B., Ericsson M., Wolffe E. J., Shida H., Hiller G., Griffiths G. 1994; Assembly of vaccinia virus : the second wrapping cisterna is derived from the trans Golgi network. Journal of Virology 68:130–147
    [Google Scholar]
  17. Smith G. A., Portnoy D. A., Theriot J. A. 1995; Asymmetric distribution of the Listeria monocytogenes ActA protein is required and sufficient to direct actin-based motility. Molecular Microbiology 17:945–951
    [Google Scholar]
  18. Sodeik B., Doms R. W., Ericsson M., Hiller G., Machamer C. E., Hof W. v. t., Meer G. v., Moss B., Griffiths G. 1993; Assembly of vaccinia virus : role of the intermediate compartment between the endoplasmic reticulum and the Golgi stacks. Journal of Cell Biology 121:521–541
    [Google Scholar]
  19. Southwick F. S., Purich D. L. 1994; Arrest of Listeria movement in host cells by a bacterial ActA analogue : implications for actin-based motility. Proceedings of the National Academy of Sciences USA: 915168–5172
    [Google Scholar]
  20. Stokes G. V. 1976; High-voltage electron microscope study of the release of vaccinia virus from whole cells. Journal of Virology 18:636–643
    [Google Scholar]
  21. Suzuki T., Saga S., Sasakawa C. 1996; Functional analysis of Shigella VirG domains essential for interaction with vinculin and actin- based motility. Journal of Biological Chemistry 271:21878–21885
    [Google Scholar]
  22. Theriot J. A. 1995; The cell biology of infection by intracellular bacterial pathogens. Annual Review of Cell and Developmental Biology 11:213–239
    [Google Scholar]
  23. Zeile W. L., Purich D. L., Southwick F. S. 1996; Recognition of two classes of oligoproline sequences in profilin-mediated acceleration of actin-based Shigella motility. Journal of Cell Biology 133:49–59
    [Google Scholar]
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