The Parasitophorous Vacuole Membrane Surrounding T. Gondii: A Specialized Interface Between Parasite and Cell

  • Keith A. Joiner
Conference paper
Part of the NATO ASI Series book series (volume 78)

Abstract

Cell invasion by apicomplexan parasites is a rapid yet highly ordered process dependent upon oriented attachment of the parasite to the target cell, parasite motility, and secretion of anterior organelles (rhoptries) during the invasion event (reviewed in Werk 1985). Subsequent to invasion of the host cell, the apicomplexan parasite, Toxoplasma gondii, resides within a specialized parasitophorous vacuole (PV). Unlike phagolysosomes, the parasitophorous vacuole neither fuses with lysosomes nor acidifies [Joiner et al. 1990; Jones and Hirsch 1972; Sibley et al. 1985].

Keywords

Toxoplasma Gondii Nucleoside Transport Parasitophorous Vacuole Apicomplexan Parasite Putative Transmembrane Domain 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. Allegra, C.J., Kovacs, J.A., Drake, J.C, Swan, J.C., Chabner, B.A. and Masur, H. [ 1987 ]. Potent in vitro and in vivo antitoxoplasma activity of the lipid-soluble antifolate trimetrexate. J. Clin. Invest. 79: 478–482.PubMedCrossRefGoogle Scholar
  2. Achbarou, A., Mercereau-Puijalon, O., Sadak, A., Fortier, B., Leriche, J.A., Camus, D., and Dubremetz, J.F. [ 1991 ]. Differential targeting of dense granule proteins in the parasitophorous vacuole of Toxoplasma gondii. Parasitology. 103: 321–329.PubMedCrossRefGoogle Scholar
  3. Asai, T. and Kim, T. [ 1987 ]. Possible regulation mechanism of potent nucleoside triphosphate hydrolase in Toxoplasma gondii. Zentralbl Bakteriol Mikrobiol Hyg A. 264: 464–467.PubMedGoogle Scholar
  4. Asai, T., and O’Sullivan, W.J. [ 1983 ]. A potent nucleoside triphosphate hydrolase from the parasitic protozoan Toxoplasma gondii. J. Biol. Chem. 258: 6816–6822.PubMedGoogle Scholar
  5. Cesbron-Delauw, M.F., Guy, B., Torpier, G., Pierce, R.J., Lenzen, G., Cesbron, J.Y., Charif, H., Lepage, P., Darcy, F., Lecocq, J.P. and Capron, A. [ 1989 ]. Molecular characterization of a 23-kilodalton major antigen secreted by Toxoplasma gondii. Proc. Natl. Acad. Sci. 86: 7537–7541.Google Scholar
  6. Chamberland, S., Kirst, H.A. and Current, W.L. [ 1991 ]. Comparative activity of macrolides against Toxoplasma gondii demonstrating utility of an in vitro microassay. Antimicrob. Agents Chemo. 35: 903–909.Google Scholar
  7. Chang, H.R. and Pechere, J.C.F. [ 1988 ]. In vitro effects of four macrolides (roxithromycin, spiramycin, azithromycin [CP-62-993] and A-56268) on Toxoplasma gondii. Antimicrob. Agents Chemo. 32: 524–529.Google Scholar
  8. Charif, H., Darcy, F., Torpier, G., Cesbron-Delauw, M.F. and Capron, A. [ 1990 ]. “Characterization and localization of antigens secreted from tachyzoites”. Exp. Parasit. 71: 114–124.PubMedCrossRefGoogle Scholar
  9. Danneman, B. [ 1992 ]. Treatment of toxoplasmic encephalitis in patients with AIDS: A randomized trial comparing pyrimethamine plus clindamycin to pyrimethamine plus sulfadiazine. Ann. Int. Med. 116: 33–43.Google Scholar
  10. Furtado, G.C., Slowik, M., Kleinman, H.K. and Joiner, K.A. [ 1992c ]. Laminin enhances binding of Toxoplasma gondii tachyzoites to J774 murine macrophage cells. Infect. Immun. 60: 2337–2342.PubMedGoogle Scholar
  11. Furtado, G.C., Collins, F.L., Cao, J. and Joiner, K.A., [ 1992a ]. Laminin on tachyzoites of Toxoplasma gondii mediates parasite binding to the βl integrin receptor α6βl on human foreskin fibroblasts and Chinese hamster ovary cells. Submitted.Google Scholar
  12. Furtado, G.C., Fuhr man, S.A., Dubremetz, J.F. and Joiner, K.A. [ 1992b ]. Detergent insolube surface proteins on Toxoplasma gondii mediate cell attachment and include host-derived laminin and 32/67 laminin binding protein. Submitted.Google Scholar
  13. Harris, C., Salgo, M.P., Tanowitz, H.B., and Wittner, M. [ 1988 ] In vitro assessment of antimicrobial agents against Toxoplasma gondii. J. Infect. Dis. 157: 14–22.PubMedCrossRefGoogle Scholar
  14. Johnson, A.M., Illana, S., McDonald, P.J., and Asai, T. [ 1989 ]. Cloning expression and nucleotide sequence of the gene fragment encoding an antigenic portion of the nucleoside triphosphate hydrolase of Toxoplasma gondii. Gene. 85: 215–220.PubMedCrossRefGoogle Scholar
  15. Joiner, K.A., Fuhrman, S.A., Mietinnen, H., Kasper, L.H., and Mellman, I. [ 1990 ]. Toxoplasma gondii: Fusion competence of parasitophorous vacuoles in Fc receptor transfected fibroblasts. Science. 249: 641–646.PubMedCrossRefGoogle Scholar
  16. Jones, T.C., and Hirsch, J.G. [ 1972 ]. The interaction between Toxoplasma gondii and mammalian cells. II. The absence of lysosomal fusion with phagocytic vacuoles containing living parasites. J. Exp. Med. 136: 1173.PubMedCrossRefGoogle Scholar
  17. Krug, E.C., Marr, J.J. and Berens, R.L. [ 1989 ]. Purine metabolism in Toxoplasma gondii. J. Biol. Chem. 264: 10601–10607.PubMedGoogle Scholar
  18. Leriche, M.A., and Dubremetz, J.F. [ 1991 ]. Characterization of the protein contents of rhoptries and dense granules of Toxoplasma gondii tachyzoites by subcellular fractionation and monoclonal antibodies. Mol. Biochem, Parasit. 45: 249–260.CrossRefGoogle Scholar
  19. Pfefferkorn, E.R. [1988]. Toxoplasma gondii viewed from a virological perspective. The Biology of Parasitism., New York, Alan R. Liss.Google Scholar
  20. Plagemann, P.G.W., Wohlhueter, R.M. and Woffendin, C. [ 1988 ]. Nucleoside and nucleobase transport in animal cells. Biochim. Biophys. Acta. 947: 405–443.Google Scholar
  21. Porchet-Hennere, E., and Torpier, G. [ 1983 ]. Relations entre Toxoplasma et sa cellule-hote. Protistologica. 3: 357.Google Scholar
  22. Remington, J.S., and McLeod, R. [1992]. Toxoplasmosis. Infectious Diseases. Philadelphia, W.B. Saunders. Sibley, D.L. and Krahenbuhl, J.L. [ 1988 ]. Modification of host cell phagosomes by Toxoplasma gondii involves redistribution of surface proteins and secretion of a 32kDa protein. Eur. J. Cell Biol. 47: 81–87.Google Scholar
  23. Sibley, D.L. and Krahenbuhl, J.L. [1988]. Modification of host cell phagosomes by Toxoplasma gondii involves redistribution of surface of surface proteins and sectretion of a 32kDa protein. Eur. J. Cell Biol. 47: 81–.Google Scholar
  24. Sibley, L.D., Krahenbuhl, J.L., Adams, G.M.W. and Weidner, E. [ 1986 ]. Toxoplasma modifies macrophage phagosomes by secretion of a vesicular network rich in surface proteins. J. Cell Biol. 103: 867–874.PubMedCrossRefGoogle Scholar
  25. Sibley, L.D., Weidner, E., and Krahenbuhl, J.L. [ 1985 ]. Phagosome acidification blocked by intracellular Toxoplasma gondii. Nature. 315: 1985.CrossRefGoogle Scholar
  26. Werk, R. [ 1985 ]. How does Toxoplasma gondii enter host cells? Rev. Infect. Dis. 7: 449–457.PubMedCrossRefGoogle Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 1993

Authors and Affiliations

  • Keith A. Joiner
    • 1
  1. 1.Section of Infectious Diseases Department of MedicineYale University School of MedicineNew HavenUSA

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