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. 1998;109:160–173.

Listeria and Shigella actin-based motility in host cells.

F S Southwick 1, D L Purich 1
PMCID: PMC2194352  PMID: 9601135

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bernardini M. L., Mounier J., d'Hauteville H., Coquis-Rondon M., Sansonetti P. J. Identification of icsA, a plasmid locus of Shigella flexneri that governs bacterial intra- and intercellular spread through interaction with F-actin. Proc Natl Acad Sci U S A. 1989 May;86(10):3867–3871. doi: 10.1073/pnas.86.10.3867. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bârzu S., Benjelloun-Touimi Z., Phalipon A., Sansonetti P., Parsot C. Functional analysis of the Shigella flexneri IpaC invasin by insertional mutagenesis. Infect Immun. 1997 May;65(5):1599–1605. doi: 10.1128/iai.65.5.1599-1605.1997. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Chakraborty T., Ebel F., Domann E., Niebuhr K., Gerstel B., Pistor S., Temm-Grove C. J., Jockusch B. M., Reinhard M., Walter U. A focal adhesion factor directly linking intracellularly motile Listeria monocytogenes and Listeria ivanovii to the actin-based cytoskeleton of mammalian cells. EMBO J. 1995 Apr 3;14(7):1314–1321. doi: 10.1002/j.1460-2075.1995.tb07117.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Dabiri G. A., Sanger J. M., Portnoy D. A., Southwick F. S. Listeria monocytogenes moves rapidly through the host-cell cytoplasm by inducing directional actin assembly. Proc Natl Acad Sci U S A. 1990 Aug;87(16):6068–6072. doi: 10.1073/pnas.87.16.6068. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Domann E., Wehland J., Rohde M., Pistor S., Hartl M., Goebel W., Leimeister-Wächter M., Wuenscher M., Chakraborty T. A novel bacterial virulence gene in Listeria monocytogenes required for host cell microfilament interaction with homology to the proline-rich region of vinculin. EMBO J. 1992 May;11(5):1981–1990. doi: 10.1002/j.1460-2075.1992.tb05252.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Dramsi S., Biswas I., Maguin E., Braun L., Mastroeni P., Cossart P. Entry of Listeria monocytogenes into hepatocytes requires expression of inIB, a surface protein of the internalin multigene family. Mol Microbiol. 1995 Apr;16(2):251–261. doi: 10.1111/j.1365-2958.1995.tb02297.x. [DOI] [PubMed] [Google Scholar]
  7. Gaillard J. L., Berche P., Frehel C., Gouin E., Cossart P. Entry of L. monocytogenes into cells is mediated by internalin, a repeat protein reminiscent of surface antigens from gram-positive cocci. Cell. 1991 Jun 28;65(7):1127–1141. doi: 10.1016/0092-8674(91)90009-n. [DOI] [PubMed] [Google Scholar]
  8. Havell E. A. Synthesis and secretion of interferon by murine fibroblasts in response to intracellular Listeria monocytogenes. Infect Immun. 1986 Dec;54(3):787–792. doi: 10.1128/iai.54.3.787-792.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Kang F., Laine R. O., Bubb M. R., Southwick F. S., Purich D. L. Profilin interacts with the Gly-Pro-Pro-Pro-Pro-Pro sequences of vasodilator-stimulated phosphoprotein (VASP): implications for actin-based Listeria motility. Biochemistry. 1997 Jul 8;36(27):8384–8392. doi: 10.1021/bi970065n. [DOI] [PubMed] [Google Scholar]
  10. Kathariou S., Metz P., Hof H., Goebel W. Tn916-induced mutations in the hemolysin determinant affecting virulence of Listeria monocytogenes. J Bacteriol. 1987 Mar;169(3):1291–1297. doi: 10.1128/jb.169.3.1291-1297.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Kocks C., Gouin E., Tabouret M., Berche P., Ohayon H., Cossart P. L. monocytogenes-induced actin assembly requires the actA gene product, a surface protein. Cell. 1992 Feb 7;68(3):521–531. doi: 10.1016/0092-8674(92)90188-i. [DOI] [PubMed] [Google Scholar]
  12. Laine R. O., Zeile W., Kang F., Purich D. L., Southwick F. S. Vinculin proteolysis unmasks an ActA homolog for actin-based Shigella motility. J Cell Biol. 1997 Sep 22;138(6):1255–1264. doi: 10.1083/jcb.138.6.1255. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Ménard R., Prévost M. C., Gounon P., Sansonetti P., Dehio C. The secreted Ipa complex of Shigella flexneri promotes entry into mammalian cells. Proc Natl Acad Sci U S A. 1996 Feb 6;93(3):1254–1258. doi: 10.1073/pnas.93.3.1254. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Pantaloni D., Carlier M. F. How profilin promotes actin filament assembly in the presence of thymosin beta 4. Cell. 1993 Dec 3;75(5):1007–1014. doi: 10.1016/0092-8674(93)90544-z. [DOI] [PubMed] [Google Scholar]
  15. Portnoy D. A., Jacks P. S., Hinrichs D. J. Role of hemolysin for the intracellular growth of Listeria monocytogenes. J Exp Med. 1988 Apr 1;167(4):1459–1471. doi: 10.1084/jem.167.4.1459. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Purich D. L., Southwick F. S. ABM-1 and ABM-2 homology sequences: consensus docking sites for actin-based motility defined by oligoproline regions in Listeria ActA surface protein and human VASP. Biochem Biophys Res Commun. 1997 Feb 24;231(3):686–691. doi: 10.1006/bbrc.1997.6158. [DOI] [PubMed] [Google Scholar]
  17. Reinhard M., Halbrügge M., Scheer U., Wiegand C., Jockusch B. M., Walter U. The 46/50 kDa phosphoprotein VASP purified from human platelets is a novel protein associated with actin filaments and focal contacts. EMBO J. 1992 Jun;11(6):2063–2070. doi: 10.1002/j.1460-2075.1992.tb05264.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Sanger J. M., Sanger J. W., Southwick F. S. Host cell actin assembly is necessary and likely to provide the propulsive force for intracellular movement of Listeria monocytogenes. Infect Immun. 1992 Sep;60(9):3609–3619. doi: 10.1128/iai.60.9.3609-3619.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Southwick F. S., Purich D. L. Arrest of Listeria movement in host cells by a bacterial ActA analogue: implications for actin-based motility. Proc Natl Acad Sci U S A. 1994 May 24;91(11):5168–5172. doi: 10.1073/pnas.91.11.5168. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Southwick F. S., Purich D. L. Intracellular pathogenesis of listeriosis. N Engl J Med. 1996 Mar 21;334(12):770–776. doi: 10.1056/NEJM199603213341206. [DOI] [PubMed] [Google Scholar]
  21. Stossel T. P. The machinery of cell crawling. Sci Am. 1994 Sep;271(3):54-5, 58-63. doi: 10.1038/scientificamerican0994-54. [DOI] [PubMed] [Google Scholar]
  22. Theriot J. A., Mitchison T. J., Tilney L. G., Portnoy D. A. The rate of actin-based motility of intracellular Listeria monocytogenes equals the rate of actin polymerization. Nature. 1992 May 21;357(6375):257–260. doi: 10.1038/357257a0. [DOI] [PubMed] [Google Scholar]
  23. Theriot J. A., Rosenblatt J., Portnoy D. A., Goldschmidt-Clermont P. J., Mitchison T. J. Involvement of profilin in the actin-based motility of L. monocytogenes in cells and in cell-free extracts. Cell. 1994 Feb 11;76(3):505–517. doi: 10.1016/0092-8674(94)90114-7. [DOI] [PubMed] [Google Scholar]
  24. Tilney L. G., Portnoy D. A. Actin filaments and the growth, movement, and spread of the intracellular bacterial parasite, Listeria monocytogenes. J Cell Biol. 1989 Oct;109(4 Pt 1):1597–1608. doi: 10.1083/jcb.109.4.1597. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Zeile W. L., Purich D. L., Southwick F. S. Recognition of two classes of oligoproline sequences in profilin-mediated acceleration of actin-based Shigella motility. J Cell Biol. 1996 Apr;133(1):49–59. doi: 10.1083/jcb.133.1.49. [DOI] [PMC free article] [PubMed] [Google Scholar]

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