Actin and cell pathogenesis

Current Opinion in Cell Biology

Volumn 9, Issue 1, 1997, Pages 62-69

  Higley, Sidney ^a   Way, Michael ^a  

^a EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN;

ACTIN POLYMERIZATION; CYTOSKELETON; HOST PARASITE INTERACTION; LISTERIA MONOCYTOGENES; NONHUMAN; PATHOGENESIS; PRIORITY JOURNAL; REVIEW; SHIGELLA FLEXNERI; VIRUS;

EID: 0031042322     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(97)80153-6     Document Type: Article

References (63)

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4. 4. Kocks C, Marchand J-B, Gouin E, D'Hauteville H, Sansonetti PJ, Carlier M-F, Cossart P: The unrelated surface proteins ActA of Listeria monocytogenes and IcsA of Shigella flexneri are sufficient to confer actin-based motility on Listeria innocua and Escherichia coli respectively. Mol Microbiol 1995, 18:413-423. Describes the demonstration that ActA and IcsA are able to induce actin-tail assembly and bacterial motility when expressed in the nonpathogenic bacterial species Listeria innocua and Escherichia coli. See also related articles [3•,5•].
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21. 4 accounts for the high concentration (12μM) of unassembled actin in these extracts. Unlike in earlier work [18], Xenopus egg extracts depleted of endogenous profilin are still able to support Listeria motility [21••]. A model for Listeria motility based on the maintenance of free barbed actin ends at the bacterium surface is proposed. Interestingly, endogenous vesicles in extracts are able to induce actin assembly and move in a similar fashion to Listeria.
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24. 3, which is thought to represent the profilin-binding site in VASP, into Shigella-infected cells completely inhibits bacterial motility. This inhibition suggests that Listeria and Shigella have evolved a similar motility mechanism involving profilin and VASP.
25. 25. Reinhard M, Jouvenal K, Tripier D, Walter U: Identification, purification, and characterization of a zyxin-related protein that binds the focal adhesion and microfilament protein VASP (vasodilator-stimulated phosphoprotein). Proc Natl Acad Sci USA 1995, 92:7956-7960. Demonstration that VASP binds to a host 83 kDa protein that is related to the focal adhesion protein zyxin. Immunolocalizations show that p83 and VASP have a similar distribution at focal adhesions. It is suggested that p83 (zyxin) is responsible for targeting of VASP to stress fibres and focal adhesions.
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28. 28. Reinhard M, Rüdiger M, Jockusch BM, Walter U: VASP interaction with vinculin: a recurring theme of interactions with proline-rich motifs. FEBS Lett 1996, 399:103-107. Demonstration that VASP binds the single FPPPP (single-letter code for amino acids) motif in the hinge region between the head and tail domains of vinculin. VASP binds to vinculin with much lower efficiency than it binds to zyxin which contains four FPPPP motifs. See also the related article [29•].
29. 29. Brindle NPJ, Holt MR, Davies JE, Price CJ, Critchley DR: The focal-adhesion vasodilator phosphoprotein (VASP) binds to the proline-rich domain in vinculin. Biochem J 1996, 318:753-757. This paper shows that VASP is capable of binding the single FPPPP (single-letter code for amino acids) motif in the hinge region of vinculin. In addition, deletion of the carboxyl terminus of VASP abolishes vinculin binding. See also the related article [28•].
30. 30. Gertler FB, Niebuhr K, Reinhard M, Wehland J, Soriano P: Mena, a relative of VASP and Drosophila Enabled, is implicated in the control of microfilament dynamics. Cell 1996, 87:227-239. Describes the identification of two murine proteins, Mena and Evl, that are related to enabled and VASP. Like VASP, Mena is localized at focal adhesions and is also recruited to Listeria during infection. A conserved domain (EVH1) found in this emerging family of proteins is sufficient to target Mena to Listeria via interactions with an FPPPP (single-letter code for amino acids) motif in ActA, vinculin and zyxin. The polarized localization of Mena on the surface of motile Listeria, together with the induction of actin-rich outgrowths by expression of Mena isoforms, suggests that this protein plays a role in actin-filament assembly and cell motility.
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32. 2-dependent manner.
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36. c-src and tyrosine phosphorylation may play a role in the cytoskeletal changes that occur during Shigella invasion.
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48. -1. EPEC are also able to extend from the cell surface when not laterally translocating. All EPEC movements are inhibited by CD, suggesting that polymerization of host actin is essential. Differences in actin density and sensitivity to CD suggest a significant difference in both the organization of actin and the mechanism of motility between EPEC-induced actin pedestals and Listeria actin tails.
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55. 55. Charlton CA, Volkman LE: Penetration of Autographa californica nuclear polyhedrosis virus nucleocapsids into IPLB Sf 21 cells induces actin cable formation. Virology 1993, 197:245-254.
56. 56. Lanier LM, Slack JM, Volkman LE: Actin binding and proteolysis by the baculovirus AcMNPV: the role of virion-associated V-CATH. Virology 1996, 216:380-388.
57. 57. Ott DE, Coren LV, Kane BP, Busch LK, Johnson DG, Sowder RC II, Chertova EN, Arthur LO, Henderson LE: Cytoskeletal proteins inside human immunodeficiency virus type 1 virions. J Virol 1996, 70:7734-7743. The identification of actin isoforms as well as the actin-binding proteins ezrin, moesin and cofilin inside HIV-1 virions suggests that the actin cytoskeleton plays an important function during viral budding.
58. 58. Rey O, Canon J, Krogstad P: HIV-1 gag protein associates with F-actin present in microfilaments. Virology 1996, 220:530-534. Demonstration that, in vivo, unprocessed HIV-1 gag is associated with the actin cytoskeleton in infected cells and when expressed in a nonviral background. In vitro cosedimentation assays show that HIV-1 gag interacts directly with actin filaments.
59. 59. Sasaki H, Nakamura M, Ohno T, Matsuda Y, Yuda Y, Nonomura Y: Myosin-actin interaction plays an important role in human immunodeficiency virus type 1 release from host cells. Proc Natl Acad Sci USA 1995, 92:2026-2030.
60. -1. The similarities between vaccinia and bacterial systems suggest that intracellular pathogens have developed a common mechanism to exploit the actin cytoskeleton of their host in order to facilitate their spread.
61. 61. Cudmore S, Reckmann I, Griffiths G, Way M: Vaccinia virus: a model system for actin-membrane interactions. J Cell Sci 1996, 109:1739-1747. Examination of the structural organization of vaccinia actin tails. The incorporation of rhodamine actin in a permeablized cell system is used to analyze the mechanism of actin-tail assembly. Evidence is presented that actin-nucleation sites on the virus particle surface become transferred to the inner surface of the plasma membrane during viral fusion with the plasma membrane.
62. 62. Strauss EJ: Intracellular pathogens: a virus joins the movement. Curr Biol 1996, 6:504-507.
63. 63. Sanders MA, Theriot JA: Tails from the hall of infection: actin-based motility of pathogens. Trends Microbiol 1996, 4:211-213.