Literature DB >> 1618908

How Listeria exploits host cell actin to form its own cytoskeleton. I. Formation of a tail and how that tail might be involved in movement.

L G Tilney1, D J DeRosier, M S Tilney.   

Abstract

After Listeria is phagocytosed by a macrophage, it dissolves the phagosomal membrane and enters the cytoplasm. The Listeria then nucleates actin filaments from its surface. These actin filaments rearrange to form a tail with which the Listeria moves to the macrophage surface as a prelude to spreading. Since individual actin filaments appear to remain in their same positions in the tail in vitro after extraction with detergent, the component filaments must be cross-bridged together. From careful examination of the distribution of actin filaments attached to the surface of Listeria and in the tail, and the fact that during and immediately after division filaments are not nucleated from the new wall formed during septation, we show how a cloud of actin filaments becomes rearranged into a tail simply by the mechanics of growth. From lineage studies we can relate the length of the tail to the age of the surface of Listeria and make predictions as to the ratio of Listeria with varying tail lengths at a particular time after the initial infection. Since we know that division occurs about every 50 min, after 4 h we would predict that if we started with one Listeria in a macrophage, 16 bacteria would be found, two with long tails, two with medium tails, four with tiny tails, and eight with no tails or a ratio of 1:1:2:4. We measured the lengths of the tails on Listeria 4 h after infection in serial sections and confirmed this prediction. By decorating the actin filaments that make up the tail of Listeria with subfragment 1 of myosin we find (a) that the filaments are indeed short (maximally 0.3 microns in length); (b) that the filament length is approximately the same at the tip and the base of the tail; and (c) that the polarity of these filaments is inappropriate for myosin to be responsible or to facilitate movement through the cytoplasm, but the polarity insures that the bacterium will be located at the tip of a pseudopod, a location that is essential for spreading to an adjacent cell. Putting all this information together we can begin to unravel the problem of how the Listeria forms the cytoskeleton and what is the biological purpose of this tail. Two functions are apparent: movement and pseudopod formation.

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Year:  1992        PMID: 1618908      PMCID: PMC2289525          DOI: 10.1083/jcb.118.1.71

Source DB:  PubMed          Journal:  J Cell Biol        ISSN: 0021-9525            Impact factor:   10.539


  18 in total

1.  Cell wall replication in Streptococcus pyogenes.

Authors:  R M COLE; J J HAHN
Journal:  Science       Date:  1962-03-02       Impact factor: 47.728

2.  Adoptive transfer of immunity to Listeria monocytogenes. The influence of in vitro stimulation on lymphocyte subset requirements.

Authors:  D K Bishop; D J Hinrichs
Journal:  J Immunol       Date:  1987-09-15       Impact factor: 5.422

3.  How Listeria exploits host cell actin to form its own cytoskeleton. II. Nucleation, actin filament polarity, filament assembly, and evidence for a pointed end capper.

Authors:  L G Tilney; D J DeRosier; A Weber; M S Tilney
Journal:  J Cell Biol       Date:  1992-07       Impact factor: 10.539

4.  Mapping of the microvillar 110K-calmodulin complex: calmodulin-associated or -free fragments of the 110-kD polypeptide bind F-actin and retain ATPase activity.

Authors:  L M Coluccio; A Bretscher
Journal:  J Cell Biol       Date:  1988-02       Impact factor: 10.539

5.  Formation of arrowhead complexes with heavy meromyosin in a variety of cell types.

Authors:  H Ishikawa; R Bischoff; H Holtzer
Journal:  J Cell Biol       Date:  1969-11       Impact factor: 10.539

6.  Actin filaments and the growth, movement, and spread of the intracellular bacterial parasite, Listeria monocytogenes.

Authors:  L G Tilney; D A Portnoy
Journal:  J Cell Biol       Date:  1989-10       Impact factor: 10.539

7.  Actin filament nucleation by the bacterial pathogen, Listeria monocytogenes.

Authors:  L G Tilney; P S Connelly; D A Portnoy
Journal:  J Cell Biol       Date:  1990-12       Impact factor: 10.539

8.  Characterization of intestinal microvillar membrane disks: detergent-resistant membrane sheets enriched in associated brush border myosin I (110K-calmodulin).

Authors:  M S Mooseker; K A Conzelman; T R Coleman; J E Heuser; M P Sheetz
Journal:  J Cell Biol       Date:  1989-09       Impact factor: 10.539

9.  Role of hemolysin for the intracellular growth of Listeria monocytogenes.

Authors:  D A Portnoy; P S Jacks; D J Hinrichs
Journal:  J Exp Med       Date:  1988-04-01       Impact factor: 14.307

10.  Calcium-regulated cooperative binding of the microvillar 110K-calmodulin complex to F-actin: formation of decorated filaments.

Authors:  L M Coluccio; A Bretscher
Journal:  J Cell Biol       Date:  1987-07       Impact factor: 10.539

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  42 in total

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Review 2.  Actin-based motility of intracellular microbial pathogens.

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4.  VASP protects actin filaments from gelsolin: an in vitro study with implications for platelet actin reorganizations.

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5.  Probing polymerization forces by using actin-propelled lipid vesicles.

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Journal:  Proc Natl Acad Sci U S A       Date:  2003-03-25       Impact factor: 11.205

6.  Actin-membrane coupling: a role for talin.

Authors:  G Isenberg; W H Goldmann
Journal:  J Muscle Res Cell Motil       Date:  1992-12       Impact factor: 2.698

7.  Quantitative analysis of actin turnover in Listeria comet tails: evidence for catastrophic filament turnover.

Authors:  Hao Yuan Kueh; William M Brieher; Timothy J Mitchison
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Review 8.  Intracellular transport of hepatitis B virus.

Authors:  Michael Kann; Andre Schmitz; Birgit Rabe
Journal:  World J Gastroenterol       Date:  2007-01-07       Impact factor: 5.742

9.  Deformations in actin comets from rocketing beads.

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10.  Mechanism of Cdc42-induced actin polymerization in neutrophil extracts.

Authors:  S H Zigmond; M Joyce; C Yang; K Brown; M Huang; M Pring
Journal:  J Cell Biol       Date:  1998-08-24       Impact factor: 10.539

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