Actin Cytoskeleton: Missing link for intracellular bacterial motility?
Current BiologyPublished 1 August 1995Open access
Thomas D. Pollard
Citations45
SJR quartileQ1
SJR score2.71
SNIP1.83
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TL;DR
Vasodilator-stimulated phosphoprotein associates with virulence factors on the surface of intracellular bacteria; by binding to profilin, VASP may help direct the actin assembly that appears to drive bacterial motility.
Abstract
Vasodilator-stimulated phosphoprotein (VASP) associates with virulence factors on the surface of intracellular bacteria; by binding to profilin, VASP may help direct the actin assembly that appears to drive bacterial motility.
Keywords
Immunology and MicrobiologyBiochemistry, Genetics and Molecular Biology
The Journal of Cell BiologyActin filaments and the growth, movement, and spread of the intracellular bacterial parasite, Listeria monocytogenes.
1,265 Citations1989L G Tilney, Daniel A. Portnoy
Once inside a host cell, the infecting Listeria and their progeny can spread from cell to cell by remaining intracellular and thus bypass the humoral immune system of the organism.
CellL. monocytogenes-induced actin assembly requires the actA gene product, a surface protein
812 Citations1992Christine Kocks, Edith Gouin +4 more
Analyzing an avirulent Tn917-lac mutant defective for actin polymerization showed that the actA gene encodes a surface protein necessary for bacterially induced actin assembly, and results indicate that it is a 610 amino acid protein with an apparent molecular weight of 90 kd.
Proceedings of the National Academy of SciencesIdentification of icsA, a plasmid locus of Shigella flexneri that governs bacterial intra- and intercellular spread through interaction with F-actin.
727 Citations1989Maria Lina Bernardini, Joëlle Mounier +3 more
IicsA, a locus necessary for intra- and intercellular spread, was identified on the Shigella flexneri virulence plasmid pWR100 and shown to express a 120-kDa outer membrane protein, which plays an important role in the interactions established between host cell microfilaments and the bacterial surface, thus leading to intracellular movement.
NatureThe rate of actin-based motility of intracellular Listeria monocytogenes equals the rate of actin polymerization
541 Citations1992Julie A. Theriot, Timothy J. Mitchison +2 more
The results imply that the motile mechanism involves continuous polymerization and release of actin filaments at the bacterial surface and that the rate of filament generation is related to the rates of movement.
The EMBO JournalThe proline‐rich focal adhesion and microfilament protein VASP is a ligand for profilins.
480 Citations1995Matthias Reinhard, Klaudia Giehl +6 more
The data support the hypothesis that profilin and VASP act in concert to convey signal transduction to actin filament formation and suggest that both proteins also interact within living cells.
The EMBO JournalA novel bacterial virulence gene in Listeria monocytogenes required for host cell microfilament interaction with homology to the proline‐rich region of vinculin.
410 Citations1992Eugen Domann, J Wehland +7 more
Within the cytoplasm of the infected cells, the mutant strain grew as microcolonies, was unable to accumulate actin following escape from the phagocytic compartment and was incapable of infecting adjacent cells, demonstrating that the capacity to move intracellularly and spread intercellularly is a key determinant of L.monocytogenes virulence.
The EMBO JournalThe 46/50 kDa phosphoprotein VASP purified from human platelets is a novel protein associated with actin filaments and focal contacts.
378 Citations1992Matthias Reinhard, Maria Halbrügge +4 more
The data demonstrate that VASP is a novel phosphoprotein associated with actin filaments and focal contact areas, i.e. transmembrane junctions between microfilaments and the extracellular matrix.
Proceedings of the National Academy of SciencesListeria monocytogenes moves rapidly through the host-cell cytoplasm by inducing directional actin assembly.
321 Citations1990Guissou A. Dabiri, J M Sanger +2 more
Listeria monocytogenes can dramatically stimulate host-cell actin assembly in a directional manner, which serves to rapidly propel the bacteria through the cytoplasm, allowing the organisms to move to peripheral membranes and spread to uninfected cells.
BiochemistryQuantitative analysis of the effect of Acanthamoeba profilin on actin filament nucleation and elongation
316 Citations1984Thomas D. Pollard, John A. Cooper
A new and more complex model for the mechanism of action that is related to a proposal of Tilney and co-workers is proposed, which includes two different Kd's--one for profilin bound to actin monomers and one for profils bound to an actin molecule at the barbed end of a filament.
Journal of BacteriologyUnipolar localization and ATPase activity of IcsA, a Shigella flexneri protein involved in intracellular movement
301 Citations1993Marcia B. Goldberg, Octavian Bârzu +2 more
It is demonstrated here that in vitro IcsA is secreted into the culture supernatant in a cleaved form and interacts with elements within the tail of shigella flexneri.
CellInvolvement of profilin in the actin-based motility of L. monocytogenes in cells and in cell-free extracts
284 Citations1994Julie A. Theriot, Jody Rosenblatt +3 more
A cell-free extract system capable of faithfully reconstituting L. monocytogenes motility is devised, and it is demonstrated that profilin, a host actin monomer-binding protein, is necessary for bacterial actin-based motility.
The EMBO JournalA focal adhesion factor directly linking intracellularly motile Listeria monocytogenes and Listeria ivanovii to the actin‐based cytoskeleton of mammalian cells.
269 Citations1995Trinad Chakraborty, Frank Ebel +8 more
Following Listeria infection the host vasodilator‐stimulated phosphoprotein (VASP), a microfilament‐ and focal adhesion‐associated substrate of both the cAMP‐ and cGMP‐dependent protein kinases, accumulates on the surface of intracytoplasmic bacteria prior to the detection of F‐actin ‘clouds’.
Proceedings of the National Academy of SciencesExpression and phosphorylation of the Listeria monocytogenes ActA protein in mammalian cells.
261 Citations1993Rodney A. Brundage, Gregory A. Smith +3 more
Data indicate that ActA is phosphorylated during intracellular growth, and it is speculated that it may modulate the intrACEllular activity of ActA.
The EMBO JournalMolecular cloning, structural analysis and functional expression of the proline‐rich focal adhesion and microfilament‐associated protein VASP.
208 Citations1995Christof Haffner, Thomas Jarchau +4 more
The results provide evidence for the structural basis by which VASP, both a target of the cAMP and cGMP signal transduction pathways and a component of the actin‐based cytoskeleton, including the cytos skeleton‐membrane interface, may be able to exchange signals between these networks.
Journal of Cell SciencePolarized distribution of <i>Listeria monocytogenes</i> surface protein ActA at the site of directional actin assembly
196 Citations1993Christine Kocks, Raymond Hellio +3 more
This work has used immunocytochemistry to show that the actA gene product, ActA, is distributed asymmetrically on the bacterial surface: it is not expressed at one pole and is increasingly concentrated towards the other.
The EMBO JournalThe ActA protein of Listeria monocytogenes acts as a nucleator inducing reorganization of the actin cytoskeleton.
196 Citations1994Susanne Pistor, Trinad Chakraborty +3 more
The results identify the ActA polypeptide as a nucleator of the actin cytoskeleton and provide the first insights into the molecular nature of such controlling elements in microfilament organization.
Infection and ImmunityHost cell actin assembly is necessary and likely to provide the propulsive force for intracellular movement of Listeria monocytogenes
164 Citations1992J M Sanger, Joseph W. Sanger +1 more
The results indicate that host cell actin polymerization is necessary for intracellular migration of listeriae and suggest that directional actin assembly may in fact generate the propulsive force for bacterial and filopodial movement.
Current BiologyThe bacterial actin nucleator protein ActA of Listeria monocytogenes contains multiple binding sites for host microfilament proteins
142 Citations1995Susanne Pistor, Trinad Chakraborty +2 more
The studies reveal the initial interactions that take place between invading Listeria and host microfilament proteins and suggest that host cell analogues of ActA exist and are important components of structures involved in cell motility.
Molecular MicrobiologyAsymmetric distribution of the <i>Listeria monocytogenes</i> ActA protein is required and sufficient to direct actin‐based motility
130 Citations1995Gregory A. Smith, Daniel A. Portnoy +1 more
It is demonstrated that the ActA protein is sufficient to direct motility in the absence of other L. monocytogenes gene products, and that polarized localization of the protein is required for efficient unidirectional movement.
The Journal of Cell BiologyHow Listeria exploits host cell actin to form its own cytoskeleton. I. Formation of a tail and how that tail might be involved in movement.
120 Citations1992L G Tilney, David J. DeRosier +1 more
It is shown how a cloud of actin filaments becomes rearranged into a tail simply by the mechanics of growth, and how 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.
BiochemistryInteraction of Profilin with G-Actin and Poly(L-Proline)
115 Citations1994Irina Perelroizen, Jean‐Baptiste Marchand +3 more
The interaction of bovine spleen profilin with ATP- and ADP-G-actin and poly(L-proline) has been studied by spectrofluorimetry, analytical ultracentrifugation, and rapid kinetics in low ionic strength buffer.
Current Opinion in Cell BiologyActin-based bacterial motility
109 Citations1995Pascale Cossart
A cell-free system that reconstitutes faithfully the actin-based motility of L. monocytogenes promises to be instrumental in the further dissection of this fascinating phenomenon.
The Journal of Cell BiologyHow Listeria exploits host cell actin to form its own cytoskeleton. II. Nucleation, actin filament polarity, filament assembly, and evidence for a pointed end capper.
107 Citations1992L G Tilney, David J. DeRosier +2 more
The results of this experiment and others tell us that in vivo filament assembly must be tightly coupled to filament capping and cross-bridging so that if one process outstrips another, chaos ensues.
Infection and ImmunityLocalization of the ActA polypeptide of Listeria monocytogenes in infected tissue culture cell lines: ActA is not associated with actin "comets"
89 Citations1993Kirsten Niebuhr, Trinad Chakraborty +5 more
The ActA polypeptide appears to be required in the initiation of actin accumulation by the bacterium and is apparently not directly involved in the generation of the actin "tail" of individual bacteria.
Trends in MicrobiologyThe wily ways of a parasite: induction of actin assembly by Listeria
85 Citations1993Lewis G. Tilney, M S Tilney
The antics of Listeria and some of the bacterial genes instrumental in maintaining it in the host are discussed.
Cell Motility and the CytoskeletonIntact alpha‐actinin molecules are needed for both the assembly of actin into the tails and the locomotion of <i>Listeria monocytogenes</i> inside infected cells
69 Citations1994Frederick G. Dold, Jean M. Sanger +3 more
Results indicate that intact alpha-actinin molecules play an important role in the intracellular motility of Listeria, presumably by stabilizing the actin fibers in the stationary tails that are required for the bacteria to move forward.
Proceedings of the National Academy of SciencesArrest of Listeria movement in host cells by a bacterial ActA analogue: implications for actin-based motility.
54 Citations1994Frederick S. Southwick, D L Purich
The findings demonstrate the efficacy of low molecular weight peptides in efforts to distinguish mechanistic features in Listeria motility and PtK2 host cell membrane reorganization and suggest that a cytoskeletal component sensitive to specific oligoproline peptides may participate in protein-protein interactions essential for both of these actin-associated processes.
Journal of Cell ScienceExploitation of microfilament proteins by<i>Listeria monocytogenes</i>: microvillus-like composition of the comet tails and vectorial spreading in polarized epithelial sheets
47 Citations1994Constance J. Temm‐Grove, Brigitte M. Jockusch +4 more
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Cell Motility and the CytoskeletonOrganization and structure of actin filament bundles in <i>Listeria</i>‐infected cells
37 Citations1995Vladimir Zhukarev, F. Ashton +3 more
It is revealed that actin filaments can be deposited asymmetrically around the long axis of the bacteria, a distribution that may affect the direction of motility of Listeria monocytogenes inside infected cells.
Cell Motility and the CytoskeletonDynamics of actin and alpha‐actinin in the tails of <i>Listeria monocytogenes</i> in Infected PtK<sub>2</sub> Cells
29 Citations1994Dipali Nanavati, F. Ashton +4 more
Measurements suggest that while actin polymerization at the bacterial surface is coupled to the movement of the bacterium, the periodic changes in intracellular motility are not a simple function of the number of actin filaments nucleating at theacterial surfaces.
Cell Motility and the Cytoskeleton<i>Listeria monocytogenes</i> intracellular migration: Inhibition by profilin, vitamin D‐binding protein and DNase I
25 Citations1995Jean M. Sanger, Jean M. Sanger +4 more
It is demonstrated that Listeria-induced actin assembly in PtK2 cells is the result of assembly of actin monomers into new filaments and that Listersia's ability to recruit polymerization competent monomeric actin is very sensitive to the introduction of exogenous act in monomer-binding proteins.
Current BiologyIntracellular Motility: Profilin puts pathogens on the actin drive
12 Citations1994Christine Kocks
Intracellular motility of the bacterial pathogen Listeria monocytogenes depends on actin polymerization that is coordinated by the bacterial surface protein ActA and host actin-binding protein profilin.
