Click here to close
Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly.
We suggest using a current version of Chrome,
FireFox, or Safari.
J Bacteriol
1999 Feb 01;1813:869-78. doi: 10.1128/JB.181.3.869-878.1999.
Show Gene links
Show Anatomy links
Functional analysis of a rickettsial OmpA homology domain of Shigella flexneri icsA.
Charles M
,
Magdalena J
,
Theriot JA
,
Goldberg MB
.
???displayArticle.abstract???
Shigella flexneri is a gram-negative bacterium that causes diarrhea and dysentery by invasion and spread through the colonic epithelium. Bacteria spread by assembling actin and other cytoskeletal proteins of the host into "actin tails" at the bacterial pole; actin tail assembly provides the force required to move bacteria through the cell cytoplasm and into adjacent cells. The 120-kDa S. flexneri outer membrane protein IcsA is essential for actin assembly. IcsA is anchored in the outer membrane by a carboxy-terminal domain (the beta domain), such that the amino-terminal 706 amino acid residues (the alpha domain) are exposed on the exterior of the bacillus. The alpha domain is therefore likely to contain the domains that are important to interactions with host factors. We identify and characterize a domain of IcsA within the alpha domain that bears significant sequence similarity to two repeated domains of rickettsial OmpA, which has been implicated in rickettsial actin tail formation. Strains of S. flexneri and Escherichia coli that carry derivatives of IcsA containing deletions within this domain display loss of actin recruitment and increased accessibility to IcsA-specific antibody on the surface of intracytoplasmic bacteria. However, site-directed mutagenesis of charged residues within this domain results in actin assembly that is indistinguishable from that of the wild type, and in vitro competition of a polypeptide of this domain fused to glutathione S-transferase did not alter the motility of the wild-type construct. Taken together, our data suggest that the rickettsial homology domain of IcsA is required for the proper conformation of IcsA and that its disruption leads to loss of interactions of other IcsA domains within the amino terminus with host cytoskeletal proteins.
Allaoui,
icsB: a Shigella flexneri virulence gene necessary for the lysis of protrusions during intercellular spread.
1992, Pubmed
Allaoui,
icsB: a Shigella flexneri virulence gene necessary for the lysis of protrusions during intercellular spread.
1992,
Pubmed
Anderson,
A protective protein antigen of Rickettsia rickettsii has tandemly repeated, near-identical sequences.
1990,
Pubmed
Bass,
A systematic mutational analysis of hormone-binding determinants in the human growth hormone receptor.
1991,
Pubmed
Bernardini,
Identification of icsA, a plasmid locus of Shigella flexneri that governs bacterial intra- and intercellular spread through interaction with F-actin.
1989,
Pubmed
Chakraborty,
A focal adhesion factor directly linking intracellularly motile Listeria monocytogenes and Listeria ivanovii to the actin-based cytoskeleton of mammalian cells.
1995,
Pubmed
Clerc,
Entry of Shigella flexneri into HeLa cells: evidence for directed phagocytosis involving actin polymerization and myosin accumulation.
1987,
Pubmed
Cudmore,
Actin-based motility of vaccinia virus.
1995,
Pubmed
Dabiri,
Listeria monocytogenes moves rapidly through the host-cell cytoplasm by inducing directional actin assembly.
1990,
Pubmed
d'Hauteville,
Phosphorylation of IcsA by cAMP-dependent protein kinase and its effect on intracellular spread of Shigella flexneri.
1992,
Pubmed
d'Hauteville,
Lack of cleavage of IcsA in Shigella flexneri causes aberrant movement and allows demonstration of a cross-reactive eukaryotic protein.
1996,
Pubmed
Domann,
A novel bacterial virulence gene in Listeria monocytogenes required for host cell microfilament interaction with homology to the proline-rich region of vinculin.
1992,
Pubmed
Egile,
SopA, the outer membrane protease responsible for polar localization of IcsA in Shigella flexneri.
1997,
Pubmed
Fukuda,
Cleavage of Shigella surface protein VirG occurs at a specific site, but the secretion is not essential for intracellular spreading.
1995,
Pubmed
Gilmore,
Comparison of the rompA gene repeat regions of Rickettsiae reveals species-specific arrangements of individual repeating units.
1993,
Pubmed
Gilmore,
DNA polymorphism in the conserved 190 kDa antigen gene repeat region among spotted fever group Rickettsiae.
1991,
Pubmed
Goldberg,
Shigella flexneri surface protein IcsA is sufficient to direct actin-based motility.
1995,
Pubmed
,
Xenbase
Goldberg,
Shigella actin-based motility in the absence of vinculin.
1997,
Pubmed
Goldberg,
Unipolar localization and ATPase activity of IcsA, a Shigella flexneri protein involved in intracellular movement.
1993,
Pubmed
Hackstadt,
The biology of rickettsiae.
1996,
Pubmed
Heinzen,
Directional actin polymerization associated with spotted fever group Rickettsia infection of Vero cells.
1993,
Pubmed
High,
IpaB of Shigella flexneri causes entry into epithelial cells and escape from the phagocytic vacuole.
1992,
Pubmed
Hovde,
Evidence that glutamic acid 167 is an active-site residue of Shiga-like toxin I.
1988,
Pubmed
Kadurugamuwa,
Intercellular spread of Shigella flexneri through a monolayer mediated by membranous protrusions and associated with reorganization of the cytoskeletal protein vinculin.
1991,
Pubmed
Kang,
Profilin interacts with the Gly-Pro-Pro-Pro-Pro-Pro sequences of vasodilator-stimulated phosphoprotein (VASP): implications for actin-based Listeria motility.
1997,
Pubmed
Kocks,
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.
1995,
Pubmed
,
Xenbase
Kocks,
L. monocytogenes-induced actin assembly requires the actA gene product, a surface protein.
1992,
Pubmed
Labrec,
EPITHELIAL CELL PENETRATION AS AN ESSENTIAL STEP IN THE PATHOGENESIS OF BACILLARY DYSENTERY.
1964,
Pubmed
Lasa,
The amino-terminal part of ActA is critical for the actin-based motility of Listeria monocytogenes; the central proline-rich region acts as a stimulator.
1995,
Pubmed
,
Xenbase
Lasa,
Identification of two regions in the N-terminal domain of ActA involved in the actin comet tail formation by Listeria monocytogenes.
1997,
Pubmed
,
Xenbase
Lett,
virG, a plasmid-coded virulence gene of Shigella flexneri: identification of the virG protein and determination of the complete coding sequence.
1989,
Pubmed
Meissner,
Bacteriophage lambda cloning system for the construction of directional cDNA libraries.
1987,
Pubmed
Mounier,
Intracellular and cell-to-cell spread of Listeria monocytogenes involves interaction with F-actin in the enterocytelike cell line Caco-2.
1990,
Pubmed
Niebuhr,
A novel proline-rich motif present in ActA of Listeria monocytogenes and cytoskeletal proteins is the ligand for the EVH1 domain, a protein module present in the Ena/VASP family.
1997,
Pubmed
Oaks,
Plaque formation by virulent Shigella flexneri.
1985,
Pubmed
Pál,
Intracellular spread of Shigella flexneri associated with the kcpA locus and a 140-kilodalton protein.
1989,
Pubmed
Pistor,
The bacterial actin nucleator protein ActA of Listeria monocytogenes contains multiple binding sites for host microfilament proteins.
1995,
Pubmed
Prévost,
Unipolar reorganization of F-actin layer at bacterial division and bundling of actin filaments by plastin correlate with movement of Shigella flexneri within HeLa cells.
1992,
Pubmed
Sansonetti,
Cadherin expression is required for the spread of Shigella flexneri between epithelial cells.
1994,
Pubmed
Sansonetti,
Involvement of a plasmid in the invasive ability of Shigella flexneri.
1982,
Pubmed
Sansonetti,
Multiplication of Shigella flexneri within HeLa cells: lysis of the phagocytic vacuole and plasmid-mediated contact hemolysis.
1986,
Pubmed
Shere,
Disruption of IcsP, the major Shigella protease that cleaves IcsA, accelerates actin-based motility.
1997,
Pubmed
Smith,
The tandem repeat domain in the Listeria monocytogenes ActA protein controls the rate of actin-based motility, the percentage of moving bacteria, and the localization of vasodilator-stimulated phosphoprotein and profilin.
1996,
Pubmed
Studier,
Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes.
1986,
Pubmed
Suzuki,
Functional analysis of Shigella VirG domains essential for interaction with vinculin and actin-based motility.
1996,
Pubmed
,
Xenbase
Suzuki,
Extracellular transport of VirG protein in Shigella.
1995,
Pubmed
Theriot,
The rate of actin-based motility of intracellular Listeria monocytogenes equals the rate of actin polymerization.
1992,
Pubmed
Tilney,
Actin filaments and the growth, movement, and spread of the intracellular bacterial parasite, Listeria monocytogenes.
1989,
Pubmed
Welch,
Interaction of human Arp2/3 complex and the Listeria monocytogenes ActA protein in actin filament nucleation.
1998,
Pubmed
Welch,
Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes.
1997,
Pubmed
,
Xenbase
Wertman,
Systematic mutational analysis of the yeast ACT1 gene.
1992,
Pubmed
