L. monocytogenes-induced actin assembly requires the actA gene product, a surface protein

Kocks, Christine; Gouin, Edith; Tabouret, Marc; Berche, Patrick; Ohayon, Hélène; Cossart, Pascale

doi:10.1016/0092-8674(92)90188-i

Cited by 759 publications

(629 citation statements)

References 38 publications

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“…The procedures used were essentially the same as those described previously (Kocks et al, 1992). Bacterial cells were washed three times in ice-cold phosphate-buffered saline (PBS, pH 8.0) to remove any contaminating proteins.…”

Section: Biotinylation Of Cell-surface Proteinsmentioning

confidence: 99%

Structure and function of repetitive sequence elements associated with a highly polymorphic domain of the Neisseria meningitidis PilQ protein

Tønjum

Caugant²,

Dunham

et al. 1998

Molecular Microbiology

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Section: Biotinylation Of Cell-surface Proteinsmentioning

confidence: 99%

Structure and function of repetitive sequence elements associated with a highly polymorphic domain of the Neisseria meningitidis PilQ protein

Tønjum

Caugant²,

Dunham

et al. 1998

Molecular Microbiology

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“…On its C-terminal domain, ActA has a transmembrane hydrophobic tail region that retains the protein at the bacterial cytoplasmic membrane. 159,160 ActA is responsible for the polymerization of actin filaments at one pole of the bacteria, forming a structure resembling a comet tail that enables bacterial ©2 0 1 1 L a n d e s B i o s c i e n c e .…”

Section: Monocytogenesmentioning

confidence: 99%

The arsenal of virulence factors deployed byListeria monocytogenesto promote its cell infection cycle

et al. 2011

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“…monocytogenes (Bof 343) and the isogenic, nonhemolytic mutant (Bof 415), obtained from Pascale Cossart (Institute Pasteur, Paris, France), were cultured in brain heart infusion broth (32). Heat-killed cells of L. monocytogenes (hkL) were prepared by incubating the viable bacterial suspension at 70°C for 10 min.…”

Section: Bacterial Strains Cytokines and Drugsmentioning

confidence: 99%

Listeria monocytogenesModulates Macrophage Cytokine Responses Through STAT Serine Phosphorylation and the Induction of Suppressor of Cytokine Signaling 3

Stoiber

Stockinger

Steinlein

et al. 2001

The Journal of Immunology

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Macrophage activation as part of natural resistance to infection is caused by stimulation with IFN-γ and by the invading microorganisms or microbial products. Infection of macrophages with the Gram-positive bacterium Listeria monocytogenes for short periods before activation with IFN-γ increased the phosphorylation of transcription factor STAT1 at S727 and thereby the expression of IFN-γ-induced genes. By contrast, persistent infection with viable bacteria or treatment with heat-killed Listeria diminished IFN-γ-stimulated transcription and the phosphorylation of STAT1 at Y701. Decreased IFN-γ signaling correlated with the induction of suppressor of cytokine signaling 3 (SOCS3) mRNA and protein. Contrasting our previous findings with LPS, maximal synthesis of SOCS3 required both the immediate signals from Listeria receptors on the cell surface and the activity of a polypeptide secreted in response to bacterial infection. SOCS3 induction by the secreted protein could not be blocked by neutralizing Abs to IL-10 and it did not require the presence of STAT1. Consistent with the induction of SOCS3 activity, Listeria also inhibited activation of STAT5 by GM-CSF. The p38 mitogen-activated protein kinase was rapidly activated upon infection of macrophages with L. monocytogenes. Inhibition of p38 mitogen-activated protein kinase with the pyridinyl imidazol SB203580 abrogated both STAT1 S727 phosphorylation and the expression of SOCS3. The data suggest that STAT1 serine kinase and SOCS3 activity are hallmarks of immediate and delayed phases of influence by bacterial signals on signal transduction in response to IFN-γ.

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L. monocytogenes-induced actin assembly requires the actA gene product, a surface protein

Cited by 759 publications

References 38 publications

Structure and function of repetitive sequence elements associated with a highly polymorphic domain of the Neisseria meningitidis PilQ protein

Structure and function of repetitive sequence elements associated with a highly polymorphic domain of the Neisseria meningitidis PilQ protein

The arsenal of virulence factors deployed byListeria monocytogenesto promote its cell infection cycle

Listeria monocytogenesModulates Macrophage Cytokine Responses Through STAT Serine Phosphorylation and the Induction of Suppressor of Cytokine Signaling 3

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