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*
Institute of Microbiology and Genetics, and
Institute of Molecular Pathology, Vienna Biocenter, Vienna, Austria; and
Department of Cellular and Molecular Oncology, Masaryk Memorial Cancer Institute, Brno, Czech Republic
Macrophage activation as part of natural resistance to infection is
caused by stimulation with IFN-
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- increased the phosphorylation of
transcription factor STAT1 at S727 and thereby the expression of
IFN--induced genes. By contrast, persistent infection with viable
bacteria or treatment with heat-killed Listeria
diminished IFN--stimulated transcription and the phosphorylation of
STAT1 at Y701. Decreased IFN- 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-.
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