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J Biol Chem, Vol. 273, Issue 51, 34391-34398, December 18, 1998
From the § Institut Pasteur, Laboratoire des
Mycoplasmes, 25 Rue Docteur Roux, 75724 Paris Cedex 15, France,
Mycoplasma lipoproteins have been demonstrated to
stimulate monocytic cells and induce proinflammatory cytokine
secretion. In this paper, we show that a synthetic analog of the
Mycoplasma fermentans membrane-associated lipopeptide
macrophage-activating lipopeptide-2 (MALP-2) induces mRNA synthesis
and protein secretion of interleukin-1
A Mycoplasma fermentans-derived Synthetic Lipopeptide
Induces AP-1 and NF-
B Activity and Cytokine Secretion in Macrophages
via the Activation of Mitogen-activated Protein Kinase Pathways
, Université Paris VII, UFR de Biochimie, 2 place
Jussieu, 75251 Paris Cedex 05, France, and
¶ Hoechst-Marion-Roussel, Centre de Recherche Romainville, 111 Route de Noisy, 93230 Romainville, France
and tumor necrosis factor-
in human monocytes/macrophages and the murine macrophage cell line RAW
264.7, whereas the nonlipidated counterpart lacks this effect,
underscoring the importance of protein acylation for cell activation.
Synthetic MALP-2 (sMALP-2) induced the activation of MAPK family
members extracellular signal regulated kinases 1 and 2, c-Jun
NH2-terminal kinase, and p38 and induced NF-
B and AP-1
transactivation in macrophages. Whereas the specific p38 inhibitor
SB203580 abrogated both cytokine synthesis and NF-B and AP-1
transactivation in response to MALP-2, the selective MAPK/extracellular
signal-regulated kinase-1 inhibitor PD-98059 decreased interleukin-1
and tumor necrosis factor- production in response to sMALP-2 without
affecting the transactivation of NF-B or AP-1. These results
indicate that activation of MAPKs by sMALP-2 is a crucial event leading
to the expression of proinflammatory cytokines. Our findings
demonstrate that the synthetic analog of MALP-2 reproduces the
macrophage stimulation activity found in different fractions of
mycoplasmas. Given that MALP-2 has been recently shown to be expressed
at the surface of M. fermentans as a molecular entity,
sMALP-2 constitutes a valuable surrogate for investigating
immunomodulation by these microorganisms and evaluating the role that
this activity plays in the development of inflammatory diseases
associated with mycoplasma infections.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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