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*
Department of Immunology, Osaka Medical Center for Cancer and Cardiovascular Diseases, Higashinari-ku, Osaka, Japan;
Division of Environmental Pharmacology, Department of Pharmaceutical Sciences,
Institute for Protein Research, and
§
Department of Host Defense, Research Institute for Microbial Diseases, Osaka University, Osaka, Japan; and
¶
Organization for Pharmaceutical Safety and Research, Tokyo, Japan
M161Ag is a 43-kDa surface lipoprotein of Mycoplasma
fermentans, serving as a potent cytokine inducer for
monocytes/macrophages, maturing dendritic cells (DCs), and activating
host complement on affected cells. It possesses a unique N-terminal
lipo-amino acid, S-diacylglyceryl cysteine. The 2-kDa
macrophage-activating lipopeptide-2 (MALP-2), recently identified as a
ligand for Toll-like receptor 2 (TLR2), is derived from M161Ag. In this
study, we identified structural motifs sustaining the functions of
M161Ag using wild-type and unlipidated rM161Ag with (SP+)
or without signal peptides (SP-). Because the
SP+ rM161Ag formed dimers via 25Cys, we obtained a
monomeric form by mutagenesis (SP+C25S). Only wild type
accelerated maturation of human DCs as determined by the CD83/86
criteria, suggesting the importance of the N-terminal fatty acids for
this function. Wild-type and the SP+ form of monomer
induced secretion of TNF-
and IL-12 p40 by human monocytes and DCs.
Either lipid or signal peptide at the N-terminal portion of monomer was
required for expression of this function. In contrast, murine
macrophages produced TNF- in response to wild type, but not to any
recombinant form of M161Ag, suggesting the species-dependent response
to rM161Ag. Wild-type and both monomeric and dimeric SP+
forms possessed the ability to activate complement via the alternative
pathway. Again, the hydrophobic portion was associated with this
function. These results, together with the finding that macrophages
from TLR2-deficient mice did not produce TNF- in response to M161Ag,
infer that the N-terminal hydrophobic structure of M161Ag is important
for TLR2-mediated cell activation and complement
activation.
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