Triacylated lipoproteins derived from Mycoplasma pneumoniae activate nuclear factor-kappaB through toll-like receptors 1 and 2

Takashi Shimizu, Yutaka Kida, Koichi Kuwano
Immunology 2007, 121 (4): 473-83
Pathogenesis of Mycoplasma pneumoniae infection is considered to be in part attributed to excessive immune responses. Recently, a mycoplasma lipoprotein has been shown to induce nuclear factor kappaB (NF-kappaB) activation through toll-like receptor 1 (TLR1), TLR2 and TLR6. In this study, we examined the ability of lipoproteins from M. pneumoniae to activate NF-kappaB through TLR1- and TLR2-dependent, but TLR6-independent, pathways, and the active components responsible for the NF-kappaB activation through the TLR6-independent pathway were identified. The active lipoproteins were found to be MPN611 and MPN162 of M. pneumoniae (designated N-ALP1 and N-ALP2, respectively). Purified N-ALP1 and N-ALP2 from M. pneumoniae and triacylated partial synthetic lipopeptides of N-ALP1 and N-ALP2 augmented the levels of NF-kappaB induction through TLR1- and TLR2-dependent pathways, whereas diacylated partial synthetic lipopeptides of N-ALP1 and N-ALP2 activated NF-kappaB through TLR1-, TLR2- and TLR6-dependent pathways. These data suggest that N-ALP1 and N-ALP2 would be triacylated lipoproteins. The activity of N-ALP1 and N-ALP2 was decreased with a pretreatment of lipoprotein lipase, and partially decreased by protease treatment, indicating that the lipid moiety of N-ALP1 and N-ALP2 is critical for the NF-kappaB activation. Thus, triacylated lipoproteins derived from M. pneumoniae might activate NF-kappaB through TLR1 and TLR2, but not TLR6.

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