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*
Department of Oral Bacteriology, Hokkaido University School of Dentistry, Sapporo, Japan; and
Department of Bio-material Chemistry, Graduate School of Environmental Earth Science, Hokkaido University, Sapporo, Japan
The activities to induce TNF-
production by a monocytic cell
line, THP-1, and ICAM-1 expression and IL-6 production by human
gingival fibroblasts were detected in plural membrane lipoproteins of
Mycoplasma salivarium. Although SDS-PAGE of the
lipoproteins digested by proteinase K did not reveal any protein bands
with molecular masses higher than approximately10 kDa, these activities
were detected in the front of the gel. A lipoprotein with a molecular
mass of 44 kDa (Lp44) was purified. Proteinase K did not affect the
ICAM-1 expression-inducing activity of Lp44, but lipoprotein lipase
abrogated the activity. These results suggested that the proteinase
K-resistant and low molecular mass entity, possibly the N-terminal
lipid moiety, played a key role in the expression of the activity. The
N-terminal lipid moiety of Lp44 was purified from Lp44 digested with
proteinase K by HPLC. Judging from the structure of microbial
lipopeptides as well as the amino acid sequence and
infrared spectrum of Lp44, the structure of the N-terminal lipid moiety
of Lp44 was speculated to be S-(2,
3-bisacyloxypropyl)-cysteine-GDPKHPKSFTEWV-. Its analogue,
S-(2, 3-bispalmitoyloxypropyl)-cysteine-GDPKHPKSF, was
synthesized. The lipopeptide was similar to the N-terminal lipid moiety
of Lp44 in the infrared spectrum and the ICAM-1 expression-inducing
activity. Thus, this study suggested that the active entity of Lp44 was
its N-terminal lipopeptide moiety, the structure of which was very
similar to S-(2,
3-bispalmitoyloxypropyl)-cysteine-GDPKHPKSF.
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