CFIDS/ME/FM are conditions of immune
suppression if not caused by the Lyme
lipoproteins, than from other such
mycoplasmal-type antigens:
http://www.jimmunol.org/cgi/content/full/164/2/554

Unfortunately the CFIDS/FM people in America
absolutely will not listen to reason.  The vast
majority of chronic Lyme patients were first
diagnosed with CFIDS or FM, but when somebody
with a brain in their heads read the "negative"
Lyme test, read that, indeed, it wasn't negative.

If you think the US medical goverment entities
give a sh.t about your health, you need to replant
your brain in the same sand hole.  No insult to
the victims intended.  These entities have to
be dragged before a federal judge and have to
account for their crimes and they will be.

"End of discussion."

Kathleen

"Introduction
Top
Abstract
Introduction
Materials and Methods
Results and Discussion
References

Mycoplasmas are wall-less bacteria that occur as commensals or
pathogens in animals and humans (1). Being wall-less, mycoplasmas lack
the classical modulins such as LPS, lipoteichoic acid (LTA),4 or murein
fragments (reviewed in Ref. 2), yet they are potent activators of
macrophages (3). A number of independent reports have identified this
macrophage-activating material as lipoproteins (4, 5, 6) or
lipopeptides (7, 8). One of these lipopeptides, the 2-kDa
macrophage-activating lipopeptide-2 (MALP-2) from Mycoplasma
fermentans, was biochemically fully characterized and has become
available by synthesis (7). The lipid moiety has an asymmetric C atom
at the 2 position. The formerly used synthetic MALP-2 was the S, R
racemate and had a similar sp. act. as the natural compound acting at
picomolar concentrations in vitro (7, 9, 10).

Little is known about the signal pathways or the cell-surface receptors
for MALP-2, except that MALP-2 activates the nuclear transcription
factor NF-{kappa}B (11, 12). A new class of receptors of the innate
immune system, the so-called Toll-like receptors (TLRs), was recently
discovered (13, 14, 15), which recognize various bacterial cell-wall
components such as LPS, peptidoglycan (PGN), LTA, and
lipoproteins/lipopeptides (16, 17, 18, 19, 20, 21, 22). Overexpression
of human TLR2 conferred responsiveness to various kinds of bacterial
components (16, 17, 19, 20, 21, 22). To investigate the in vivo roles
of the TLR family in the recognition of bacterial components, we have
generated TLR2-deficient and TLR4-deficient mice. A mutation in the
TLR4 gene is responsible for the LPS hyporesponsiveness of C3H/HeJ
mouse strain (18), and the deficiency results in lack of responsiveness
to LPS and LTA (23, 24). In contrast, TLR2-deficient mice show impaired
responsiveness to PGN, but normal responses to LPS (24). These
observations indicate different respective specificities of TLR2 and
TLR4 in the recognition of bacterial components. The TLR family, whose
cytoplasmic domain is homologous to that of IL-1R, has been shown to
interact with an adapter molecule, MyD88, for the activation of
IL-1R-associated kinase (IRAK) (25). Ultimately, NF-{kappa}B
translocates from the cytoplasm to the nucleus and activates genes with
NF-{kappa}B binding sites in their promoters. We have previously shown
that MyD88-deficient mice are unresponsive to LPS, IL-1, and IL-18 (26,
27).

To assess the role of TLR family and MyD88 in mycoplasmal lipopeptide
signaling, we analyzed MALP-2-mediated responses using two steroisomers
of MALP-2 and macrophages from TLR2-, TLR4-, and MyD88-deficient mice.
We will show that there is a stringent requirement of the correct
stereochemistry in the lipid moiety for the recognition of MALP by its
functional receptor. We will further show that this receptor is TLR2,
which transfers its signal via MyD88.

Kathleen