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Two lipoproteins extracted from Escherichia coli K-12 LCD25 lipopolysaccharide are major components responsible for Toll-like receptor 2 mediated signaling
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The ability of endotoxin to signal through TLR2 has been controversial. This report indicates that previous evidence that it does have this ability is spurious in that the activity can be attributed to several lipoproteins that contaminate some endotoxin preparations.
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A soluble extracellular domain of TLR2 is shown to bind to insoluble, poorly characterized, commercially prepared staphylococcal peptidoglycan. This is the only report of such direct binding and warrants confirmation using chemically defined peptidoglycan preparations.
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CRP binds the phosphorylcholine on pneumococcal lipoteichoic acid, leading to inhibition of the adherence of the bacteria to the PAF receptor that is required for bacterial invasion. Surfactant, which contains abundant phosphorylcholine, competes with CBP and decreases lung defenses. This work extends our knowledge of the in vivo biological significance of adducts to lipoteichoic acids.
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Gould J., Weiser J. The inhibitory effect of C-reactive protein on bacterial phosphorylcholine platelet-activating-factor receptor-mediated adherence is blocked by surfactant. J. Infect. Dis. 186:2002;361-371 CRP binds the phosphorylcholine on pneumococcal lipoteichoic acid, leading to inhibition of the adherence of the bacteria to the PAF receptor that is required for bacterial invasion. Surfactant, which contains abundant phosphorylcholine, competes with CBP and decreases lung defenses. This work extends our knowledge of the in vivo biological significance of adducts to lipoteichoic acids.
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This report extends our recognition of the interaction of lipoteichoic acid with the PAF receptor from pneumococci to staphylococci. Signaling downstream of this interaction may activate bacterial uptake or increase metalloproteinase production, depending on the pathogen. This indicates that pathways independent of TLR2 contribute to Gram-positive disease.
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