Abstract
LPS binding protein (LBP) was discovered about 20 years ago because of its ability to bind to bacterial lipopolysaccharide (LPS). We have shown that in addition to its complex function of transferring LPS to its cellular receptor into the cell or into lipoproteins, LBP also binds to other bacterial compounds and can modulate their ability to stimulate the host's innate immune system. The majority of compounds found to also interact with LBP are amphiphilic molecules such as glycolipids or lipoproteins. Lipoteichoic acid (LTA) of different Gram-positive bacteria is recognized by LBP and both its complexation with CD14 and biological activity towards immune cells is modulated by LBP. LTA-like glycolipids isolated from spirochetes are recognized by LBP and initiate signaling in the presence of LBP. Lipopeptides corresponding to lipoproteins present in spirochetes,
