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Immunity. 2003 Aug;19(2):269-79.

Recognition of pneumococcal peptidoglycan: an expanded, pivotal role for LPS binding protein.

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Department of Neurology, Universitaetsklinikum Charité, Humboldt University, 10117 Berlin, Germany.


Lipopolysaccharide binding protein (LBP) has a well-established role in LPS-induced immune responses. Here, we report that LBP also plays an essential role in the innate immune response to Gram-positive pneumococci, specifically to their major inflammatory component, pneumococcal cell wall (PCW). LBP was present in the CSF of patients with meningitis, and LBP-deficient mice failed to develop meningeal inflammation. LBP enhanced PCW-induced cell signaling and TNF-alpha release. LBP bound specifically to PCW multimers, indicating novel lipid-independent binding capability for LBP. We propose the iterative anionic groups along the glycan backbone of the cell wall are a crucial structure for recognition by LBP. Such a function for LBP expands its role to Gram-positive infections.

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