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LBP (Lipopolysaccharide binding protein) is a 58-kD acute phase glycoprotein, binds to the lipid A portion of Lipopolysaccharide (LPS) with high affinity and catalyzed the CD14 and TLR4 dependent cellular activation by LPS. LBP interacted with CD14, TLR2, TLR4 und the co-receptor MD-2. LBP is involved in the acute-phase immunologic response to gram-negative bacterial infections. Gram-negative bacteria contain LPS on their outer cell wall. Together with bactericidal permeability-increasing protein (BPI), LBP binds LPS and interacts with the CD14 receptor, probably playing a role in regulating LPS-dependent monocyte responses. Earlier studies suggest that LBP is necessary for the rapid acute-phase response to LPS but not for the clearance of LPS from circulation. LBP is part of a family of structurally and functionally related proteins, including BPI, plasma cholesteryl ester transfer protein (CETP), and phospholipid transfer protein (PLTP).




Schütt, C. et al. (1999): Implications for a general role of LPS binding proteins (CD14, LBP) in combating bacterial intections. J. Endotoxin Research 5, 75-80


Schütt, C.; Witt, S.; Grunwald, U.; Stelter, F.; Schilling, T.; Fan, X.; Marquart, B.; Bassarab, P.; Krüger, C. (1995): Epitope mapping of CD14 glycoprotein in Leukocyte typing V, ( L. Bournsell, W. Gilks, J. M. Harlan, T. Kishimoto, C. Morimoto, J. Ritz, S. F. Schossmanns, S. Shaw, R. Silverstein, T. Springer, T. F. Tedder, R. F. Todd, eds), Oxford University Press, Oxford, 785-788


Stelter, F.; Bernheiden, M.; Menzel, R.; Jack, R. S.; Witt, S.; Fan, X.; Pfister, M.; Schütt, C. (1997): Mutation of amino acids 39-44 of human CD14 abrogates binding of lipopolysaccharide and Escherichia coli. Eur. J. Biochem, 243, 100-109


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