Structure and Function of Lipopolysaccharide Binding Protein

Ralf R. Schumann; Steven R. Leong; Gail W. Flaggs; Patrick W. Gray; Samuel D. Wright; John C. Mathison; Peter S. Tobias; Richard J. Ulevitch

doi:10.1126/science.2402637

Abstract

The primary structure of lipopolysaccharide binding protein (LBP), a trace plasma protein that binds to the lipid A moiety of bacterial lipopolysaccharides (LPSs), was deduced by sequencing cloned complementary DNA. LBP shares sequence identity with another LPS binding protein found in granulocytes, bactericidal/permeability-increasing protein, and with cholesterol ester transport protein of the plasma. LBP may control the response to LPS under physiologic conditions by forming high-affinity complexes with LPS that bind to monocytes and macrophages, which then secrete tumor necrosis factor. The identification of this pathway for LPS-induced monocyte stimulation may aid in the development of treatments for diseases in which Gram-negative sepsis or endotoxemia are involved.

Keywords

LipopolysaccharideLipopolysaccharide binding proteinLipid ATumor necrosis factor alphaChemistryBinding proteinSecretionMonocyteSepsisStimulationDNA-binding proteinBiochemistryReceptorBiologyImmunologyCD14EndocrinologyTranscription factor

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Publication Info

Year: 1990
Type: article
Volume: 249
Issue: 4975
Pages: 1429-1431
Citations: 1672
Access: Closed

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APA Style

                            
                                
                                    Ralf R. Schumann, 
                                
                                    Steven R. Leong, 
                                
                                    Gail W. Flaggs
                                
                                et al.
                            
                            (1990). 
                            Structure and Function of Lipopolysaccharide Binding Protein. 
                            Science
                            , 249
                            (4975)
                            , 1429-1431.
                            https://doi.org/10.1126/science.2402637
                        

Identifiers

DOI: 10.1126/science.2402637