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PubMed · 2402637

Structure and function of lipopolysaccharide binding protein.

R R Schumann·S R Leong·G W Flaggs·P W Gray·S D Wright·J C Mathison·P S Tobias·R J Ulevitch
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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.

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Acute-Phase ProteinsAmino Acid SequenceAnimalsBase SequenceBlood ProteinsCarrier ProteinsGene LibraryHumansKineticsLipid ALipopolysaccharidesMaleMembrane GlycoproteinsMolecular Sequence DataOligonucleotide ProbesRabbitsSequence Homology, Nucleic AcidSheepStaphylococcus aureusTumor Necrosis Factor-alphaLipopolysaccharide-Binding ProteinComparative StudyJournal ArticleResearch Support, U.S. Gov't, P.H.S.

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R R Schumann, S R Leong, G W Flaggs, P W Gray, S D Wright, J C Mathison, P S Tobias, R J Ulevitch. 1990-09-21. Structure and function of lipopolysaccharide binding protein.. https://doi.org/10.1126/science.2402637

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