Structure and function of lipopolysaccharide binding protein

Science. 1990 Sep 21;249(4975):1429-31. doi: 10.1126/science.2402637.


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.

Publication types

  • Comparative Study
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Acute-Phase Proteins*
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Blood Proteins / genetics*
  • Carrier Proteins / genetics*
  • Carrier Proteins / metabolism
  • Gene Library
  • Humans
  • Kinetics
  • Lipid A / metabolism
  • Lipopolysaccharides / metabolism*
  • Lipopolysaccharides / pharmacology
  • Male
  • Membrane Glycoproteins*
  • Molecular Sequence Data
  • Oligonucleotide Probes
  • Rabbits
  • Sequence Homology, Nucleic Acid
  • Sheep
  • Staphylococcus aureus
  • Tumor Necrosis Factor-alpha / biosynthesis


  • Acute-Phase Proteins
  • Blood Proteins
  • Carrier Proteins
  • Lipid A
  • Lipopolysaccharides
  • Membrane Glycoproteins
  • Oligonucleotide Probes
  • Tumor Necrosis Factor-alpha
  • lipopolysaccharide-binding protein

Associated data

  • GENBANK/M35533
  • GENBANK/M35534