Structure and function of lipopolysaccharide binding protein.
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.
Department of Immunology, Research Institute of Scripps Clinic, La Jolla, CA 92037.
R R
RR
Schumann
S R
SR
Leong
G W
GW
Flaggs
P W
PW
Gray
S D
SD
Wright
J C
JC
Mathison
P S
PS
Tobias
R J
RJ
Ulevitch
D000209:Acute-Phase Proteins; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001798:Blood Proteins / Q000235:genetics*; D002352:Carrier Proteins / Q000235:genetics* / Q000378:metabolism; D015723:Gene Library; D006801:Humans; D007700:Kinetics; D008050:Lipid A / Q000378:metabolism; D008070:Lipopolysaccharides / Q000378:metabolism* / Q000494:pharmacology; D008297:Male; D008562:Membrane Glycoproteins; D008969:Molecular Sequence Data; D015345:Oligonucleotide Probes; D011817:Rabbits; D012689:Sequence Homology, Nucleic Acid; D012756:Sheep; D013211:Staphylococcus aureus; D014409:Tumor Necrosis Factor-alpha / Q000096:biosynthesis; D000099231:Lipopolysaccharide-Binding Protein
D000209:Acute-Phase Proteins; D001798:Blood Proteins; D002352:Carrier Proteins; D008050:Lipid A; D008070:Lipopolysaccharides; D008562:Membrane Glycoproteins; D015345:Oligonucleotide Probes; D014409:Tumor Necrosis Factor-alpha; D000099231:Lipopolysaccharide-Binding Protein