Bactericidal/permeability-increasing protein (BPI) and lipopolysaccharide-binding protein (LBP): structure, function and regulation in host defence against Gram-negative bacteria

Biochem Soc Trans. 2003 Aug;31(Pt 4):785-90. doi: 10.1042/bst0310785.

Abstract

Lipopolysaccharide-binding protein (LBP) and bactericidal/permeability-increasing protein (BPI) are closely related endotoxin-binding proteins that function in a co-ordinated manner to facilitate an integrated host response to invading Gram-negative bacteria. Differences in the structure and function of BPI and LBP, as well as differences in their mobilization, permit highly sensitive pro-inflammatory responses to small numbers of bacteria at the onset of bacterial invasion and, later, efficient elimination of viable bacteria and their remnants and of endotoxin-driven inflammation.

Publication types

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

MeSH terms

  • Acute-Phase Proteins*
  • Animals
  • Antimicrobial Cationic Peptides
  • Blood Proteins / chemistry
  • Blood Proteins / immunology*
  • Carrier Proteins / chemistry
  • Carrier Proteins / immunology*
  • Endotoxins / antagonists & inhibitors
  • Endotoxins / immunology
  • Endotoxins / metabolism
  • Gram-Negative Bacterial Infections / immunology*
  • Inflammation / immunology
  • Membrane Glycoproteins*
  • Membrane Proteins*
  • Models, Molecular
  • Structure-Activity Relationship

Substances

  • Acute-Phase Proteins
  • Antimicrobial Cationic Peptides
  • Blood Proteins
  • Carrier Proteins
  • Endotoxins
  • Membrane Glycoproteins
  • Membrane Proteins
  • bactericidal permeability increasing protein
  • lipopolysaccharide-binding protein