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

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.

• Authors: J Weiss
• Journal: Biochemical Society transactions (Biochem Soc Trans) Vol. 31 Issue Pt 4 Pg. 785-90 (Aug 2003) ISSN: 0300-5127 [Print] England
• PMID: 12887306 (Publication Type: Comparative Study, Journal Article, Research Support, U.S. Gov't, P.H.S., Review)

Chemical References

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

Topics

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