Role of the bactericidal/permeability-increasing protein in host defence.
Much has been learned recently about the structure and function of 55 kDa bactericidal/permeability-increasing protein (BPI), a member of a genomically conserved lipid-interactive protein family. Analysis of BPI fragments and the crystal structure of human BPI have established that BPI consists of two functionally distinct domains: a potently antibacterial and anti-endotoxin amino-terminal domain (approximately 20 kDa) and a carboxy-terminal portion that imparts opsonic activity to BPI. A recombinant amino-terminal fragment (rBPI21) protects animals against the effects of Gram-negative bacteria and endotoxin. In man, rBPI21 is nontoxic and non-immunogenic and is in Phase II/III clinical trials with apparent therapeutic benefit.
Elsbach
P
P
Department of Medicine, New York University School of Medicine, NY 10016, USA. elsbap01@mcrcr.med.nyu.edu
Weiss
J
J
D000818:Animals; D000900:Anti-Bacterial Agents / Q000737:chemistry / Q000145:classification / Q000276:immunology*; D023181:Antimicrobial Cationic Peptides; D001798:Blood Proteins / Q000737:chemistry / Q000145:classification / Q000276:immunology*; D001826:Body Fluids / Q000276:immunology; D018360:Crystallography, X-Ray; D006801:Humans; D007249:Inflammation; D008070:Lipopolysaccharides / Q000276:immunology; D008565:Membrane Proteins; D010587:Phagocytosis; D013329:Structure-Activity Relationship
D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; D001798:Blood Proteins; D008070:Lipopolysaccharides; D008565:Membrane Proteins; C021623:bactericidal permeability increasing protein