Role of the bactericidal/permeability-increasing protein in host defence

✍ Scribed by Peter Elsbach; Jerrold Weiss

• Publisher: Elsevier Science
• Year: 1998
• Tongue: English
• Weight: 545 KB
• Volume: 10
• Category: Article
• ISSN: 0952-7915
• DOI: 10.1016/s0952-7915(98)80030-7

✦ Synopsis

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.