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

  • Curr Opin Immunol. 1998 Feb;10(1):45-9. doi: 10.1016/s0952-7915(98)80030-7.
P Elsbach  1 ,  J Weiss
Affiliations
  • 1. Department of Medicine, New York University School of Medicine, NY 10016, USA. [email protected]
PMID: 9523110 DOI: 10.1016/s0952-7915(98)80030-7
Abstract

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.

Products