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.


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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Animals
  • Anti-Bacterial Agents / chemistry
  • Anti-Bacterial Agents / classification
  • Anti-Bacterial Agents / immunology*
  • Antimicrobial Cationic Peptides
  • Blood Proteins / chemistry
  • Blood Proteins / classification
  • Blood Proteins / immunology*
  • Body Fluids / immunology
  • Crystallography, X-Ray
  • Humans
  • Inflammation
  • Lipopolysaccharides / immunology
  • Membrane Proteins*
  • Phagocytosis
  • Structure-Activity Relationship


  • Anti-Bacterial Agents
  • Antimicrobial Cationic Peptides
  • Blood Proteins
  • Lipopolysaccharides
  • Membrane Proteins
  • bactericidal permeability increasing protein