Bactericidal/permeability-increasing protein in host defense and its efficacy in the treatment of bacterial sepsis

Ofer Levy; Peter Elsbach

doi:10.1007/s11908-007-1007-y

Bactericidal/permeability-increasing protein in host defense and its efficacy in the treatment of bacterial sepsis

Curr Infect Dis Rep. 2007 Oct;3(5):407-12. doi: 10.1007/s11908-007-1007-y.

Authors

Ofer Levy¹, Peter Elsbach

Affiliation

¹ Division of Infectious Diseases, Children's Hospital of Boston, 300 Longwood Avenue, 02115, Boston, MA, USA, olevy@bics.bwh.harvard.edu.

PMID: 24395478
DOI: 10.1007/s11908-007-1007-y

Abstract

The 55-kD bactericidal/permeability-increasing protein (BPI) is a neutrophil-derived polypeptide belonging to a family of lipid and endotoxin binding proteins. BPI is composed of two functionally distinct structural domains: a potently antibacterial and antiendotoxin ∼ 20-kD aminoterminal half, and an opsonic carboxy-terminal portion. In multiple animal models, a recombinant amino-terminal fragment of BPI (rBPI21) is nontoxic and protects against gram-negative bacteria and endotoxin. In humans, rBPI21 is also nontoxic and nonimmunogenic and has undergone phase II/III clinical trials with apparent therapeutic benefit.