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

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.

journal_name

Curr Opin Immunol

authors

Elsbach P,Weiss J

doi

10.1016/s0952-7915(98)80030-7

subject

Has Abstract

pub_date

1998-02-01 00:00:00

pages

45-9

issue

1

eissn

0952-7915

issn

1879-0372

pii

S0952-7915(98)80030-7

journal_volume

10

pub_type

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