Protective effects of a recombinant amino-terminal fragment of human bactericidal/permeability-increasing protein in an animal model of gram-negative sepsis.

Abstract	Bactericidal/permeability-increasing protein (BPI) has bactericidal properties and also binds lipopolysaccharide (LPS). The ability of a recombinant amino-terminal fragment of BPI to protect mice from death after challenge with a number of different strains of Escherichia coli was tested. BPI prevented death in animals challenged with the J5 rough strain but not with smooth strains O111:B4 and O7K1. Protection was associated with a reduction in serum LPS and tumor necrosis factor-alpha levels but not with reduction in blood bacterial counts. BPI was effective at protecting against death in mice injected with purified O111:B4 LPS. Lack of protection after injection with live O111:B4 and O7K1 may be due to production by these models of approximately 1000-fold higher blood bacterial count compared with J5. Thus, BPI is a promising therapy in the treatment of gram-negative septic shock, although the range of organisms against which it is effective remains to be determined.
Authors	T J Evans, A Carpenter, D Moyes, R Martin, J Cohen
Journal	The Journal of infectious diseases (J Infect Dis) Vol. 171 Issue 1 Pg. 153-60 (Jan 1995) ISSN: 0022-1899 [Print] United States
PMID	7798655 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References	Anti-Bacterial Agents Antimicrobial Cationic Peptides Blood Proteins Endotoxins Lipopolysaccharides Membrane Proteins Recombinant Proteins Tumor Necrosis Factor-alpha bactericidal permeability increasing protein Galactosamine
Topics	Animals Anti-Bacterial Agents (therapeutic use) Antimicrobial Cationic Peptides Bacteremia (drug therapy, microbiology) Blood Bactericidal Activity Blood Proteins (therapeutic use) Colony Count, Microbial Disease Models, Animal Endotoxins (blood) Escherichia coli (growth & development) Escherichia coli Infections (drug therapy) Galactosamine (pharmacology) Lipopolysaccharides (toxicity) Male Membrane Proteins Mice Recombinant Proteins (therapeutic use) Sepsis (drug therapy) Tumor Necrosis Factor-alpha (analysis)

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