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J Infect Dis. 2003 Nov 1;188(9):1382-93. Epub 2003 Oct 20.

Protective efficacy of CAP18106-138-immunoglobulin G in sepsis.

Author information

1
Department of Pediatrics and Medicine, Massachusetts General Hospital, Boston, Massachusetts 02129, USA. swarren1@partners.org.

Abstract

Naturally present antibacterial proteins play an important role in innate host defense. A synthetic peptide mimicking the C-terminal lipopolysaccharide (LPS)-binding domain of rabbit cathelicidin CAP18 was coupled to immunoglobulin (Ig) G to create CAP18(106-138)-IgG, a construct that, in concentrations equimolar to those of peptide alone, binds and neutralizes LPS and kills multiple gram-negative bacterial strains. The protective efficacy of CAP18(106-138)-IgG was evaluated in a model of cecal ligation and puncture in mice. A single intravenous administration of 20 mg/kg CAP18(106-138)-IgG protected against mortality, compared with sham-coupled IgG (P<.03). There was no protection offered by administration of equimolar peptide alone (P=.96). There was a trend toward protection in C3H/HeJ mice that are minimally sensitive to LPS (P=.06), suggesting that direct detoxification of LPS was not the only mechanism of protection. Chemical or genetic coupling of antimicrobial peptides to IgG may be a means of using these peptides to treat infections.

PMID:
14593598
DOI:
10.1086/379081
[Indexed for MEDLINE]

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