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de Haas, C.J. et al.

de Haas, van der Zee, Benaissa-Trouw, van Kessel, Verhoef, van Strijp,

Lipopolysaccharide (LPS)-binding synthetic peptides derived from serum amyloid P component neutralize LPS.

Lipopolysaccharide (LPS) is the major mediator of gram-negative septic shock. Molecules that bind LPS and neutralize its toxic effects could have important clinical applications. We showed that serum amyloid P component (SAP) neutralizes LPS. A SAP-derived peptide, consisting of amino acids 27 to 39, inhibited LPS-mediated effects in the presence of human blood. In this study, we used a pepscan of overlapping 15-mer peptides and distinguished two additional LPS-binding regions within the SAP molecule, identified in the regions spanning amino acids 61 to 75 and 186 to 200. The corresponding SAP-derived peptides, pep61-75 and pep186-200, inhibited the binding of fluorescein isothiocyanate-labeled LPS to monocytes as efficiently as a bactericidal/permeability-increasing protein (BPI)-derived 15-mer peptide comprising amino acids 85 to 99. The same SAP-derived peptides very potently inhibited LPS-induced priming of phagocytes in human blood. Also, SAP-derived pep186-200 caused a prolonged survival of actinomycin D-sensitized mice treated with LPS to induce septic shock, indicating a potential use of this peptide in the defense against serious gram-negative sepsis in humans.[1]

References

Lipopolysaccharide (LPS)-binding synthetic peptides derived from serum amyloid P component neutralize LPS. de Haas, C.J., van der Zee, R., Benaissa-Trouw, B., van Kessel, K.P., Verhoef, J., van Strijp, J.A. Infect. Immun. (1999) [Pubmed]

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