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Isolation and Chemical Characterization of Lipid A from Gram-negative Bacteria
Published on: September 17, 2013
Reactivity of murine and human recombinant LPS-binding protein (LBP) within LPS and gram negative bacteria
S Lengacher1, C V Jongeneel, D Le Roy
1Division of Infectious Diseases, CHUV, Laussane, Switzerland.
Abstract:
The serum lipopolysaccharide (LPS) binding protein, LBP, has been shown to greatly enhance cellular responses to low concentrations of LPS. Purified LBP facilitates the transfer of LPS to membrane-bound or soluble CD14; the CD14/LPS complex then triggers a signal in responsive cells. We have cloned and sequenced a cDNA encoding murine LBP, and produced recombinant murine LBP using a baculovirus expression system. Using either a solid-phase or a cytofluorometric assay, recombinant murine and human LBP were found to bind avidly to free LPS, but only weakly to live bacteria from most LPS-containing Gram negative strains. Binding correlated loosely with the length and composition of the polysaccharide O chains. However, recombinant LBP did bind well to all heat-killed bacterial preparations. These findings suggest that LBP could be implicated in the response to killed but not live Gram negative bacteria.

