Reactivity of Murine and Human Recombinant LPS-binding Protein (LBP) with IPS and Gram Negative Bacteria

S. Lengacher, C. V. Jongeneel, D. Le Roy, J. D. Lee, V. Kravchenko, R. J. Ulevitch, M. P. Glauser, D. Neumann

Research output: Contribution to journalArticlepeer-review

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 membranebound 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.

Original languageEnglish (US)
Pages (from-to)165-172
Number of pages8
JournalJournal of inflammation
Volume47
Issue number4
StatePublished - Dec 1 1995

ASJC Scopus subject areas

  • Cardiology and Cardiovascular Medicine

Fingerprint Dive into the research topics of 'Reactivity of Murine and Human Recombinant LPS-binding Protein (LBP) with IPS and Gram Negative Bacteria'. Together they form a unique fingerprint.

Cite this