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Infection and Immunity, May 2001, p. 2821-2828, Vol. 69, No. 5
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.5.2821-2828.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Distribution and Kinetics of Lipoprotein-Bound Endotoxin

J. H. M. Levels,1,* P. R. Abraham,2 A. van den Ende,1 and S. J. H. van Deventer2

Department of Vascular Medicine1 and Department of Experimental Internal Medicine,2 Academic Medical Center, Amsterdam, The Netherlands

Received 3 October 2000/Returned for modification 21 December 2000/Accepted 29 January 2001

Lipopolysaccharide (LPS), the major glycolipid component of gram-negative bacterial outer membranes, is a potent endotoxin responsible for pathophysiological symptoms characteristic of infection. The observation that the majority of LPS is found in association with plasma lipoproteins has prompted the suggestion that sequestering of LPS by lipid particles may form an integral part of a humoral detoxification mechanism. Previous studies on the biological properties of isolated lipoproteins used differential ultracentrifugation to separate the major subclasses. To preserve the integrity of the lipoproteins, we have analyzed the LPS distribution, specificity, binding capacity, and kinetics of binding to lipoproteins in human whole blood or plasma by using high-performance gel permeation chromatography and fluorescent LPS of three different chemotypes. The average distribution of O111:B4, J5, or Re595 LPS in whole blood from 10 human volunteers was 60% (±8%) high-density lipoprotein (HDL), 25% (±7%) low-density lipoprotein, and 12% (±5%) very low density lipoprotein. The saturation capacity of lipoproteins for all three LPS chemotypes was in excess of 200 µg/ml. Kinetic analysis however, revealed a strict chemotype dependence. The binding of Re595 or J5 LPS was essentially complete within 10 min, and subsequent redistribution among the lipoprotein subclasses occurred to attain similar distributions as O111:B4 LPS at 40 min. We conclude that under simulated physiological conditions, the binding of LPS to lipoproteins is highly specific, HDL has the highest binding capacity for LPS, the saturation capacity of lipoproteins for endotoxin far exceeds the LPS concentrations measured in clinical situations, and the kinetics of LPS association with lipoproteins display chemotype-dependent differences.

* Corresponding author. Mailing address: Academic Medical Center, Department of Vascular Medicine, P.O. Box 22660, 1100 DD Amsterdam, The Netherlands. Phone: 31-20-5663895. Fax: 31-20-5669232. E-mail: h.levels{at}amc.uva.nl.

Infection and Immunity, May 2001, p. 2821-2828, Vol. 69, No. 5
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.5.2821-2828.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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