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Infection and Immunity, June 2003, p. 3280-3284, Vol. 71, No. 6
0019-9567/03/$08.00+0     DOI: 10.1128/IAI.71.6.3280-3284.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Distribution and Kinetics of Lipoprotein-Bound Lipoteichoic Acid

Johannes H. M. Levels,1* Philip R. Abraham,2 Erik P. van Barreveld,1 Joost C. M. Meijers,1 and Sander J. H. van Deventer3

Departments of Vascular Medicine,1 Experimental Internal Medicine,2 Gastroenterology, Academic Medical Center, Amsterdam, The Netherlands3

Received 20 November 2002/ Returned for modification 4 February 2003/ Accepted 10 March 2003

Lipoteichoic acid (LTA), a major cell wall component of gram-positive bacteria, is an amphipathic anionic glycolipid with structural similarities to lipopolysaccharide (LPS) from gram-negative bacteria. LTA has been implicated as one of the primary immunostimulatory components that may trigger the systemic inflammatory response syndrome. Plasma lipoproteins have been shown to sequester LPS, which results in attenuation of the host response to infection, but little is known about the LTA binding characteristics of plasma lipid particles. In this study, we have examined the LTA binding capacities and association kinetics of the major lipoprotein classes under simulated physiological conditions in human whole blood (ex vivo) by using biologically active, fluorescently labeled LTA and high-performance gel permeation chromatography. The average distribution of an LTA preparation from Staphylococcus aureus in whole blood from 10 human volunteers revealed that >95% of the LTA was associated with total plasma lipoproteins in the following proportions: high-density lipoprotein (HDL), 68% ± 10%; low-density lipoprotein (LDL), 28% ± 8%; and very low density lipoprotein (VLDL), 4% ± 5%. The saturation capacity of lipoproteins for LTA was in excess of 150 µg/ml. The LTA distribution was temperature dependent, with an optimal binding between 22 and 37°C. The binding of LTA by lipoproteins was essentially complete within 10 min and was followed by a subsequent redistribution from HDL and VLDL to LDL. We conclude that HDL has the highest binding capacity for LTA and propose that the loading and redistribution of LTA among plasma lipoproteins is a specific process that closely resembles that previously described for LPS (J. H. M. Levels, P. R. Abraham, A. van den Ende, and S. J. H. van Deventer, Infect. Immun. 68:2821-2828, 2001).

* Corresponding author. Mailing address: Academic Medical Center, Department of Vascular Medicine, Room G1-114, P.O. Box 22660, 1100 DD Amsterdam, The Netherlands. Phone: 31-20-5665899. Fax: 31-20-5669232. E-mail: h.levels{at}amc.uva.nl.

Editor: J. T. Barbieri

Infection and Immunity, June 2003, p. 3280-3284, Vol. 71, No. 6
0019-9567/03/$08.00+0     DOI: 10.1128/IAI.71.6.3280-3284.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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