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Infection and Immunity, May 2000, p. 2410-2417, Vol. 68, No. 5
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Lipopolysaccharide-Binding Protein and Phospholipid Transfer Protein Release Lipopolysaccharides from Gram-Negative Bacterial Membranes

C. J. Vesy,1 R. L. Kitchens,2 G. Wolfbauer,3 J. J. Albers,3 and R. S. Munford2,4,*

Division of Digestive and Liver Disease1 and Infectious Disease Division,2 Department of Internal Medicine, and Department of Microbiology,4 UT Southwestern Medical Center, Dallas, Texas 75235-9113, and Department of Medicine and Northwest Lipid Research Laboratories, University of Washington, Seattle, Washington 98103-91033

Received 2 September 1999/Returned for modification 9 November 1999/Accepted 18 January 2000

Although animals mobilize their innate defenses against gram-negative bacteria when they sense the lipid A moiety of bacterial lipopolysaccharide (LPS), excessive responses to this conserved bacterial molecule can be harmful. Of the known ways for decreasing the stimulatory potency of LPS in blood, the binding and neutralization of LPS by plasma lipoproteins is most prominent. The mechanisms by which host lipoproteins take up the native LPS that is found in bacterial membranes are poorly understood, however, since almost all studies of host-LPS interactions have used purified LPS aggregates. Using native Salmonella enterica serovar Typhimurium outer membrane fragments (blebs) that contained 3H-labeled lipopolysaccharide (LPS) and 35S-labeled protein, we found that two human plasma proteins, LPS-binding protein (LBP) and phospholipid transfer protein (PLTP), can extract [3H]LPS from bacterial membranes and transfer it to human high-density lipoproteins (HDL). Soluble CD14 (sCD14) did not release LPS from blebs yet could facilitate LBP-mediated LPS transfer to HDL. LBP, but not PLTP, also promoted the activation of human monocytes by bleb-derived LPS. Whereas depleting or neutralizing LBP significantly reduced LPS transfer from blebs to lipoproteins in normal human serum, neutralizing serum PLTP had no demonstrable effect. Of the known lipid transfer proteins, LBP is thus most able to transfer LPS from bacterial membranes to the lipoproteins in normal human serum.

* Corresponding author. Mailing address: Department of Internal Medicine, UT Southwestern Medical Center, 5323 Harry Hines Blvd., Dallas, TX 75235-9113. Phone: (214) 648-3480. Fax: (214) 648-9478. E-mail: robert.munford{at}emailswmed.edu.

Infection and Immunity, May 2000, p. 2410-2417, Vol. 68, No. 5
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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