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Infection and Immunity, December 2003, p. 6799-6807, Vol. 71, No. 12
0019-9567/03/$08.00+0     DOI: 10.1128/IAI.71.12.6799-6807.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Porphyromonas gingivalis Lipopolysaccharide Antagonizes Escherichia coli Lipopolysaccharide at Toll-Like Receptor 4 in Human Endothelial Cells

Stephen R. Coats,* Robert A. Reife, Brian W. Bainbridge, Thu-Thao T. Pham, and Richard P. Darveau

Department of Periodontics, University of Washington, Seattle, Washington 98195

Received 30 June 2003/ Returned for modification 21 August 2003/ Accepted 18 September 2003

E. coli lipopolysaccharide (LPS) induces cytokine and adhesion molecule expression via the toll-like receptor 4 (TLR4) signaling complex in human endothelial cells. In the present study, we investigated the mechanism by which Porphyromonas gingivalis LPS antagonizes E. coli LPS-dependent activation of human endothelial cells. P. gingivalis LPS at 1 µg/ml inhibited both E. coli LPS (10 ng/ml) and Mycobacterium tuberculosis heat shock protein (HSP) 60.1 (10 µg/ml) stimulation of E-selectin mRNA expression in human umbilical vein endothelial cells (HUVEC) without inhibiting interleukin-1 beta (IL-1ß) stimulation. P. gingivalis LPS (1 µg/ml) also blocked both E. coli LPS-dependent and M. tuberculosis HSP60.1-dependent but not IL-1ß-dependent activation of NF-{kappa}B in human microvascular endothelial (HMEC-1) cells, consistent with antagonism occurring upstream from the TLR/IL-1 receptor adaptor protein, MyD88. Surprisingly, P. gingivalis LPS weakly but significantly activated NF-{kappa}B in HMEC-1 cells in the absence of E. coli LPS, and the P. gingivalis LPS-dependent agonism was blocked by transient expression of a dominant negative murine TLR4. Pretreatment of HUVECs with P. gingivalis LPS did not influence the ability of E. coli LPS to stimulate E-selectin mRNA expression. Taken together, these data provide the first evidence that P. gingivalis LPS-dependent antagonism of E. coli LPS in human endothelial cells likely involves the ability of P. gingivalis LPS to directly compete with E. coli LPS at the TLR4 signaling complex.

* Corresponding author. Mailing address: Department of Periodontics, University of Washington, Health Sciences Center, Box 357444. Seattle, WA 98195. Phone: (206) 543-5043. Fax: (206) 616-7478. E-mail address: scoats@u.washington.edu.

Editor: W. A. Petri, Jr.

Infection and Immunity, December 2003, p. 6799-6807, Vol. 71, No. 12
0019-9567/03/$08.00+0     DOI: 10.1128/IAI.71.12.6799-6807.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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