Cutting Edge: Repurification of Lipopolysaccharide Eliminates Signaling Through Both Human and Murine Toll-Like Receptor 2

Journal of Immunology - Tập 165 Số 2 - Trang 618-622 - 2000
Matthew Hirschfeld1, Ying Ma1, John H. Weis1, Stefanie N. Vogel2, Janis J. Weis1
1*Department of Pathology, University of Utah School of Medicine, Salt Lake City, UT 84132; and
2†Department of Microbiology and Immunology, Uniformed Services University of the Health Sciences, Bethesda, MD 20814

Tóm tắt

AbstractToll-like receptor (TLR) 2 has recently been associated with cellular responses to numerous microbial products, including LPS and bacterial lipoproteins. However, many preparations of LPS contain low concentrations of highly bioactive contaminants described previously as “endotoxin protein,” suggesting that these contaminants could be responsible for the TLR2-mediated signaling observed upon LPS stimulation. To test this hypothesis, commercial preparations of LPS were subjected to a modified phenol re-extraction protocol to eliminate endotoxin protein. While it did not influence the ability to stimulate cells from wild-type mice, repurification eliminated the ability of LPS to activate cells from C3H/HeJ (Lpsd) mice. Additionally, only cell lines transfected with human TLR4, but not human or murine TLR2, acquired responsiveness to both re-extracted LPS and to a protein-free, synthetic preparation of lipid A. These results suggest that neither human nor murine TLR2 plays a role in LPS signaling in the absence of contaminating endotoxin protein.

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Journal of Immunology

Tập 165 Số 2

618-622

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