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

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      The Journal of Immunology
      The American Association of Immunologists

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          Abstract

          Toll-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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          Author and article information

          Journal
          The Journal of Immunology
          J Immunol
          The American Association of Immunologists
          0022-1767
          1550-6606
          July 15 2000
          July 15 2000
          July 15 2000
          July 15 2000
          : 165
          : 2
          : 618-622
          Article
          10.4049/jimmunol.165.2.618
          10878331
          7de71966-2ef4-4fd9-8981-b7ad08e453dc
          © 2000
          History

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