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Interactions of bacterial lipopolysaccharide with microtubule proteins.

A Ding, E Sanchez, M Tancinco and C Nathan
J Immunol May 1, 1992, 148 (9) 2853-2858;
A Ding
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E Sanchez
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M Tancinco
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C Nathan
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Abstract

Bacterial LPS is a potent stimulator of immune cells, but its mechanisms are unknown. A possible role for microtubules in LPS actions has been indicated by previous findings that the microtubule-active agent, taxol, can mimic some effects of LPS in macrophages from normal strains of mice, but not from genetically LPS-hyporesponsive strains. In this report we demonstrate that isolated microtubules from mouse brain can bind LPS in vitro. LPS and tubulin coeluted through a gel filtration column, and LPS was cross-linked to microtubule proteins with an iodinatable, photoreactive agent, sulfosuccinimidyl 2-(p-azidosalicylamido) ethyl-1,3'-dithiopropionate. beta-Tubulin and microtubule-associated protein-2 (MAP), a predominant MAP in the brain, bound LPS specifically. Cross-linking was inhibited by an excess of unlabeled LPS or partially by unlabeled lipid A, but not by 2 M NaCl. Under the same conditions, neither myosin nor soybean trypsin inhibitor was labeled by the photoaffinity LPS probe, nor did these proteins compete for binding of LPS to beta-tubulin. These findings support the hypothesis that the microtubule network could be an intracellular target for LPS, and suggest further that a beta-tubulin-associated MAP could have an important role in LPS actions.

  • Copyright © 1992 by American Association of Immunologists

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The Journal of Immunology
Vol. 148, Issue 9
1 May 1992
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Interactions of bacterial lipopolysaccharide with microtubule proteins.
A Ding, E Sanchez, M Tancinco, C Nathan
The Journal of Immunology May 1, 1992, 148 (9) 2853-2858;

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Interactions of bacterial lipopolysaccharide with microtubule proteins.
A Ding, E Sanchez, M Tancinco, C Nathan
The Journal of Immunology May 1, 1992, 148 (9) 2853-2858;
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Print ISSN 0022-1767        Online ISSN 1550-6606