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Bogard Jr., W.C., Siegel, S.A., Leone, A.O., Damiano, E., Sheal, D.J., Ely, T.M., Frederick, B., Mascelli, M.A., Siegel, R.C., Machiels, N.D., Kapian, P.M. and Daddona, P.E. (1993) Human monoclonal antibody HA-1A binds to endotoxin via an epitope in the lipid A domain of lipopolysaccharide. Journal of Immunology, 150, 4438-4449.

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• TITLE: Inhibition of Lon protease by bacterial lipopolisaccharide (LPS) though inhibition of ATPase

  AUTHORS: Nahoko Sugiyama, Noriko Minami, Yoshiyuki Ishii, Fumio Amano

  KEYWORDS: ATPase; Lipid A; Lipopolysaccharide (LPS); Lon; Protease

  JOURNAL NAME: Advances in Bioscience and Biotechnology, Vol.4 No.4, April 30, 2013

  ABSTRACT: Lon protease, an ATP-dependent protease in Escherichia coli, degrades abnormal proteins and regulates several important cellular functions. Here we show novel inhibitory effects of lipopolysaccharide (LPS) on Lon protease activities. LPS inhibited the peptidase, protease, and ATPase activities of Lon; and a dose-response study showed that LPS at low doses more effectively inhibited the ATPase activity than the peptidase one, suggesting different susceptibility to LPS of these activities associated with Lon. Structure-activity relationship studies revealed that ReLPS, detoxified LPS, and mono-phosphoryl as well as diphosphoryl lipid A, also showed similar inhibition, suggesting that neither O-antigen polysaccharide nor O-acyl chain, but rather phosphate groups in the lipid A domain, seem to have been responsible for the inhibitory effects. Besides, LPS was co-precipitated with Lon by an anti-Lon antibody, showing the direct binding of LPS to Lon. These results suggest that LPS bound to Lon and inhibited the protease activity of Lon by inhibiting its ATPase activity. These results also seem to be another example of a negatively charged phosphate group in membrane components of Escherichia coli being involved in the regulation of protease activity of Lon through binding to Lon and inhibiting its ATPase activity, as in the case of cardiolipin.