The lipid A 1‐phosphatase, LpxE, play multiple roles in bacteria envelope biogenesis

Abstract

Gram‐negative bacteria cell envelope is multilayered structure that consist of lipopolysaccharide at outer leaflet of the outer‐membrane, peptidoglycan at periplasmic space and glycerophospholipids which is the major component of inner‐membrane and the inner leaflet of the outer‐membrane. Distinct lipid phosphatases are thought to be involved in cell envelope biogenesis by dephosphorylating precursors such as lipid A, undecaprenyl pyrophosphate (C55‐PP) and phosphatidylglycerol phosphate (PGP). Lipid A 1‐phosphatase (LpxE) is a member of the lipid phosphatase/phosphotransferase (LPT) family, which is responsible for bacterial virulence, cationic antibiotic resistance and modulation of the host innate immune system. We report the identification of lipid phosphatase, named as LpxEAA in Aquifex aeolicus (A.aeolicus) VF5, capable of dephosphorylating all of above lipid precursors. Additionally, we show that the LpxE from the human pathogens Francisella (LpxEFN) and Helicobacter (LpxEHP) are not only able to dephosphorylating lipid A but also C55‐PP and/or PGP, respectively. This multi‐functionalities of LpxE suggests that it could participate in a wide range of bacterial envelope biogenesis, beyond the well‐established lipid A 1‐phosphatase activity. Based on our research, we hypothesized that pathogens which have LpxE could survive against various environmental changes by regulating the overall bacterial envelope biogenesis through LpxE activity.Support or Funding InformationThis work was supported by National Institutes of Health (NIH) grants (GM051796 to C.R.H.R and P.Z. and AI055588 to P.Z.) and Kist intramural grants (2E27391 to H.S.C and 2E27470 to S.H.K), We thank Dr. Ziqiang Guan for assisting mass spectrometry analysis.This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal.