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

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.