The carboxy terminus causes interfacial assembly of oleate hydratase on a membrane bilayer.

The soluble flavoprotein oleate hydratase (OhyA) hydrates the 9-cis double bond of unsaturated fatty acids. OhyA substrates are embedded in membrane bilayers; OhyA must remove the fatty acid from the bilayer and enclose it in the active site. Here, we show that the positively charged helix-turn-helix motif in the carboxy terminus (CTD) is responsible for interacting with the negatively charged phosphatidylglycerol (PG) bilayer.

Taste vs. pain: A sensory feast in bacterial meningitis.

During meningitis, sensory neurons detect bacterial toxins and metabolites. Early activation of pain receptors suppresses host defense in the meninges while, later, taste receptors amplify inflammation in the spinal cord. Is a neuroimmune axis a clue to new treatments?

Mini-Review: Bioactivities of Bacterial Cell Envelopes in the Central Nervous System.

During acute bacterial meningitis, recognition of the bacterial envelope by immune cells of the central nervous system (CNS) generates a robust response that is essential to clear bacteria. This response is further amplified during treatment when lytic antibiotics, required for cure, also generate a burst of highly inflammatory cell envelope debris. Different peptidoglycan (PG) subcomponents interact with neurons, glia, and the blood brain barrier resulting in the entire symptom complex of meningitis.

Simultaneously inhibiting undecaprenyl phosphate production and peptidoglycan synthases promotes rapid lysis in Escherichia coli.

Peptidoglycan (PG) is a highly cross-linked polysaccharide that encases bacteria, resists the effects of turgor and confers cell shape. PG precursors are translocated across the cytoplasmic membrane by the lipid carrier undecaprenyl phosphate (Und-P) where they are incorporated into the PG superstructure. Previously, we found that one of our Escherichia coli laboratory strains (CS109) harbors a missense mutation in uppS, which encodes an enzymatically defective Und-P(P) synthase.

A Defective Undecaprenyl Pyrophosphate Synthase Induces Growth and Morphological Defects That Are Suppressed by Mutations in the Isoprenoid Pathway of Escherichia coli.

The peptidoglycan exoskeleton shapes bacteria and protects them against osmotic forces, making its synthesis the target of many current antibiotics. Peptidoglycan precursors are attached to a lipid carrier and flipped from the cytoplasm into the periplasm to be incorporated into the cell wall. In , this carrier is undecaprenyl phosphate (Und-P), which is synthesized as a diphosphate by the enzyme undecaprenyl pyrophosphate synthase (UppS).