@article{89546,
  keywords = {Biological Transport, Escherichia coli, Models, Biological, Metabolic Networks and Pathways, Escherichia coli Proteins, Cell Membrane, Bacterial Outer Membrane Proteins, Lipopolysaccharides},
  author = {Suguru Okuda and David Sherman and Thomas Silhavy and Natividad Ruiz and Daniel Kahne},
  title = {Lipopolysaccharide transport and assembly at the outer membrane: the PEZ model},
  abstract = {<p>Gram-negative bacteria have a double-membrane cellular envelope that enables them to colonize harsh environments and prevents the entry of many clinically available antibiotics. A main component of most outer membranes is lipopolysaccharide (LPS), a glycolipid containing several fatty acyl chains and up to hundreds of sugars that is synthesized in the cytoplasm. In the past two decades, the proteins that are responsible for transporting LPS across the cellular envelope and assembling it at the cell surface in Escherichia coli have been identified, but it remains unclear how they function. In this Review, we discuss recent advances in this area and present a model that explains how energy from the cytoplasm is used to power LPS transport across the cellular envelope to the cell surface.</p>
},
  year = {2016},
  journal = {Nat Rev Microbiol},
  volume = {14},
  pages = {337-45},
  month = {06/2016},
  issn = {1740-1534},
  doi = {10.1038/nrmicro.2016.25},
  language = {eng},
}