Title | Lipopolysaccharide transport and assembly at the outer membrane: the PEZ model. |
Publication Type | Journal Article |
Year of Publication | 2016 |
Authors | Okuda, S, Sherman, DJ, Silhavy, TJ, Ruiz, N, Kahne, D |
Journal | Nat Rev Microbiol |
Volume | 14 |
Issue | 6 |
Pagination | 337-45 |
Date Published | 2016 Jun |
ISSN | 1740-1534 |
Keywords | Bacterial Outer Membrane Proteins, Biological Transport, Cell Membrane, Escherichia coli, Escherichia coli Proteins, Lipopolysaccharides, Metabolic Networks and Pathways, Models, Biological |
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> |
DOI | 10.1038/nrmicro.2016.25 |
Alternate Journal | Nat Rev Microbiol |
PubMed ID | 27026255 |
PubMed Central ID | PMC4937791 |
Grant List | R01 GM100951 / GM / NIGMS NIH HHS / United States R35 GM118024 / GM / NIGMS NIH HHS / United States R01 GM034821 / GM / NIGMS NIH HHS / United States R01 AI081059 / AI / NIAID NIH HHS / United States R37 GM034821 / GM / NIGMS NIH HHS / United States |