Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Acinetobacter baumannii [ICD11:
XN8LS 
]
NCBI PubMed ID: 29114953Publication DOI: 10.1111/mmi.13872Journal NLM ID: 8712028Publisher: Blackwell Publishing
Correspondence: strent

uga.edu
Institutions: Department of Microbiology, University of Georgia, Athens, GA, USA, Department of Infectious Diseases, University of Georgia, 510 DW Brooks Drive, Athens, GA 30602, USA
Asymmetry in the outer membrane has long defined the cell envelope of Gram-negative bacteria. This asymmetry, with lipopolysaccharide (LPS) or lipooligosaccharide (LOS) exclusively in the outer leaflet of the membrane, establishes an impermeable barrier that protects the cell from a number of stressors in the environment. Work done over the past 5 years has shown that Acinetobacter baumannii has the remarkable capability to survive with inactivated production of lipid A biosynthesis and the absence of LOS in its outer membrane. The implications of LOS-deficient A. baumannii are far-reaching - from impacts on cell envelope biogenesis and maintenance, bacterial physiology, antibiotic resistance and virulence. This review examines recent work that has contributed to our understanding of LOS-deficiency and compares it to studies done on Neisseria meningitidis and Moraxella catarrhalis; the two other organisms with this capability.
Lipopolysaccharide, Lipooligosaccharide, Acinetobacter baumannii, lipid A, Gram-negative bacteria, barrier, bacterial outer membrane proteins
Structure type: oligomer
Location inside paper: fig.2, A. baumannii modified lipid A
Compound class: lipid A
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_137473,IEDB_141807,IEDB_151531,IEDB_534864
Enzymes that release or process the structure: EptA (PmrC), LpxO, ArnT homolog
Comments, role: (review) structure from ref. Boll et al., 2015b [DOI:10.1128/mBio.00478-15]
Related record ID(s): 12963
NCBI Taxonomy refs (TaxIDs): 400667
Show glycosyltransferases
There is only one chemically distinct structure: