Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Citrobacter [ICD11:
XN0FZ 
]
NCBI PubMed ID: 33538159Publication DOI: 10.1021/acs.jmedchem.0c02185Journal NLM ID: 9716531Publisher: Washington, DC: American Chemical Society
Correspondence: bruneljm
yahoo.fr
Institutions: UMR-MD1, U1261, Aix Marseille Université, INSERM, SSA, MCT, 13385 Marseille, France, Laboratory of Microorganisms and Active Biomolecules, Department of Biology, Faculty of Sciences of Tunis, University of Tunis El Manar, Tunis 1008, Tunisia
The outer membrane (OM) of Gram-negative bacteria provides an efficient barrier against external noxious compounds such as antimicrobial agents. Associated with drug target modification, it contributes to the overall failure of chemotherapy. In the complex OM architecture, Lipid A plays an essential role by anchoring the lipopolysaccharide in the membrane and ensuring the spatial organization between lipids, proteins, and sugars. Currently, the targets of almost all antibiotics are intracellularly located and require translocation across membranes. We report herein an integrated view of Lipid A synthesis, membrane assembly, a structure comparison at the molecular structure level of numerous Gram-negative bacterial species, as well as its recent use as a target for original antibacterial molecules. This review paves the way for a new vision of a key membrane component that acts during bacterial adaptation to environmental stresses and for the development of new weapons against microbial resistance to usual antibiotics.
Lipopolysaccharide, lipid A, Gram-negative bacteria, outer membrane, stress, adaptation
Structure type: oligomer
Location inside paper: Fig. 4, Citrobacter WT
Compound class: lipid A
Contained glycoepitopes: IEDB_141181,IEDB_141807,IEDB_151531,IEDB_176772,IEDB_534864
Comments, role: review
NCBI Taxonomy refs (TaxIDs): 544
Show glycosyltransferases
There is only one chemically distinct structure:
Found 
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