Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Acinetobacter baumannii [ICD11:
XN8LS 
]
NCBI PubMed ID: 37791675Publication DOI: 10.2478/aiht-2023-74-3717Journal NLM ID: 0373100Publisher: Zagreb, Croatia: Institute for Medical Research and Occupational Health
Correspondence: I. Kosalec <ivan.kosalec
pharma.unizg.hr>
Institutions: University of Zagreb Faculty of Pharmacy and Biochemistry, Department of Microbiology, Zagreb, Croatia
Polymyxin antibiotics are the last resort for treating patients in intensive care units infected with multiple-resistant Gram-negative bacteria. Due to their polycationic structure, their mode of action is based on an ionic interaction with the negatively charged lipid A portion of the lipopolysaccharide (LPS). The most prevalent polymyxin resistance mechanisms involve covalent modifications of lipid A: addition of the cationic sugar 4-amino-L-arabinose (L-Ara4N) and/or phosphoethanolamine (pEtN). The modified structure of lipid A has a lower net negative charge, leading to the repulsion of polymyxins and bacterial resistance to membrane disruption. Genes encoding the enzymatic systems involved in these modifications can be transferred either through chromosomes or mobile genetic elements. Therefore, new approaches to resistance diagnostics have been developed. On another note, interfering with these enzymatic systems might offer new therapeutic targets for drug discovery. This literature review focuses on diagnostic approaches based on structural changes in lipid A and on the therapeutic potential of molecules interfering with these changes.
lipid A, Gram-negative bacteria, MALDI-TOF-MS, antimicrobial resistance, adjuvants, MCR-1
Structure type: oligomer ; 1728
Location inside paper: table 3, native lipid A
Compound class: lipid A
Contained glycoepitopes: IEDB_135394,IEDB_135515,IEDB_141807,IEDB_151531,IEDB_534864
Comments, role: review; the proposed structures of native lipid A for A. baumannii
NCBI Taxonomy refs (TaxIDs): 470
Show glycosyltransferases
There is only one chemically distinct structure:
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