Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Bordetella pertussis [ICD11:
XN23B 
]
NCBI PubMed ID: 33668925Publication DOI: 10.3390/ijms22052281Journal NLM ID: 101092791Publisher: Basel, Switzerland: MDPI
Correspondence: kawahara
kanto-gakuin.ac.jp
Institutions: Department of Biosciences, College of Science and Engineering, Kanto Gakuin University, Yokohama, Kanagawa 236-8501, Japan
Lipid A of Gram-negative bacteria is known to represent a central role for the immunological activity of endotoxin. Chemical structure and biosynthetic pathways as well as specific receptors on phagocytic cells had been clarified by the beginning of the 21st century. Although the lipid A of enterobacteria including Escherichia coli share a common structure, other Gram-negative bacteria belonging to various classes of the phylum Proteobacteria and other taxonomical groups show wide variety of lipid A structure with relatively decreased endotoxic activity compared to that of E. coli. The structural diversity is produced from the difference of chain length of 3-hydroxy fatty acids and non-hydroxy fatty acids linked to their hydroxyl groups. In some bacteria, glucosamine in the backbone is substituted by another amino sugar, or phosphate groups bound to the backbone are modified. The variation of structure is also introduced by the enzymes that can modify electrostatic charges or acylation profiles of lipid A during or after its synthesis. Furthermore, lipid A structure can be artificially modified or engineered by the disruption and introduction of biosynthetic genes especially those of acyltransferases. These technologies may produce novel vaccine adjuvants or antagonistic drugs derived from endotoxin in the future.
Lipopolysaccharide, lipid A, endotoxin, chemical structure, fatty acid, engineering
Structure type: oligomer
Location inside paper: Fig. 7, 3HO-C10:0 transferase gene (lpxA) from P. aeruginosa
Compound class: lipid A
Contained glycoepitopes: IEDB_135394,IEDB_135515,IEDB_141807,IEDB_151531,IEDB_176772
Biosynthesis and genetic data: lpxA
Comments, role: review; engineering of B. pertussis lipid A using acyltransferase genes from P. aeruginosa
NCBI Taxonomy refs (TaxIDs): 520,
287
Show glycosyltransferases
There is only one chemically distinct structure:
Found 
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