Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Escherichia coli [ICD11:
XN6P4 
]
The structure was elucidated in this paperNCBI PubMed ID: 29321776Publication DOI: 10.3389/fimmu.2017.01741Journal NLM ID: 101560960Publisher: Lausanne: Frontiers Research Foundation
Correspondence: marta.kaszowska
iitd.pan.wroc.pl
Institutions: Department of Biotechnology and Molecular Biology, University of Opole, Opole, Poland, Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Wroclaw, Poland
Plesiomonas shigelloides is a Gram-negative bacterium that is associated with diarrheal disease in humans. Lipopolysaccharide (LPS) is the main surface antigen and virulence factor of this bacterium. The lipid A (LA) moiety of LPS is the main region recognized by target cells of immune system. Here, we evaluated the biological activities of P. shigelloides LA for their abilities to induce the productions of proinflammatory cytokines (TNF-α, IL-1β, and IL-6) by human and murine macrophages [THP-1 macrophages and immortalized murine bone marrow-derived macrophages (iBMDM)]. Four native P. shigelloides LA preparations differing in their phosphoethanolamine (PEtn) substitution, length, number, and saturation of fatty acids were compared with Escherichia coli O55 LA. The bisphosphorylated, hexaacylated, and asymmetric forms of the P. shigelloides and E. coli LA molecules had similar activities in human and murine macrophages, indicating that shortening of the acyl chains in P. shigelloides LA had no effect on its in vitro activities. The PEtn decoration also had no impact on the interaction with the toll-like receptor 4/MD-2 receptor complex. The heptaacylated form of P. shigelloides LA decorated with 16:0 exhibited strong effect on proinflammatory activity, significantly decreasing the levels of all tested cytokines in both murine and human macrophages. Our results revealed that despite the presence of shorter acyl chains and an unsaturated acyl residue (16:1), the bisphosphorylated, hexaacylated, and asymmetric forms of P. shigelloides LA represent highly immunostimulatory structures.
Lipopolysaccharide, lipid A, Plesiomonas, proinflammatory cytokines, THP-1, BMDM
Structure type: oligomer ; 1796.90
Location inside paper: fig.2, LA O55
Compound class: lipid A
Contained glycoepitopes: IEDB_135394,IEDB_135515,IEDB_141807,IEDB_151531,IEDB_176772,IEDB_534864
Methods: GLC-MS, GC-MS, de-O-acylation, ELISA, anion-exchange chromatography, mild acid hydrolysis, MALDI-TOF MS, composition analysis, HPLC, GPC, extraction, HF treatment, acetylation, cytokine production, cell viability assay
Comments, role: the main hexaacylated form lipid A from E.coli O55:B5
Related record ID(s): 12016, 12398, 12399, 12400, 12401, 12402
NCBI Taxonomy refs (TaxIDs): 2170726
Show glycosyltransferases
There is only one chemically distinct structure:
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