Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Escherichia coli [ICD11:
XN6P4 
]
Publication DOI: 10.1002/9783527638192.ch13Publisher: New York: J. Wiley & Sons Ltd
Editors: Stulik J, Toman R, Butaye P, Ulrich RG
Correspondence: Toman R <virutoma
savba.sk>
Institutions: Laboratory for Diagnosis and Prevention of Rickettsial and Chlamydial Infections, Institute of Virology, SAS, Bratislava, Slovakia
From the studies presented we conclude that the major P. salmonis lipid A species represents the hexaacyl form, resembling the classical lipid A found in the Enterobacteriaceae family. This fact might be one of the reasons for the high endotoxic potency of the P. salmonis bacterium. On the contrary, the structures of the investigated lipids A from two C. burnetii strains (NM I, NM II) and Priscilla show a considerable heterogeneity due to their fatty acid variations at the O-3 and O-3′ positions of the GlcN disaccharide. They differ noticeably from those of a typical enterobacterial lipid A with high endotoxicity, and in fact their endotoxin activity was considerably lower than that found with the E. coli lipid A
lipid A, endotoxin, Coxiella burnetii, Proteobacteria, Piscirickettsia salmonis
Structure type: oligomer
Location inside paper: Fig. 13.1
Compound class: LPS, lipid A, glycolipid, phosphoglycolipid
Contained glycoepitopes: IEDB_135394,IEDB_135515,IEDB_141807,IEDB_151531,IEDB_176772,IEDB_534864
Methods: GC-MS, acid hydrolysis, ESI-MS/MS, MALDI-MS
Related record ID(s): 47793, 47794, 47795
NCBI Taxonomy refs (TaxIDs): 562
Show glycosyltransferases
There is only one chemically distinct structure:
Found 
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