Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Bordetella bronchiseptica [ICD11:
XN173 
]
The structure was elucidated in this paperNCBI PubMed ID: 21764941Journal NLM ID: 2985120RPublisher: American Society for Microbiology
Correspondence: rkernst

umaryland.edu
Institutions: Department of Molecular and Cellular Biology, University of Guelph, Guelph, Ontario, Canada, Department of Medicinal Chemistry, University of Washington, Seattle, Washington, Department of Microbial Pathogenesis, School of Dentistry, University of Maryland—Baltimore, Baltimore, Maryland, School of Veterinary Science, University of Bristol, Langford, United Kingdom
PagL and LpxO are enzymes that modify lipid A. PagL is a 3-O deacylase that removes the primary acyl chain from the 3 position, and LpxO is an oxygenase that 2-hydroxylates specific acyl chains in the lipid A. pagL and lpxO homologues have been identified in the genome of Bordetella bronchiseptica, but in the current structure for B. bronchiseptica lipid A the 3 position is acylated and 2-OH acylation is not reported. We have investigated the role of B. bronchiseptica pagL and lpxO in lipid A biosynthesis. We report a different structure for wild-type (WT) B. bronchiseptica lipid A, including the presence of 2-OH-myristate, the presence of which is dependent on lpxO. We also demonstrate that the 3 position is not acylated in the major WT lipid A structures but that mutation of pagL results in the presence of 3-OH-decanoic acid at this position, suggesting that lipid A containing this acylation is synthesized but that PagL removes most of it from the mature lipid A. These data refine the structure of B. bronchiseptica lipid A and demonstrate that pagL and lpxO are involved in its biosynthesis.
biosynthesis, structure, lipid A, Bordetella bronchiseptica, lpxO, pagL
Structure type: oligomer
Location inside paper: p.4727, fig.1C
Compound class: lipid A
Contained glycoepitopes: IEDB_135394,IEDB_141181,IEDB_141807,IEDB_151531,IEDB_176772
Methods: PCR, DNA techniques, ESI-ICR-MS, GC, conjugatation
Comments, role: structure of B. bronchiseptica RB50 major species of the lipid A in this study.
Related record ID(s): 26279, 31949
NCBI Taxonomy refs (TaxIDs): 257310
Show glycosyltransferases
There is only one chemically distinct structure: