Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Escherichia coli [ICD11:
XN6P4 
]
NCBI PubMed ID: 28108356Publication DOI: 10.1016/j.bbalip.2017.01.004Journal NLM ID: 0217513Publisher: Elsevier
Correspondence: rkernst
umaryland.edu
Institutions: Institute of Marine & Environmental Technology, University of Maryland Center for Environmental Science, Baltimore, MD 21202, United States, Department of Pharmaceutical Sciences, School of Pharmacy, University of Maryland, Baltimore, MD 21201, United States, Department of Microbial Pathogenesis, School of Dentistry, University of Maryland, Baltimore, MD 21201, United States
Strategies utilizing Toll-like receptor 4 (TLR4) agonists for treatment of cancer, infectious diseases, and other targets report promising results. Potent TLR4 antagonists are also gaining attention as therapeutic leads. Though some principles for TLR4 modulation by lipid A have been described, a thorough understanding of the structure-activity relationship (SAR) is lacking. Only through a complete definition of lipid A-TLR4 SAR is it possible to predict TLR4 signaling effects of discrete lipid A structures, rendering them more pharmacologically relevant. A limited 'toolbox' of lipid A-modifying enzymes has been defined and is largely composed of enzymes from mesophile human and zoonotic pathogens. Expansion of this 'toolbox' will result from extending the search into lipid A biosynthesis and modification by bacteria living at the extremes. Here, we review the fundamentals of lipid A structure, advances in lipid A uses in TLR4 modulation, and the search for novel lipid A-modifying systems in extremophile bacteria. This article is part of a Special Issue entitled: Bacterial Lipids edited by Russell E. Bishop.
lipid A structure, Marine bacteria, TLR4 agonists, TLR4 antagonists, TLR4 immunomodulation, Lipid A modifying enzymes
Structure type: oligomer
Location inside paper: p.1441, fig.2A
Compound class: LPS, lipid A, glycolipid, phosphoglycolipid
Contained glycoepitopes: IEDB_135394,IEDB_135515,IEDB_141807,IEDB_151531,IEDB_176772,IEDB_534864
Biological activity: E. coli lipid A results in a highly endotoxic structure with strong TLR4 agonism
Comments, role: review
Related record ID(s): 12423, 12424, 12425, 12426, 12427
NCBI Taxonomy refs (TaxIDs): 562
Show glycosyltransferases
There is only one chemically distinct structure:
Found 
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