Taxonomic group: bacteria / Chlamydiae
(Phylum: Chlamydiae)
Host organism: Homo sapiens
Associated disease: pelvic inflammatory disease [ICD11:
GA05 
, Sex: female];
blindness [ICD11:
9D90 ];
infection due to Chlamydia trachomatis [ICD11:
XN4Q4 ]
NCBI PubMed ID: 28080049Publication DOI: 10.1021/acs.jctc.6b00856Journal NLM ID: 101232704Publisher: Washington, DC: American Chemical Society
Correspondence: snangia
syr.edu
Institutions: Department of Biomedical and Chemical Engineering, Syracuse University , Syracuse, New York 13244, United States
Lipopolysaccharides (LPSs) are vital components of the outer membrane of Gram-negative bacteria, and they act as extremely strong stimulators of innate immunity in diverse eukaryotic species. The primary immunostimulatory center of the LPS molecule is lipid A, a disaccharide-bound lipophilic domain. Considering the broad diversity in bacterial species, there are variations in the lipid A structures and their immunogenic potencies. In this work, we model the lipid A structures of eight commensal or human pathogenic bacterial species: Helicobacter pylori, Porphyromonas gingivalis, Bacteroides fragilis, Bordetella pertussis, Chlamydia trachomatis, Campylobacter jejuni, Neisseria meningitidis, and Salmonella minnesota. The membrane properties of these bacterial species were characterized and compared using molecular simulations. The structure-property relationships that emerge from this lipid A molecular library highlight the roles of acyl chain lengths, number of chains, phosphorylation state, membrane composition, and counterion charge in regulating the phase transition temperature of the membrane, diffusion coefficient of the lipids, and membrane thickness. The molecular and structural insights provided reveal the diversity in bacterial outer membrane lipids and their contribution to human disease and immunity.
Lipopolysaccharide, lipid A, outer membrane
Structure type: oligomer
Location inside paper: fig. S5
Compound class: lipid A
Contained glycoepitopes: IEDB_135394,IEDB_135515,IEDB_141807,IEDB_151531,IEDB_176772,IEDB_534865
Methods: MD simulations, molecular mechanics
3D data: membrane structure
Related record ID(s): 12017, 12403, 12404, 12405, 12407, 12408, 12409
NCBI Taxonomy refs (TaxIDs): 813
Show glycosyltransferases
There is only one chemically distinct structure:
Taxonomic group: bacteria / Chlamydiae
(Phylum: Chlamydiae)
Host organism: Homo sapiens
Associated disease: trachoma [ICD11:
1C23 , ICD11:
XN4Q4 ];
salpingitis [ICD11:
GA07 ];
pelvic inflammatory disease [ICD11:
GA05 , Sex: female];
infection due to Chlamydia trachomatis [ICD11:
XN4Q4 ]
NCBI PubMed ID: 21628561Journal NLM ID: 7505876Publisher: National Academy of Sciences
Correspondence: raetz
biochem.duke.edu
Institutions: Department of Molecular Genetics and Microbiology, Duke University Medical Center, Durham, NC 27710, USA.
Lipopolysaccharides (LPS) and lipooligosaccharides (LOS) are the main lipid components of bacterial outer membranes and are essential for cell viability in most Gram-negative bacteria. Here we show that small molecule inhibitors of LpxC [UDP-3-O-(R-3-hydroxymyristoyl)-GlcNAc deacetylase], the enzyme that catalyzes the first committed step in the biosynthesis of lipid A, block the synthesis of LOS in the obligate intracellular bacterial pathogen Chlamydia trachomatis. In the absence of LOS, Chlamydia remains viable and establishes a pathogenic vacuole ('inclusion') that supports robust bacterial replication. However, bacteria grown under these conditions were no longer infectious. In the presence of LpxC inhibitors, replicative reticulate bodies accumulated in enlarged inclusions but failed to express selected late-stage proteins and transition to elementary bodies, a Chlamydia developmental form that is required for invasion of mammalian cells. These findings suggest the presence of an outer membrane quality control system that regulates Chlamydia developmental transition to infectious elementary bodies and highlights the potential application of LpxC inhibitors as unique class of antichlamydial agents.
Lipooligosaccharide, lipid A, Chlamydia trachomatis, outer membrane
Structure type: oligomer
Location inside paper: p.10285, fig.1
Trivial name: genus-specific epitope
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_130650,IEDB_130657,IEDB_130658,IEDB_130659,IEDB_135394,IEDB_135515,IEDB_141807,IEDB_150760,IEDB_150908,IEDB_151531,IEDB_176772,IEDB_534865
Methods: genetic methods
Biosynthesis and genetic data: genetic data,biochemical data
NCBI Taxonomy refs (TaxIDs): 813
Show glycosyltransferases
There is only one chemically distinct structure:
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