Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Campylobacter jejuni [ICD11:
XN4Q5 
]
The structure was elucidated in this paperNCBI PubMed ID: 29535976Publication DOI: 10.3389/fcimb.2018.00058Journal NLM ID: 101585359Publisher: Lausanne: Frontiers Media SA
Correspondence: Dmitry V. Kuprash <kuprash
gmail.com>
Institutions: Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia, Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow, Russia, Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, Russia, CNR Institute for Polymers Composites and Biomaterials, Catania, Italy, Department of Immunology, Biological Faculty, Lomonosov Moscow State University, Moscow, Russia, German Rheumatism Research Center, Leibniz Institute, Berlin, Germany, Branch of Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Pushchino, Russia
Toll-like receptor 4 (TLR4) initiates immune response against Gram-negative bacteria upon specific recognition of lipid A moiety of lipopolysaccharide (LPS), the major component of their cell wall. Some natural differences between LPS variants in their ability to interact with TLR4 may lead to either insufficient activation that may not prevent bacterial growth, or excessive activation which may lead to septic shock. In this study we evaluated the biological activity of LPS isolated from pathogenic strain of Campylobacter jejuni, the most widespread bacterial cause of foodborne diarrhea in humans. With the help of hydrophobic chromatography and MALDI-TOF mass spectrometry we showed that LPS from a C. jejuni strain O2A consists of both hexaacyl and tetraacyl forms. Since such hypoacylation can result in a reduced immune response in humans, we assessed the activity of LPS from C. jejuni in mouse macrophages by measuring its capacity to activate TLR4-mediated proinflammatory cytokine and chemokine production, as well as NF?B-dependent reporter gene transcription. Our data support the hypothesis that LPS acylation correlates with its bioactivity.
LPS, lipid A, Campylobacter jejuni, pathogenic bacteria, macrophages, TLR4, acyl chains, proinflammatory cytokines
Structure type: oligomer ; 1402.8
Location inside paper: fig.1, tetraacyl lipid A
Compound class: lipid A
Contained glycoepitopes: IEDB_135394,IEDB_135515,IEDB_141807,IEDB_151531
Methods: ELISA, MALDI-TOF MS, biological assays, cytokine analysis, RT-PCR, statistical analysis, LPS bioactivity in murine macrophages
Related record ID(s): 12646
NCBI Taxonomy refs (TaxIDs): 197
Show glycosyltransferases
There is only one chemically distinct structure:
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