ArticleInfection and immunity2016
Modification of the 1-Phosphate Group during Biosynthesis of Capnocytophaga canimorsus Lipid A.
Article in Infection and immunity, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 16 citations in OpenAlex.
- TheJournal of oral microbiology · 2025Article
- Molecular Mechanisms of Bacterial Resistance to Antimicrobial Peptides in the Modern Era: An Updated Review.Microorganisms · 2024Review
- Structural determination of the lipid A from the deep-sea bacterium Zunongwangia profunda SM-A87: a small-scale approach.Glycoconjugate journal · 2022Article
- Predominant phosphorylation patterns inJournal of lipid research · 2020Article
- Substrate structure-activity relationship reveals a limited lipopolysaccharide chemotype range for intestinal alkaline phosphatase.The Journal of biological chemistry · 2019Article
- Structural characterization of phosphoethanolamine-modified lipid A from probioticRSC advances · 2019Article
- Antimicrobial Photodynamic Therapy to Control Clinically Relevant Biofilm Infections.Frontiers in microbiology · 2018Review
- Biosynthesis and structure-activity relationships of the lipid a family of glycolipids.Current opinion in chemical biology · 2017Review
- Identification ofFrontiers in microbiology · 2017Article
- Structure-Activity Relationship ofFrontiers in immunology · 2017Article
- Evidence for a LOS and a capsular polysaccharide in Capnocytophaga canimorsus.Scientific reports · 2016Article
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Capnocytophaga canimorsus, a commensal bacterium of dog's mouth flora causing severe infections in humans after dog bites or scratches, has a lipopolysaccharide (LPS) (endotoxin) with low-inflammatory lipid A. In particular, it contains a phosphoethanolamine (P-Etn) instead of a free phosphate group at the C-1 position of the lipid A backbone, usually present in highly toxic enterobacterial Gram-negative lipid A. Here we show that the C. canimorsus genome comprises a single operon encoding a lipid A 1-phosphatase (LpxE) and a lipid A 1 P-Etn transferase (EptA). This suggests that lipid A is modified during biosynthesis after completing acylation of the backbone by removal of the 1-phosphate and subsequent addition of an P-Etn group. As endotoxicity of lipid A is known to depend largely on the degree of unsubstituted or unmodified phosphate residues, deletion of lpxE or eptA led to mutants lacking the P-Etn group, with consequently increased endotoxicity and decreased resistance to cationic antimicrobial peptides (CAMP). Consistent with the proposed sequential biosynthetic mechanism, the endotoxicity and CAMP resistance of a double deletion mutant of lpxE-eptA was similar to that of a single lpxE mutant. Finally, the proposed enzymatic activities of LpxE and EptA based on sequence similarity could be successfully validated by mass spectrometry (MS)-based analysis of lipid A isolated from the corresponding deletion mutant strains.
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