ArticleThe Journal of biological chemistry2012
Secondary cell wall polymers of Enterococcus faecalis are critical for resistance to complement activation via mannose-binding lectin.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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22 citing papers in PubMed, 54 citations in OpenAlex.
- Molecular mechanisms of virulence in Enterococcus faecium: integrating Esp, Acm, regulatory RNA networks in multidrug resistant nosocomial infections.Archives of microbiology · 2026Review
- Review
- Pangenome-spanning epistasis and coselection analysis via de Bruijn graphs.Genome research · 2024Article
- Exploring the role of E. faecalis enterococcal polysaccharide antigen (EPA) and lipoproteins in evasion of phagocytosis.Molecular microbiology · 2024Article
- The pathogenicity of vancomycin-resistant Enterococcus faecalis to colon cancer cells.BMC infectious diseases · 2024Article
- Review
- Carbohydrate Metabolism Affects Macrophage-Mediated Killing of Enterococcus faecalis.mSystems · 2021Article
- Sugarcoating it: Enterococcal polysaccharides as key modulators of host-pathogen interactions.PLoS pathogens · 2021Review
- Inhibition of the Classical Pathway of Complement Activation Impairs Bacterial Clearance during Enterococcus faecalis Infection.Infection and immunity · 2021Article
- Cell wall polysaccharides of Gram positive ovococcoid bacteria and their role as bacteriophage receptors.Computational and structural biotechnology journal · 2021Review
- Review
- Evolution of vancomycin-resistantProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Article
- Detection and characterization of bacterial polysaccharides in drug-resistant enterococci.Glycoconjugate journal · 2019Article
- Article
- Pathogenicity of Enterococci.Microbiology spectrum · 2019Review
- Bacteriophage Resistance Alters Antibiotic-Mediated Intestinal Expansion of Enterococci.Infection and immunity · 2019Article
- Decoration of the enterococcal polysaccharide antigen EPA is essential for virulence, cell surface charge and interaction with effectors of the innate immune system.PLoS pathogens · 2019Article
- Broad-spectrum capture of clinical pathogens using engineered Fc-mannose-binding lectin enhanced by antibiotic treatment.F1000Research · 2019Article
- Exopolysaccharide-mediated surface penetration as new virulence trait inCommunicative & integrative biology · 2019Article
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Authors and funding
11 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The complement system is part of our first line of defense against invading pathogens. The strategies used by Enterococcus faecalis to evade recognition by human complement are incompletely understood. In this study, we identified an insertional mutant of the wall teichoic acid (WTA) synthesis gene tagB in E. faecalis V583 that exhibited an increased susceptibility to complement-mediated killing by neutrophils. Further analysis revealed that increased killing of the mutant was due to a higher rate of phagocytosis by neutrophils, which correlated with higher C3b deposition on the bacterial surface. Our studies indicated that complement activation via the lectin pathway was much stronger on the tagB mutant compared with wild type. In concordance, we found an increased binding of the key lectin pathway components mannose-binding lectin and mannose-binding lectin-associated serine protease-2 (MASP-2) on the mutant. To understand the mechanism of lectin pathway inhibition by E. faecalis, we purified and characterized cell wall carbohydrates of E. faecalis wild type and V583ΔtagB. NMR analysis revealed that the mutant strain lacked two WTAs with a repeating unit of →6)[α-l-Rhap-(1→3)]β-D-GalpNAc-(1→5)-Rbo-1-P and →6) β-D-Glcp-(1→3) [α-D-Glcp-(1→4)]-β-D-GalpNAc-(1→5)-Rbo-1-P→, respectively (Rbo, ribitol). In addition, compositional changes in the enterococcal rhamnopolysaccharide were noticed. Our study indicates that in E. faecalis, modification of peptidoglycan by secondary cell wall polymers is critical to evade recognition by the complement system.
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