ArticleInfection and immunity2006
Opsonic antibodies to Enterococcus faecalis strain 12030 are directed against lipoteichoic acid.
Article in Infection and immunity, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 92 citations in OpenAlex.
- Enterococcus faecium: evolution, adaptation, pathogenesis and emerging therapeutics.Nature reviews. Microbiology · 2024Review
- Human Serum Supplementation Promotes Streptococcus mitis Growth and Induces Specific Transcriptomic Responses.Microbiology spectrum · 2023Article
- Synthetic Glycans to Improve Current Glycoconjugate Vaccines and Fight Antimicrobial Resistance.Chemical reviews · 2022Review
- Streptococcus pneumoniae, S. mitis, and S. oralis Produce a Phosphatidylglycerol-Dependent,mSphere · 2021Article
- Generation of glucosylatedRSC chemical biology · 2021Article
- Intrinsic resistance of Enterococcus faecalis strains to ΦEf11 phage endolysin is associated with the presence of ΦEf11 prophage.Archives of virology · 2021Article
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- Detection and characterization of bacterial polysaccharides in drug-resistant enterococci.Glycoconjugate journal · 2019Article
- Impact of antibiotic treatment and host innate immune pressure on enterococcal adaptation in the human bloodstream.Science translational medicine · 2019Article
- Potential targets for next generation antimicrobial glycoconjugate vaccines.FEMS microbiology reviews · 2018Review
- Envelope Structures of Gram-Positive Bacteria.Current topics in microbiology and immunology · 2017Review
- Lipoteichoic acid from anBiomedical reports · 2015Article
- A Vaccine Approach for the Prevention of Infections by Multidrug-resistant Enterococcus faecium.The Journal of biological chemistry · 2015Article
- In vitro and in vivo activity of hyperimmune globulin preparations against multiresistant nosocomial pathogens.Infection · 2015Article
- Article
- Mechanisms of antibiotic resistance in enterococci.Expert review of anti-infective therapy · 2014Review
- Detection of opsonic antibodies against Enterococcus faecalis cell wall carbohydrates in immune globulin preparations.Infection · 2014Article
- A novel role for D-alanylation of lipoteichoic acid of enterococcus faecalis in urinary tract infection.PloS one · 2014Article
- Article
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Authors and funding
7 authors at 3 institutions in 2 countries.
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Abstract
A teichoic acid (TA)-like polysaccharide in Enterococcus faecalis has previously been shown to induce opsonic antibodies that protect against bacteremia after active and passive immunization. Here we present new data providing a corrected structure of the antigen and the epitope against which the opsonic antibodies are directed. Capsular polysaccharide isolated from E. faecalis strain 12030 by enzymatic digestion of peptidoglycan and chromatography (enzyme-TA) was compared with lipoteichoic acid (LTA) extracted using butanol and purified by hydrophobic-interaction chromatography (BuOH-LTA). Structural determinations were carried out by chemical analysis and nuclear magnetic resonance spectroscopy. Antibody specificity was assessed by enzyme-linked immunosorbent assay and the opsonophagocytosis assay. After alanine ester hydrolysis, there was structural identity between enzyme-TA and BuOH-LTA of the TA-parts of the two molecules. The basic enterococcal LTA structure was confirmed: 1,3-poly(glycerol phosphate) nonstoichiometrically substituted at position C-2 of the glycerol residues with d-Ala and kojibiose. We also detected a novel substituent at position C-2, [D-Ala-->6]-alpha-D-Glcp-(1-->2-[D-Ala-->6]-alpha-D-Glcp-1-->). Antiserum raised against enzyme-TA bound equally well to BuOH-LTA and dealanylated BuOH-LTA as to the originally described enzyme-TA antigen. BuOH-LTA was a potent inhibitor of opsonophagocytic killing by the antiserum to enzyme-TA. Immunization with antibiotic-killed whole bacterial cells did not induce a significant proportion of antibodies directed against alanylated epitopes on the TA, and opsonic activity was inhibited completely by both alanylated and dealanylated BuOH-LTA. In summary, the E. faecalis strain 12030 enzyme-TA is structurally and immunologically identical to dealanylated LTA. Opsonic antibodies to E. faecalis 12030 are directed predominantly to nonalanylated epitopes on the LTA molecule.
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