ArticleThe Journal of biological chemistry2013
Structural reevaluation of Streptococcus pneumoniae Lipoteichoic acid and new insights into its immunostimulatory potency.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
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Who cites it
55 citing papers in PubMed, 109 citations in OpenAlex.
- TLR-mediated inflammatory responses to Streptococcus pneumoniae are highly dependent on surface expression of bacterial lipoproteins.Journal of immunology (Baltimore, Md. : 1950) · 2014Trial
- A pathogenic gut lipoglycan drives systemic thromboinflammation in lupus nephritis.Annals of the rheumatic diseases · 2026Article
- A peptide-based medical device for the selective removal of inflammatory factors from the blood of people with sepsis.Communications medicine · 2025Article
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- Structure, Function, and Regulation of LytA: TheMicroorganisms · 2025Review
- Saccharibacteria deploy two distinct Type IV pili, driving episymbiosis, host competition, and twitching motility.bioRxiv : the preprint server for biology · 2024Article
- Biosynthesis of mitis group streptococcal glycolipids and their roles in physiology and antibiotic susceptibility.bioRxiv : the preprint server for biology · 2024Article
- MprF-mediated immune evasion is necessary for Lactiplantibacillus plantarum resilience in the Drosophila gut during inflammation.PLoS pathogens · 2024Article
- Lipoteichoic acids influence cell shape and bacterial division of Streptococcus suis serotype 2, but play a limited role in the pathogenesis of the infection.Veterinary research · 2024Article
- The gut microbiome in systemic lupus erythematosus: lessons from rheumatic fever.Nature reviews. Rheumatology · 2024Review
- Combining antibiotic with anti-TLR2/TLR13 therapy prevents brain pathology in pneumococcal meningitis.JCI insight · 2024Article
- Lipoteichoic Acids Are Essential for Pneumococcal Colonization and Membrane Integrity.Journal of innate immunity · 2024Article
- The choline-binding proteins PspA, PspC, and LytA ofInfection and immunity · 2023Article
- Analysis of Bacterial Phosphorylcholine-Related Genes Reveals an Association between Type-Specific Biosynthesis Pathways and Biomolecules Targeted for Phosphorylcholine Modification.Microbiology spectrum · 2023Article
- WhyD tailors surface polymers to prevent premature bacteriolysis and direct cell elongation ineLife · 2022Article
- Review
- Chemical Reporters for Bacterial Glycans: Development and Applications.Chemical reviews · 2022Review
- d-Alanylation of Lipoteichoic Acids inFrontiers in microbiology · 2022Article
- A Jack of All Trades: The Role of Pneumococcal Surface Protein A in the Pathogenesis ofFrontiers in cellular and infection microbiology · 2022Review
- Streptococcus pneumoniae Binds to Host Lactate Dehydrogenase via PspA and PspC To Enhance Virulence.mBio · 2021Article
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Authors and funding
9 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Streptococcus pneumoniae is a Gram-positive human pathogen with a complex lipoteichoic acid (pnLTA) structure. Because the current structural model for pnLTA shows substantial inconsistencies, we reinvestigated purified and, more importantly, O-deacylated pnLTA, which is most suitable for NMR spectroscopy and electrospray ionization-MS spectrometry. We analyzed pnLTA of nonencapsulated pneumococcal strains D39Δcps and TIGR4Δcps, respectively. The data obtained allowed us to (re)define (i) the position and linkage of the repeating unit, (ii) the putative α-GalpNAc substitution at the ribitiol 5-phosphate (Rib-ol-5-P), and (iii) the length of (i.e. the number of repeating units in) the pnLTA chain. We here also describe for the first time that the terminal sugar residues in the pnLTA (Forssman disaccharide; α-D-GalpNAc-(1→3)-β-D-GalpNAc-(1→)), responsible for the cross-reactivity with anti-Forssman antigen antibodies, can be heterogeneous with respect to its degree of phosphorylcholine substitution in both O-6-positions. To assess the proinflammatory potency of pnLTA, we generated a (lipopeptide-free) Δlgt mutant of strain D39Δcps, isolated its pnLTA, and showed that it is capable of inducing IL-6 release in human mononuclear cells, independent of TLR2 activation. This finding was quite in contrast to LTA of the Staphylococcus aureus SA113Δlgt mutant, which did not activate human mononuclear cells in our experiments. Remarkably, this is also contrary to various other reports showing a proinflammatory potency of S. aureus LTA. Taken together, our study refines the structure of pnLTA and indicates that pneumococcal and S. aureus LTAs differ not only in their structure but also in their bioactivity.
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