Trial reportPLoS pathogens2013
Novel staphylococcal glycosyltransferases SdgA and SdgB mediate immunogenicity and protection of virulence-associated cell wall proteins.
Trial report in PLoS pathogens, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
48 citing papers in PubMed, 86 citations in OpenAlex.
- Isotype conversion of Staphylococcal-specific IgG into IgM broadens the reactivity to other bacterial pathogens.Cell reports. Medicine · 2025Article
- Article
- Single-cell Sequencing of Circulating Human Plasmablasts during Staphylococcus aureus Bacteremia.Journal of immunology (Baltimore, Md. : 1950) · 2024Article
- The characteristics of pre-existing humoral imprint determine efficacy of S. aureus vaccines and support alternative vaccine approaches.Cell reports. Medicine · 2024Article
- The role of human extracellular matrix proteins in defining Staphylococcus aureus biofilm infections.FEMS microbiology reviews · 2024Review
- Convergent behavior of extended stalk regions from staphylococcal surface proteins with widely divergent sequence patterns.Protein science : a publication of the Protein Society · 2023Article
- Convergent behavior of extended stalk regions from staphylococcal surface proteins with widely divergent sequence patterns.bioRxiv : the preprint server for biology · 2023Article
- Review
- A homogeneous high-DAR antibody-drug conjugate platform combining THIOMAB antibodies and XTEN polypeptides.Chemical science · 2022Article
- Human monoclonal antibodies againsteLife · 2022Article
- Monoclonal antibodies effectively potentiate complement activation and phagocytosis ofFrontiers in immunology · 2022Article
- Structural basis for SdgB- and SdgA-mediated glycosylation of staphylococcal adhesive proteins.Acta crystallographica. Section D, Structural biology · 2021Article
- Proteinous Components of Neutrophil Extracellular Traps Are Arrested by the Cell Wall Proteins ofCells · 2021Article
- Impact of Glycan Linkage toACS infectious diseases · 2021Article
- Article
- Identification of Three Clf-Sdr Subfamily Proteins inFrontiers in microbiology · 2021Article
- Article
- Processivity in Bacterial Glycosyltransferases.ACS chemical biology · 2020Review
- Streptococcal Serine-Rich Repeat Proteins in Colonization and Disease.Frontiers in microbiology · 2020Review
- Revisiting Bap Multidomain Protein: More Than Sticking Bacteria Together.Frontiers in microbiology · 2020Review
Corrections and comments
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Authors and funding
29 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Infection of host tissues by Staphylococcus aureus and S. epidermidis requires an unusual family of staphylococcal adhesive proteins that contain long stretches of serine-aspartate dipeptide-repeats (SDR). The prototype member of this family is clumping factor A (ClfA), a key virulence factor that mediates adhesion to host tissues by binding to extracellular matrix proteins such as fibrinogen. However, the biological siginificance of the SDR-domain and its implication for pathogenesis remain poorly understood. Here, we identified two novel bacterial glycosyltransferases, SdgA and SdgB, which modify all SDR-proteins in these two bacterial species. Genetic and biochemical data demonstrated that these two glycosyltransferases directly bind and covalently link N-acetylglucosamine (GlcNAc) moieties to the SDR-domain in a step-wise manner, with SdgB appending the sugar residues proximal to the target Ser-Asp repeats, followed by additional modification by SdgA. GlcNAc-modification of SDR-proteins by SdgB creates an immunodominant epitope for highly opsonic human antibodies, which represent up to 1% of total human IgG. Deletion of these glycosyltransferases renders SDR-proteins vulnerable to proteolysis by human neutrophil-derived cathepsin G. Thus, SdgA and SdgB glycosylate staphylococcal SDR-proteins, which protects them against host proteolytic activity, and yet generates major eptopes for the human anti-staphylococcal antibody response, which may represent an ongoing competition between host and pathogen.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.