ArticleProceedings of the National Academy of Sciences of the United States of America2004
Discovery and characterization of sialic acid O-acetylation in group B Streptococcus.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers.
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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.
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Who cites it
87 citing papers in PubMed, 151 citations in OpenAlex.
- Protective meningococcal capsular polysaccharide epitopes and the role of O acetylation.Clinical and vaccine immunology : CVI · 2007Trial
- Type VII secretion system promotes Streptococcus agalactiae virulence through magnesium acquisition and capsule maintenance.Veterinary research · 2026Article
- Identification of interbacterial adhesion between oral Schaalia species and streptococcal serine-rich repeat glycoproteins.FEMS microbiology letters · 2026Article
- Virulence and pathogenicity of group BVirulence · 2025Review
- The serine protease HtrA regulates Group B Streptococcus virulence and affects the host response to infection.PLoS pathogens · 2025Article
- Surface-Controlled Sialoside-Based Biosensing of Viral and Bacterial Neuraminidases.Langmuir : the ACS journal of surfaces and colloids · 2024Article
- Effect of Side-Chain Functional Groups in the Immunogenicity of Bacterial Surface Glycans.Molecules (Basel, Switzerland) · 2023Review
- Innovative Metrics for Reporting and Comparing the Glycan Structural Profile in Biotherapeutics.Molecules (Basel, Switzerland) · 2023Article
- Biocatalysis versus Molecular Recognition in Sialoside-Selective Neuraminidase Biosensing.ACS chemical biology · 2023Article
- Development and applications of sialoglycan-recognizing probes (SGRPs) with defined specificities: exploring the dynamic mammalian sialoglycome.Glycobiology · 2022Article
- Sweet impersonators: Molecular mimicry of host glycans by bacteria.Glycobiology · 2022Review
- Article
- Development and Immunogenicity of a Prototype Multivalent Group BACS infectious diseases · 2021Article
- Sialic acid O-acetylation: From biosynthesis to roles in health and disease.The Journal of biological chemistry · 2021Review
- Review
- Glycan cross-feeding supports mutualism between Fusobacterium and the vaginal microbiota.PLoS biology · 2020Article
- Glycoengineering of Natural Killer Cells with CD22 Ligands for Enhanced Anticancer Immunotherapy.ACS central science · 2020Article
- C-Type Lectin Receptors in Host Defense Against Bacterial Pathogens.Frontiers in cellular and infection microbiology · 2020Review
- Dual actions of group BProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Surface Structures of Group BMicrobiology spectrum · 2019Review
27 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Group B Streptococcus (GBS) is the leading cause of human neonatal sepsis and meningitis. The GBS capsular polysaccharide is a major virulence factor and the active principle of vaccines in phase II trials. All GBS capsules have a terminal alpha 2-3-linked sialic acid [N-acetylneuraminic acid (Neu5Ac)], which interferes with complement-mediated killing. We show here that some of the Neu5Ac residues of the GBS type III capsule are O-acetylated at carbon position 7, 8, or 9, a major modification evidently missed in previous studies. Data are consistent with initial O-acetylation at position 7, and subsequent migration of the O-acetyl ester at positions 8 and 9. O-acetylation was also present on several other GBS serotypes (Ia, Ib, II, V, and VI). Deletion of the CMP-Neu5Ac synthase gene neuA by precise, in-frame allelic replacement gave intracellular accumulation of O-acetylated Neu5Ac, whereas overexpression markedly decreased O-acetylation. Given the known GBS Neu5Ac biosynthesis pathway, these data indicate that O-acetylation occurs on free Neu5Ac, competing with the CMP-Neu5Ac synthase. O-acetylation often generates immunogenic epitopes on bacterial capsular polysaccharides and can modulate human alternate pathway complement activation. Thus, our discovery has important implications for GBS pathogenicity, immunogenicity, and vaccine design.
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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.