ArticleJournal of bacteriology2014
Serotype-converting bacteriophage SfII encodes an acyltransferase protein that mediates 6-O-acetylation of GlcNAc in Shigella flexneri O-antigens, conferring on the host a novel O-antigen epitope.
Article in Journal of bacteriology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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18 citing papers in PubMed, 25 citations in OpenAlex.
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- Article
- Rapid generation of Shigella flexneri GMMA displaying natural or new and cross-reactive O-Antigens.NPJ vaccines · 2022Article
- Bacteriophage Sf6 host range mutant that infects Shigella flexneri serotype 2a2 strains.FEMS microbiology letters · 2022Article
- Identification of critical residues of O-antigen-modifying O-acetyltransferase B (OacB) of Shigella flexneri.BMC molecular and cell biology · 2022Article
- Diverse functions for acyltransferase-3 proteins in the modification of bacterial cell surfaces.Microbiology (Reading, England) · 2022Article
- Impact of O-Acetylation onMicroorganisms · 2021Article
- Rationalizing the design of a broad coverage Shigella vaccine based on evaluation of immunological cross-reactivity among S. flexneri serotypes.PLoS neglected tropical diseases · 2021Article
- Influence of Shigella flexneri 2a O Antigen Acetylation on Its Bacteriophage Sf6 Receptor Activity and Bacterial Interaction with Human Cells.Journal of bacteriology · 2020Article
- Article
- PCR-Based Method for Shigella flexneri Serotyping: International Multicenter Validation.Journal of clinical microbiology · 2019Article
- Metagenomic Profiling of Microbial Pathogens in the Little Bighorn River, Montana.International journal of environmental research and public health · 2019Article
- Prophages in Salmonella enterica: a driving force in reshaping the genome and physiology of their bacterial host?Molecular microbiology · 2019Review
- Novel phages of healthy skin metaviromes from South Africa.Scientific reports · 2018Article
- Molecular basis for the structural diversity in serogroup O2-antigen polysaccharides inThe Journal of biological chemistry · 2018Article
- Article
- O-acetylation controls the glycosylation of bacterial serine-rich repeat glycoproteins.The Journal of biological chemistryArticle
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Shigella flexneri O-antigen is an important and highly variable cell component presented on the outer leaflet of the outer membrane. Most Shigella flexneri bacteria share an O-antigen backbone composed of →2)-α-L-Rhap(III)-(1→2)-α-L-Rhap(II)-(1→3)-α-L-Rhap(I)-(1→3)-β-D-GlcpNAc-(1→ repeats, which can be modified by adding various chemical groups to different sugars, giving rise to diverse O-antigen structures and, correspondingly, to various serotypes. The known modifications include glucosylation on various sugar residues, O-acetylation on Rha(I) or/and Rha(III), and phosphorylation with phosphoethanolamine on Rha(II) or/and Rha(III). Recently, a new O-antigen modification, namely, O-acetylation at position 6 of N-acetylglucosamine (GlcNAc), has been identified in S. flexneri serotypes 2a, 3a, Y, and Yv. In this study, the genetic basis of the 6-O-acetylation of GlcNAc in S. flexneri was elucidated. An O-acyltransferase gene designated oacD was found to be responsible for this modification. The oacD gene is carried on serotype-converting bacteriophage SfII, which is integrated into the host chromosome by lysogeny to form a prophage responsible for the evolvement of serotype 2 of S. flexneri. The OacD-mediated 6-O-acetylation also occurs in some other S. flexneri serotypes that carry a cryptic SfII prophage with a dysfunctional gtr locus for type II glucosylation. The 6-O-acetylation on GlcNAc confers to the host a novel O-antigen epitope, provisionally named O-factor 10. These findings enhance our understanding of the mechanisms of the O-antigen variation and enable further studies to understand the contribution of the O-acetylation to the antigenicity and pathogenicity of S. flexneri.
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