ArticleJournal of bacteriology2013
Biochemical activities of Streptococcus pneumoniae serotype 2 capsular glycosyltransferases and significance of suppressor mutations affecting the initiating glycosyltransferase Cps2E.
Article in Journal of bacteriology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 47 citations in OpenAlex.
- Intra-serotype variation ofMicrobiology spectrum · 2025Article
- Determining glycosyltransferase functional order via lethality due to accumulated O-antigen intermediates, exemplified withApplied and environmental microbiology · 2024Article
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- NADNature communications · 2023Article
- Mapping the architecture of the initiating phosphoglycosyl transferase frombioRxiv : the preprint server for biology · 2023Article
- A generalizable protocol for expression and purification of membrane-bound bacterial phosphoglycosyl transferases in liponanoparticles.Protein expression and purification · 2023Article
- Rhamnose-Containing Compounds: Biosynthesis and Applications.Molecules (Basel, Switzerland) · 2022Review
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- The bacterial tyrosine kinase system CpsBCD governs the length of capsule polymers.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- The surprising structural and mechanistic dichotomy of membrane-associated phosphoglycosyl transferases.Biochemical Society transactions · 2021Review
- S1 Domain RNA-Binding Protein CvfD Is a New Posttranscriptional Regulator That Mediates Cold Sensitivity, Phosphate Transport, and Virulence in Streptococcus pneumoniae D39.Journal of bacteriology · 2020Article
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- Progress toward a group B streptococcal vaccine.Human vaccines & immunotherapeutics · 2018Article
- Molecular Cloning, Expression and Characterization of Oenococcus oeni Priming Glycosyltransferases.Molecular biotechnology · 2017Article
- Integrated proteomic and metabolomic analysis reveals that rhodomyrtone reduces the capsule in Streptococcus pneumoniae.Scientific reports · 2017Article
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- Engineering and Dissecting the Glycosylation Pathway of a Streptococcal Serine-rich Repeat Adhesin.The Journal of biological chemistry · 2016Article
- Interrupting Biosynthesis of O Antigen or the Lipopolysaccharide Core Produces Morphological Defects in Escherichia coli by Sequestering Undecaprenyl Phosphate.Journal of bacteriology · 2016Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The capsular polysaccharide (CPS) is essential for Streptococcus pneumoniae virulence. Its synthesis requires multiple enzymes, and defects that block completion of the pathway can be lethal in the absence of secondary suppressor mutations. In this study, we examined the functions of three capsular glycosyltransferases (Cps2F, Cps2G, and Cps2I) involved in serotype 2 CPS synthesis, whose deletions select for secondary mutations. We demonstrate that Cps2F is a rhamnosyltransferase that catalyzes addition of the third and fourth sugars in the capsule repeat unit, while Cps2G adds the fifth sugar (glucose). Addition of the terminal residue (glucuronic acid) could not be detected; however, activities of the other glycosyltransferases together with bioinformatic analyses suggest that this step is mediated by Cps2I. Most of the secondary suppressor mutations resulting from loss of these enzymes occur in cps2E, the gene encoding the initiating glycosyltransferase. Examination of the 69 S. pneumoniae serotypes containing Cps2E homologues yielded a consensus amino acid sequence for this protein and demonstrated that there is a highly significant association between the residues that are 100% conserved and those altered by suppressor mutations. Cps2E contains an extracytoplasmic loop whose function is unknown. Among our collection of mutants, six contained missense mutations affecting amino acids in the extracytoplasmic loop. These residues are highly conserved among S. pneumoniae Cps2E homologues, and mutations therein severely reduced CPS synthesis and Cps2E activity. The critical functions of these amino acids suggest a role for the Cps2E extracytoplasmic loop in initiation, and possibly regulation, of capsule synthesis.
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