ArticleJournal of bacteriology2009
Characterization of the Streptococcus pneumoniae BgaC protein as a novel surface beta-galactosidase with specific hydrolysis activity for the Galbeta1-3GlcNAc moiety of oligosaccharides.
Article in Journal of bacteriology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 45 citations in OpenAlex.
- Function and Structure ofJournal of applied glycoscience · 2023Article
- Role ofFrontiers in cellular and infection microbiology · 2023Review
- The Two-Component System 09 Regulates Pneumococcal Carbohydrate Metabolism and Capsule Expression.Microorganisms · 2021Article
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- Regulation of pneumococcal epigenetic and colony phases by multiple two-component regulatory systems.PLoS pathogens · 2020Article
- An enzymatic pathway in the human gut microbiome that converts A to universal O type blood.Nature microbiology · 2019Article
- Two complementary α-fucosidases fromThe Journal of biological chemistry · 2019Article
- Cloning, purification and biochemical characterisation of a GH35 beta-1,3/beta-1,6-galactosidase from the mucin-degrading gut bacterium Akkermansia muciniphila.Glycoconjugate journal · 2018Article
- Article
- Molecular Characterization of N-glycan Degradation and Transport in Streptococcus pneumoniae and Its Contribution to Virulence.PLoS pathogens · 2017Article
- ManLMN is a glucose transporter and central metabolic regulator in Streptococcus pneumoniae.Molecular microbiology · 2016Article
- N-acetylglucosamine-Mediated Expression ofFrontiers in cellular and infection microbiology · 2016Article
- A Second β-Hexosaminidase Encoded in the Streptococcus pneumoniae Genome Provides an Expanded Biochemical Ability to Degrade Host Glycans.The Journal of biological chemistry · 2015Article
- A genomic approach to understand interactions between Streptococcus pneumoniae and its bacteriophages.BMC genomics · 2015Article
- Host glycan sugar-specific pathways in Streptococcus pneumoniae: galactose as a key sugar in colonisation and infection [corrected].PloS one · 2015Article
- Unravelling the multiple functions of the architecturally intricate Streptococcus pneumoniae β-galactosidase, BgaA.PLoS pathogens · 2014Article
- The β-galactosidase (BgaC) of the zoonotic pathogen Streptococcus suis is a surface protein without the involvement of bacterial virulence.Scientific reports · 2014Article
- Composition and development of oral bacterial communities.Periodontology 2000 · 2014Review
- A novel cold-adapted β-galactosidase isolated from Halomonas sp. S62: gene cloning, purification and enzymatic characterization.World journal of microbiology & biotechnology · 2013Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Streptococcus pneumoniae is a causative agent of high morbidity and mortality. Although sugar moieties have been recognized as ligands for initial contact with the host, only a few exoglycosidases have been reported to occur in S. pneumoniae. In this study, a putative beta-galactosidase, encoded by the bgaC gene of S. pneumoniae, was characterized for its enzymatic activity and virulence. The recombinant BgaC protein, expressed and purified from Escherichia coli, was found to have a highly regiospecific and sugar-specific hydrolysis activity for the Galbeta1-3-GlcNAc moiety of oligosaccharides. Interestingly, the BgaC hydrolysis activity was localized at the cell surface of S. pneumoniae, indicating that BgaC is expressed as a surface protein although it does not have a typical signal sequence or membrane anchorage motif. The surface localization of BgaC was further supported by immunofluorescence microscopy analysis using an antibody raised against BgaC and by a reassociation assay with fluorescein isothiocyanate-labeled BgaC. Although the bgaC deletion mutation did not significantly attenuate the virulence of S. pneumoniae in vivo, the bgaC mutant strain showed relatively low numbers of viable cells compared to the wild type after 24 h of infection in vivo, whereas the mutant showed higher colonization levels at 6 and 24 h postinfection in vivo. Our data strongly indicate for the first time that S. pneumoniae bgaC encodes a surface beta-galactosidase with high substrate specificity that is significantly associated with the infection activity of pneumococci.
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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.