ArticleInfection and immunity2000
Purification, characterization, and molecular analysis of the gene encoding glucosyltransferase from Streptococcus oralis.
Article in Infection and immunity, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 82 citations in OpenAlex.
- Article
- In Situ Raman Analysis of Biofilm Exopolysaccharides Formed inInternational journal of molecular sciences · 2023Article
- The findings of glucosyltransferase enzymes derived from oral streptococci.The Japanese dental science review · 2022Review
- Bacterial α-Glucan and Branching Sucrases from GH70 Family: Discovery, Structure-Function Relationship Studies and Engineering.Microorganisms · 2021Review
- A novel sialic acid-binding adhesin present in multiple species contributes to the pathogenesis of Infective endocarditis.PLoS pathogens · 2021Article
- Role of glucosyltransferase R in biofilm interactions between Streptococcus oralis and Candida albicans.The ISME journal · 2020Article
- Anti-biofilm activity of a novel pit and fissure self-adhesive sealant modified with metallic monomers.Biofouling · 2020Article
- Streptococcus oralis subsp.Infection and immunity · 2019Article
- Recent Progress of Basic Studies of Natural Products and Their Dental Application.Medicines (Basel, Switzerland) · 2018Review
- An Update on the Evolution of Glucosyltransferase (Frontiers in microbiology · 2018Article
- The sixth sensor: A Candida albicans biofilm master regulator that responds to inter-kingdom interactions.Virulence · 2017Article
- Biopolymers from lactic acid bacteria. Novel applications in foods and beverages.Frontiers in microbiology · 2015Review
- Global analysis of saliva as a source of bacterial genes for insights into human population structure and migration studies.BMC evolutionary biology · 2014Article
- Streptococcal co-infection augments Candida pathogenicity by amplifying the mucosal inflammatory response.Cellular microbiology · 2014Article
- Quorum sensing in group A Streptococcus.Frontiers in cellular and infection microbiology · 2014Review
- Article
- The exopolysaccharide matrix modulates the interaction between 3D architecture and virulence of a mixed-species oral biofilm.PLoS pathogens · 2012Article
- Streptococcus mutans protein synthesis during mixed-species biofilm development by high-throughput quantitative proteomics.PloS one · 2012Article
- Evolution of cariogenic character in Streptococcus mutans: horizontal transmission of glycosyl hydrolase family 70 genes.Scientific reports · 2012Article
- Novel epitopic region of glucosyltransferase B from Streptococcus mutans.Clinical and vaccine immunology : CVI · 2011Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Streptococcus oralis is a member of the oral streptococcal family and an early-colonizing microorganism in the oral cavity of humans. S. oralis is known to produce glucosyltransferase (GTase), which synthesizes glucans from sucrose. The enzyme was purified chromatographically from a culture supernatant of S. oralis ATCC 10557. The purified enzyme, GTase-R, had a molecular mass of 173 kDa and a pI of 6.3. This enzyme mainly synthesized water-soluble glucans with no primer dependency. The addition of GTase markedly enhanced the sucrose-dependent resting cell adhesion of Streptococcus mutans at a level similar to that found in growing cells of S. mutans. The antibody against GTase-R inhibited the glucan-synthesizing activities of Streptococcus gordonii and Streptococcus sanguis, as well as S. oralis. The N-terminal amino acid sequence of GTase-R exhibited no similarities to known GTase sequences of oral streptococci. Using degenerate PCR primers, an 8.1-kb DNA fragment, carrying the gene (gtfR) coding for GTase-R and its regulator gene (rgg), was cloned and sequenced. Comparison of the deduced amino acid sequence revealed that the rgg genes of S. oralis and S. gordonii exhibited a close similarity. The gtfR gene was found to possess a species-specific nucleotide sequence corresponding to the N-terminal 130 amino acid residues. Insertion of erm or aphA into the rgg or gtfR gene resulted in decreased GTase activity by the organism and changed the colony morphology of these transformants. These results indicate that S. oralis GTase may play an important role in the subsequent colonizing of mutans streptoccoci.
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Registered trials
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