ArticleInfection and immunity2008
Amylase-binding protein B of Streptococcus gordonii is an extracellular dipeptidyl-peptidase.
Article in Infection and immunity, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 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
17 citing papers in PubMed, 25 citations in OpenAlex.
- Glucose Phosphotransferase System Modulates Pyruvate Metabolism, Bacterial Fitness, and Microbial Ecology in Oral Streptococci.Journal of bacteriology · 2023Article
- Proteomic response inJournal of oral microbiology · 2021Article
- Amylases: Biofilm Inducer or Biofilm Inhibitor?Frontiers in cellular and infection microbiology · 2021Review
- Uncovering Roles of Streptococcus gordonii SrtA-Processed Proteins in the Biofilm Lifestyle.Journal of bacteriology · 2020Article
- Genome sequencing and analysis ofPeerJ · 2019Article
- Comparative genomics and evolution of the amylase-binding proteins of oral streptococci.BMC microbiology · 2017Article
- Article
- Dynamics of the Streptococcus gordonii Transcriptome in Response to Medium, Salivary α-Amylase, and Starch.Applied and environmental microbiology · 2015Article
- Draft genome sequences of 18 oral streptococcus strains that encode amylase-binding proteins.Genome announcements · 2015Article
- Mass Spectrometric Analysis of Whole Secretome and Amylase-precipitated Secretome Proteins fromJournal of proteomics & bioinformatics · 2014Article
- Implications of salivary protein binding to commensal and pathogenic bacteria.Journal of oral biosciences · 2013Article
- Expression of recombinant streptokinase from streptococcus pyogenes and its reaction with infected human and murine sera.Iranian journal of basic medical sciences · 2013Article
- Taking the starch out of oral biofilm formation: molecular basis and functional significance of salivary α-amylase binding to oral streptococci.Applied and environmental microbiology · 2013Review
- Streptococcus mutans out-competes Streptococcus gordonii in vivo.Journal of dental research · 2012Article
- Response of fatty acid synthesis genes to the binding of human salivary amylase by Streptococcus gordonii.Applied and environmental microbiology · 2012Article
- Identification and characterization of amylase-binding protein C from Streptococcus mitis NS51.Molecular oral microbiology · 2010Article
- Streptococcus adherence and colonization.Microbiology and molecular biology reviews : MMBR · 2009Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The oral commensal bacterium Streptococcus gordonii interacts with salivary amylase via two amylase-binding proteins, AbpA and AbpB. Based on sequence analysis, the 20-kDa AbpA protein is unique to S. gordonii, whereas the 82-kDa AbpB protein appears to share sequence homology with other bacterial dipeptidases. The aim of this study was to verify the peptidase activity of AbpB and further explore its potential functions. The abpB gene was cloned, and histidine-tagged AbpB (His-AbpB) was expressed in Escherichia coli and purified. Its amylase-binding activity was verified in an amylase ligand binding assay, and its cross-reactivity was verified with an anti-AbpB antibody. Both recombinant His-AbpB and partially purified native AbpB displayed dipeptidase activity and degraded human type VI collagen and fibrinogen, but not salivary amylase. Salivary amylase precipitates not only AbpA and AbpB but also glucosyltransferase G (Gtf-G) from S. gordonii supernatants. Since Streptococcus mutans also releases Gtf enzymes that could also be involved in multispecies plaque interactions, the effect of S. gordonii AbpB on S. mutans Gtf-B activity was also tested. Salivary amylase and/or His-AbpB caused a 1.4- to 2-fold increase of S. mutans Gtf-B sucrase activity and a 3- to 6-fold increase in transferase activity. An enzyme-linked immunosorbent assay verified the interaction of His-AbpB and amylase with Gtf-B. In summary, AbpB demonstrates proteolytic activity and interacts with and modulates Gtf activity. These activities may help explain the crucial role AbpB appears to play in S. gordonii oral colonization.
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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.