Four gbpC Gene Homologues in Streptococcus sobrinus

Satō, Yutaka; Ishikawa, Ayako; Okamoto-Shibayama, Kazuko; Takada, Kazuko; Hirasawa, Masatomo

doi:10.1016/s1349-0079(07)80026-0

Cited by 4 publications

(11 citation statements)

References 18 publications

(15 reference statements)

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“…However, we cannot exclude the possibility of causative genes of dextran-induced agglutination other than dblB. It has been reported that in S. sobrinus strain 6715, dextran-binding activities are observed in GbpC2 and DblA as DblB, but there is no activity in GbpC1 (Sato et al, 2007). Thus, it is presumed that GbpC2 and DblA, but not GbpC1, of S. sobrinus and probably S. criceti, are independently involved in dextraninduced agglutination.…”

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confidence: 87%

Molecular characterization of the dextran-binding lectin B gene dblB of Streptococcus criceti in Streptococcus mutans strain GS-5 with mutations in both gbpC and spaP genes

2014

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Streptococcus mutans, a cariogenic agent, has a glucan-binding protein gene, gbpC, and S. criceti possesses four gbpC homologs, including dblA and dblB, as does S. sobrinus. The S. criceti dblB gene encodes a 1,717-amino-acid protein having two repetitive alanine-rich and proline-rich regions and an LPXTG motif, which is recognized by the sortase SrtA, near the C terminus. Reverse transcription-PCR analysis indicated no cotranscription of the dblA and dblB genes of S. criceti. As we could not obtain a dblB mutant of S. criceti, the dblB gene was characterized in S. mutans strain GS-5, which has genetic mutations in both gbpC and spaP genes and shows an inability to agglutinate triggered by dextran. A dextran-induced agglutination assay showed that S. mutans cells carrying dblB agglutinated in the presence of dextran. A hydrophobicity assay showed that the cells containing dblB were hydrophobic. A biofilm formation assay showed that the dblB gene was associated with biofilm formation by cells cultivated in brain heart infusion broth supplemented with glucose and maltose, but not sucrose. Nucleotide sequence analysis of the S. criceti strains studied revealed a frameshift mutation in the srtA gene encoding sortase, but intact dblA and dblB genes were found in dextran-induced agglutination-negative strains, whereas intact dblA, dblB and srtA genes were found in dextran-induced agglutination-positive strains. These results suggest the cell-surface localization of dblA and dblB gene products by SrtA and the responsibility of dblB for dextran-induced agglutination, cellsurface hydrophobicity and biofilm formation in S. criceti.

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confidence: 87%

Molecular characterization of the dextran-binding lectin B gene dblB of Streptococcus criceti in Streptococcus mutans strain GS-5 with mutations in both gbpC and spaP genes

2014

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“…We previously identified the tandemly located gbpC1-gbpC2 and dblA-dblB genes in S. sobrinus 10,11) . Paralogous genes are often organized in a tandem localization following unequal crossover recombination with highly similar sequences between the two daughter DNAs during replication in a species.…”

Section: Discussionmentioning

confidence: 99%

“…In addition to these two factors, Streptococcus mutans and Streptococcus sobrinus express other virulence-related factors in human, including the glucan-binding cell wall-anchored proteins encoded by the glucan-binding protein C (gbpC ) and dextran-binding lectin (dbl ) genes 10,12) . The gbpC gene was initially identified as the gene solely involved in dextran (α-1,6 glucan)-dependent aggregation of A part of this work was given as a poster presentation by YK at the 87th IADR meeting held in Miami, Fla., USA on April 2, 2009 as a 2009 IADR/Unilever Hatton Divisional Awardee ( Junior Category).…”

Section: Introductionmentioning

confidence: 99%

gbpC Gene Repertoire Variation among Mutans Streptococci

Kojima

Okamoto-Shibayama

Satō

et al. 2012

Bull. Tokyo Dent. Coll.

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“…Four hundred microliters of supernatant fluid was obtained as a crude extract sample and its protein concentration was determined with DC protein assay reagents (BioRad, Hercules, CA, USA). SDS-PAGE was run with 2.5 µg of samples for Quick-CBB-PLUS (Wako Pure Chemical Industries, Osaka, Japan) staining and 0.4 µg of samples were used for Western blot analysis with previously prepared anti-GlgP serum (Operon Biotechnology, Tokyo, Japan) as described previously (16). …”

Section: Methodsmentioning

confidence: 99%

ThemalQgene is essential for starch metabolism inStreptococcus mutans

Satō

Okamoto-Shibayama

Azuma

2013

Journal of Oral Microbiology

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BackgroundThe malQ and glgP genes, respectively, annotated as putative 4-α-glucanotransferase and putative glycogen phosphorylase are located with a 29 nucleotide overlap on the Streptococcus mutans genome. We found that the glgP gene of this organism was induced with maltose, and the gene likely constituted an operon with the upstream gene malQ. This putative operon was negatively regulated with the malR gene located upstream from the malQ gene and a MalR-binding consensus sequence was found upstream of the malQ gene. S. mutans is not able to catabolize starch. However, this organism utilizes maltose degraded from starch in the presence of saliva amylase. Therefore, we hypothesized that the MalQ/GlgP system may participate in the metabolism of starch-degradation products.MethodsA DNA fragment amplified from the malQ or glgP gene overexpressed His-tagged proteins with the plasmid pBAD/HisA. S. mutans malQ and/or glgP mutants were also constructed. Purified proteins were assayed for glucose-releasing and phosphorylase activities with appropriate buffers containing maltose, maltotriose, maltodextrin, or amylodextrin as a substrate, and were photometrically assayed with a glucose-6-phosphate dehydrogenase–NADP system.ResultsPurified MalQ protein released glucose from maltose and maltotriose but did not from either maltodextrin or amylodextrin. The purified GlgP protein did not exhibit a phosphorylase reaction with maltose or maltotriose but generated glucose-1-phosphate from maltodextrin and amylodextrin. However, the GlgP protein released glucose-1-phosphate from maltose and maltotriose in the presence of the MalQ protein. In addition, the MalQ enzyme activity with maltose released not only glucose but also produced maltooligosaccharides as substrates for the GlgP protein.ConclusionThese results suggest that the malQ gene encodes 4-α-glucanotransferase but not α-1,4-glucosidase activity. The malQ mutant could not grow in the presence of maltose as a carbon source, which suggests that the malQ gene is essential for the utilization of starch-degradation products.

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Four gbpC Gene Homologues in Streptococcus sobrinus

Cited by 4 publications

References 18 publications

Molecular characterization of the dextran-binding lectin B gene <i>dblB</i> of <i>Streptococcus criceti</i> in <i>Streptococcus mutans</i> strain GS-5 with mutations in both <i>gbpC</i> and <i>spaP</i> genes

Molecular characterization of the dextran-binding lectin B gene <i>dblB</i> of <i>Streptococcus criceti</i> in <i>Streptococcus mutans</i> strain GS-5 with mutations in both <i>gbpC</i> and <i>spaP</i> genes

gbpC Gene Repertoire Variation among Mutans Streptococci

ThemalQgene is essential for starch metabolism inStreptococcus mutans

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