Identification and analysis of the amylase-binding protein B (AbpB) and gene (abpB) from Streptococcus gordonii

Li, L

doi:10.1016/s0378-1097(02)00678-x

Cited by 10 publications

(28 citation statements)

References 16 publications

(36 reference statements)

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“…The 20 kDa AbpA appears to be the major protein responsible for amylase binding to the cell surface (Rogers et al, 1998). The 82 kDa AbpB interacts specifically with amylase, but does not appear essential for amylase binding to the cell surface of S. gordonii in vitro (Li et al, 2002). In the present work we tested strains of S. gordonii made deficient in one or both of these proteins in a rat model of human oral colonization.…”

Section: Discussionmentioning

confidence: 95%

“…The strains used in the present study and their relevant phenotypes are listed in Table 1. The constructions of the mutants have been detailed previously (Rogers et al, 1998(Rogers et al, , 2001Li et al, 2002). All strains were maintained at 270 uC in 15 % glycerolsupplemented fluid thioglycollate medium (Difco) supplemented with meat extract and excess CaCO 3 (TMM).…”

Section: Methodsmentioning

confidence: 99%

“…As an additional screen for undetected phenotypic changes other than those desired, comparisons of growth rates in chemically defined medium [FMC (Terleckji et al, 1975) supplemented with 2 % glucose] were made for strains Challis-S, Challis-ST, Challis-SE and Challis-STE at 37 uC using a Bausch and Lomb Spectronic 21 spectrophotometer with 1?5 cm light path. Additionally, bacterial proteins were extracted from the cell surface with SDS and culture supernatants were evaluated by SDS-PAGE stained with Coomassie brilliant blue, and by Western blots probed with antiserum to S. gordonii to seek any changes of protein profiles other than expected ones (Rogers et al, 1998;Li et al, 2002).…”

Section: Methodsmentioning

confidence: 99%

“…The experiments compared colonization and persistence of wild-type S. gordonii (FAS4-S or Challis-S) with their respective abpA mutants, termed FAS4-ST and Challis-ST (Rogers et al, 2001;Li et al, 2002). An abpB mutant (Challis-SE) was constructed from the more transformable strain, Challis-S, as was a double mutant (Challis-STE) defective in both abpA and abpB (Li et al, 2002). We shall detail those two experiments that are the most informative and complete with respect to the Challis-S mutants.…”

Section: Methodsmentioning

confidence: 99%

“…Recently, the genes (abpA and abpB) encoding these two amylase-binding proteins have been identified, cloned and sequenced (Rogers et al, 1998(Rogers et al, , 2001Brown et al, 1999;Li et al, 2002). They are recognized in the recent draft publication of the genome of S. gordonii (http://www.tigr.org).…”

Section: Introductionmentioning

confidence: 99%

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Amylase-binding proteins A (AbpA) and B (AbpB) differentially affect colonization of rats' teeth by Streptococcus gordonii

et al. 2003

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Streptococcus gordonii produces two a-amylase-binding proteins, AbpA and AbpB, that have been extensively studied in vitro. Little is known, however, about their significance in oral colonization and cariogenicity (virulence). To clarify these issues, weanling specific pathogen-free Osborne-Mendel rats, TAN : SPFOM(OM)BR, were inoculated either with wild-type strains FAS4-S or Challis-S or with strains having isogenic mutations of abpA, abpB, or both, to compare their colonization abilities and persistence on the teeth. Experiments were done with rats fed a sucrose-rich diet containing low amounts of starch or containing only starch. The mutants and wild-types were quantified in vivo and carious lesions were scored. In 11 experiments, S. gordonii was a prolific colonizer of the teeth when rats were fed the sucrose (with low starch)-supplemented diet, often dominating the flora. Sucrose-fed rats had several-fold higher recoveries of inoculants than those eating the sucrose-free, starch-supplemented diet, regardless of inoculant type. The strain defective in AbpB could not colonize teeth of starch-only-eating rats, but could colonize rats if sucrose was added to the diet. Strains defective in AbpA surprisingly colonized better than their wild-types. A double mutant deficient in both AbpA and AbpB (abpA/abpB) colonized like its wild-type. Wild-types FAS4-S and Challis-S had no more than marginal cariogenicity. Notably, in the absence of AbpA, cariogenicity was slightly augmented. Both the rescue of colonization by the AbpB " mutant and the augmentation of colonization by AbpA " mutant in the presence of dietary sucrose suggested additional amylase-binding protein interactions relevant to colonization. Glucosyltransferase activity was greater in mutants defective in abpA and modestly increased in the abpB mutant. It was concluded that AbpB is required for colonization of teeth of starch-eating rats and its deletion is partially masked if rats eat a sucrose-starch diet. AbpA appears to inhibit colonization of the plaque biofilm in vivo. This unexpected effect in vivo may be associated with interaction of AbpA with glucosyltransferase or with other colonization factors of these cells. These data illustrate that the complex nature of the oral environment may not be adequately modelled by in vitro systems.

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Section: Discussionmentioning

confidence: 95%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Amylase-binding proteins A (AbpA) and B (AbpB) differentially affect colonization of rats' teeth by Streptococcus gordonii

et al. 2003

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Lactobacillus plantarum for oral peptide delivery

Varmanen

Han

et al. 2007

Oral Microbiology and Immunology

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The transformed L. lactis, L. brevis, L. johnsonii, L. murinus, and the endogenous murine lactobacillus strain failed to persist in the mouth. Transformed L. plantarum, however, persisted in the mouth and comprised up to 25% of the total lactobacilli at 18 h and 10% at 24 h after feeding. L. plantarum recovered after feeding retained its ability to secrete beta-lactamase into culture medium efficiently. Beta-lactamase activity could be detected in oral secretions at 8 h after feedings. After repeated feedings, however, the L. plantarum containing pKTH2121 gradually lost its ability to persist after feedings. This experiment demonstrates that L. plantarum can transiently colonize the oral mucosa in large numbers, while continuously secreting foreign proteins, raising the possibility of using lactobacilli as a vector for delivery of oral mucosal peptides.

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Identification and characterization of amylase-binding protein C fromStreptococcus mitisNS51

Vorrasi¹,

Chaudhuri²,

Haase³

et al. 2010

Molecular Oral Microbiology

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SUMMARYA substantial proportion of the streptococcal species found in dental plaque biofilms are able to interact with the abundant salivary enzyme α-amylase. These streptococci produce proteins that specifically bind amylase. An important plaque species, Streptococcus mitis, secretes a 36-kDa amylase binding protein into the extracellular milieu. Proteins precipitated from S. mitis NS51 cell culture supernatant by the addition of purified salivary amylase were separated by SDS-PAGE, transferred to a membrane, and a prominent 36-kDa band was cut from the membrane and sequencedto yield N-terminal amino acid sequence DSQAQYSNGV. Search of the S. mitis genome sequence database revealed a single open reading frame containing this sequence, and the gene was amplified from S. mitis genomic DNA polymerase chain reaction. The coding region of this ORF, designated amylase-binding protein C (AbpC), was cloned into an Escherichia coli expression vectorand the recombinant AbpC protein (rAbpC) was purified from the soluble fraction of E. coli cell lysate. Purified AbpC was found to interact with immobilized amylase, thus confirming AbpC as a new streptococcal amylase-binding protein. Keywords Dental plaque; SalivaInteractions between salivary components and oral bacteria are thought to play an important role in the ecology of the oral biofilms (5,13,14). Amylase, the most abundant enzyme in human saliva, specifically binds to several species of oral streptococci (4,6,8,15). One or more bacterial receptors mediate the binding of amylase to the streptococcal surface (3,16). Much of our current knowledge about the mechanism of interaction of amylase with oral bacteria derives from the study of two amylase-binding proteins (AbpA and AbpB) produced by Streptococcus gordonii (2,9,12). Both of these proteins appear to be expressed transiently on the cell surface before being released into the extracellular milieu in soluble form. AbpA is a 20-kDa protein that is unique to S. gordonii, and is essential for amylase binding to the cell surface (12). AbpB, a 82-kDa AbpB protein that shares sequence homology with other bacterial dipeptidases, and appears to play a crucial role in S. gordonii oral colonization (1,20). To date, however, little is known about the amylase-binding proteins of other species of oral streptococci.Streptococcus mitis NS51 releases a 36-kDa amylase-binding protein into the culture medium during growth (7). The goal of this study was to identify the gene encoding this protein, express and purify the polypeptide andverify its function in vitro.This information

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Identification and analysis of the amylase-binding protein B (AbpB) and gene (abpB) from Streptococcus gordonii

Cited by 10 publications

References 16 publications

Amylase-binding proteins A (AbpA) and B (AbpB) differentially affect colonization of rats' teeth by Streptococcus gordonii

Amylase-binding proteins A (AbpA) and B (AbpB) differentially affect colonization of rats' teeth by Streptococcus gordonii

Lactobacillus plantarum for oral peptide delivery

Identification and characterization of amylase-binding protein C fromStreptococcus mitisNS51

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