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PubMed1990

Colonization resistance of defined bacterial plaques to Streptococcus mutans implantation on teeth in a model mouth.

We investigated the ability of Streptococcus mutans C67-1 to colonize simple bacterial plaques and the effects of age and stability of the pre-formed plaque on colonization resistance. Mixed-plaques of Actinomyces viscosus WVU627, 'Streptococcus mitior' LPA-1, and Veillonella dispar OMZ193 were grown on tooth segments, mounted back to back for simulation of approximal sites in a model mouth for 66 h. S. mutans C67-1 was either included in the original inoculum or super-inoculated onto the developing plaque. Inclusion of S. mutans C67-1 did not alter the total viable counts, but the proportional composition changed due to inter-species interactions. Colonization resistance of the mixed-plaque samples developed within 24 h, although S. mutans C67-1 was always able to colonize these stagnation sites. Colonization resistance of 24-hour plaque against a fresh isolate, S. mutans CP3, was also studied. There was greater colonization resistance by the basic plaque to this organism, compared with S. mutans C67-1, although the reasons for this were not clear. These initial experiments demonstrate the way in which the factors involved in bacterial colonization resistance in microbial films on teeth can be studied under controlled conditions.

Actinomyces↗
PubMed1994

Cloning and nucleotide sequencing of L-lactate dehydrogenase gene from Streptococcus thermophilus M-192.

The gene encoding L-lactate dehydrogenase (LDH) was cloned from an industrial dairy strain of Streptococcus thermophilus M-192 using a synthetic oligonucleotide probe based on the N-terminal amino acid sequence of the purified enzyme, and its nucleotide sequence was determined. The enzyme was deduced to have 328 amino acid residues with a molecular weight of 35,428 and found to have high sequence similarity to LDHs from other lactic acid bacteria (89.0% to Streptococcus mutans, 76.3% to Lactococcus lactis subsp. lactis, 67% to Lactobacillus casei, and 60% to Lactobacillus plantarum). The gene contained a promoter-like sequence similar to the Escherichia coli promoter consensus, and expression of the S. thermophilus LDH gene was observed in E. coli cells.

Amino Acid Sequence↗
PubMed2004

Expression of a functional single-chain Fv antibody on the surface of Streptococcus gordonii.

Gram-positive bacterium Streptococcus gordonii, a human oral commensal, was engineered to display a single-chain Fv (scFv) antibody fragment at the cell surface. The previously developed host-vector system allowed expression of the Guy's 13 scFv as a fusion with the streptococcal surface protein M6. Surface expression of the 515-amino acid M6/scFv fusion protein was confirmed by Western blot analysis on cellular fractions and flow cytometric analysis. Guy's 13 scFv was derived from the Guy's 13 monoclonal antibody, which was raised against streptococcal antigen I/II (SA I/II), the major adhesin of the caries-producing bacterium Streptococcus mutans. Surface plasmon resonance was used to test binding of scFv-expressing S. gordonii to SA I/II. Whole cells of recombinant S. gordonii were found to specifically bind to immobilised SA I/II and binding was inhibited by fluid-phase SA I/II in a dose-dependent manner. Production of a functional scFv in S. gordonii is the first step towards the development of genetically engineered commensal bacteria that, by colonizing mucosal surfaces, may provide the host with sustained delivery of recombinant antibodies.

Adhesins, Bacterial↗
PubMed1997

Carriage of multiresistant Streptococcus pneumoniae among children attending day-care centres in the Stockholm area.

To determine the prevalence of the asymptomatic carriage of drug-resistant Streptococcus pneumoniae (DRSP) by children attending day-care centres in the Stockholm area, nasopharyngeal swabs were cultured from 1129 children and 308 day-care personnel in 36 day-care centres during a 3-week period, from March to April 1995. Approximately 36% of the children were asymptomatic carriers of S. pneumoniae sensitive to penicillin and other antibiotics. The highest prevalence of nasopharyngeal carriage was found in the 2-year-old group (50%), whereas among the 4-year-old children colonization was observed in 42%, and among the 7-year-old children 21% were asymptomatic carriers of penicillin-sensitive S. pneumoniae. In 2 day-care centres, 4 and 5 children, respectively, were found to have DRSP strains in the nasopharynx. The same serotype of DRSP strain was found among the children attending the same day-care centre. During the same period, none of the staff were found to harbour DRSP in the nasopharynx, but 3% were asymptomatic carriers of penicillin-sensitive S. pneumoniae. The patterns of nasopharyngeal colonization by Haemophilus influenzae, Moraxella catarrhalis and Group A streptococci were also studied in 635 children during the same period. 42% of the nasal cultures yielded Moraxella, 32% H. influenzae and 2% Streptococcus pyogenes.

Carrier State↗
PubMed1991

Effect of milking without pulsation on teat duct colonization with Streptococcus agalactiae and penetrability to endotoxin.

Forty quarters of 10 cows were milked for a 9-d period with one of four treatments: 1) no liner pulsation, 2) conventional milking, 3) no pulsation for 4 d followed by conventional milking for 5 d, and 4) conventional milking for 4 d followed by milking without pulsation for 5 d. All teat orifices were inoculated with approximately .5 million cfu of Streptococcus agalactiae and Streptococcus dysgalactiae on d 1 and 5. Recoveries of Strep. agalactiae from the teat end were increased for teats milked without pulsation. Recoveries of Strep. dysgalactiae were lower than those of Strep. agalactiae and not increased by milking without pulsation. In a second experiment, teats of 20 cows were milked for a 15-d period with or without liner pulsation. For 10 successive milkings, all teats were inoculated with 1.0 micrograms of Escherichia coli endotoxin either immediately or 2.5 h after each milking. The frequency of endotoxin penetration, measured by the Wisconsin Mastitis Test, in pulsated quarters and in nonpulsated quarters was similar. For quarters milked without pulsation but not for pulsated quarters, inoculation of endotoxin immediately after milking led to greater incidence of teat duct penetration than for inoculation 2.5 h after milking.

Animals↗
PubMed1999

Relatedness of Streptococcus canis from canine streptococcal toxic shock syndrome and necrotizing fasciitis.

The emergence of streptococcal toxic shock syndrome (STSS) and necrotizing fasciitis (NF) in dogs caused by Streptococcus canis has been reported by our laboratory. Since clonal expansion is thought to be partially responsible for the spread of invasive strains of Streptococcus pyogenes in humans, the relatedness of 15 isolates of S. canis from canine STSS and/or NF was examined using pulsed field gel electrophoresis and biotyping; production of proteases and of a CAMP-like reaction were also examined. Only 2 of the 15 STSS and/or NF isolates were clonally related, suggesting that the emergence of canine STSS/NF is not the result of clonal expansion of one or more highly virulent strains of S. canis. All of the isolates produced proteases and demonstrated a CAMP-like reaction, which appear to be additional characteristics of S. canis.

Animals↗
PubMed1976

Susceptibility of Staphylococcus aureus, Streptococcus pyogenes and Diplococcus pneumoniae to antibiotics. Comparison of patterns in Poland and Federal Republic of Germany.

One hundred and eighty five strains of Gram-positive cocci were tested for susceptibility to 16 antibiotics, including some newer drugs, by agar dilution technique. Of these, 100 strains (50 each isolated in Poland and Germany) were Staphylococcus aureus, 55 Streptococcus pyogenes, and 30 Diplococcus pneumoniae. Previous investigations of streptococci and pneumococci isolated in Poland and Federal Republic of Grmany, revealed no differences in antibiotic-susceptibility patterns in both countries, which was not the case with staphylococci. Present study demonstrates further evidence for existence of differences in antibiotic-sensitivity of staphylococci, depending of their geographical origin, and presents actual state of susceptibility to antibiotics of Streptococcus pyogenes and Diplococcus pneumoniae.

Anti-Bacterial Agents↗
PubMed1990

Streptococcal-host interactions. Structural and functional analysis of a Streptococcus sanguis receptor for a human salivary glycoprotein.

Colonization of oral tissues by Streptococcus sanguis may be influenced by a mucin-like salivary glycoprotein (SAG) through a calcium-dependent interaction with a specific bacterial receptor. We report the nucleotide and deduced amino acid sequence of the S. sanguis receptor (SSP-5) and show that this protein may bind sialic acid residues of SAG. The SSP-5 protein contains three unique structural domains, two of which consist of repetitive amino acid sequences. The N-terminal domain is comprised of four tandem copies of an 82-residue repeat which exhibits homology to M protein of Streptococcus pyogenes. This region is highly charged and predicted to be alpha-helical. A second hydrophilic repetitive domain consists of three copies of a 39-amino acid sequence containing 30% proline flanked by nonrepetitive proline-rich sequence. The third domain consists of 48% proline and resides near the C terminus of the protein. Secondary structure analysis of the SSP-5 sequence also identified four potential helix-turn-helix motifs that resembled E-F hand calcium binding domains. The SSP-5 protein is highly homologous to a surface antigen expressed by the mutans streptococci and the domain structure of SSP-5 is conserved within this family of proteins. The interactions of SSP-5 and of intact S. sanguis with SAG were inhibited by neuraminidase digestion of the salivary glycoprotein and by simple sugars containing sialic acid, suggesting that sialic acid is the primary ligand involved in the binding reaction.

Amino Acid Sequence↗
PubMed1985

[Distribution of beta-hemolytic Streptococcus groups according to clinical sources and age group].

Distribution of beta haemolytic streptococcus groups was investigated according to their clinical sources and patients' age groups. The major portion of the isolates from the respiratory tract specimens and pus was group A, and from the urine samples and vagina swabs was groups B and G. In the pediatric age group, percentages of groups A and C were found to be higher than those of the adolescents while the rates of groups B, D and G were elevated in the adolescents. These colonization sites and the age group distribution differences between Streptococcus groups have clinical and epidemiological importance.

Adolescent↗
PubMed1979

Streptococcus bovis meningitis in a neonate.

Neonatal infections have been caused by Streptococcus bovis, a nonenterococcal group D Streptococcus. A recent case of neonatal meningitis caused by this organism prompted a literature review regarding appropriate antibiotic therapy. Although most reports suggested penicillin therapy alone for S bovis meningitis, isolates of this organism that were as resistant to the lethal effect of penicillin as the enterococcus have been recovered. Therefor, it was recommended that until the results of minimal inhibitory concentration and minimal bactericidal concentration tests are known both an aminoglycoside and a penicillin be used simultaneously. Proved susceptibility to the penicillin would justify discontinuation of the aminoglycoside therapy. Physicians caring for neonates with S bovis should be aware that some strains may be resistant to the lethal effect of penicillin.

Adult↗
PubMed2002

Self epitopes shared between human skeletal myosin and Streptococcus pyogenes M5 protein are targets of immune responses in active juvenile dermatomyositis.

OBJECTIVE: To identify self T cell epitopes associated with proinflammatory immune responses and clinically active juvenile dermatomyositis (juvenile DM). The target of our search for relevant epitopes was represented by amino acid sequences shared between human skeletal myosin and Streptococcus pyogenes M5 protein. The long-term objective of the project is to identify suitable targets for immunotherapy of the disease. METHODS: We used computerized algorithms to identify putative agretopes on both the human myosin and Streptococcus M5 proteins. Direct binding assays for homolog peptides were used to confirm such predictions. Antigenicity and functional cross-reactivity were evaluated by cytotoxicity assays and by measurement of cytokine levels. Specific T cells were isolated by T cell capture, and T cell receptor (TCR) V(beta) gene usage was identified by reverse transcriptase-polymerase chain reaction. RESULTS: We identified peptides that are targets of disease-specific cytotoxic T cell responses. T cell reactivity against the self peptides correlates with clinical signs of early, active myositis. Such reactivity is accompanied by production of proinflammatory cytokines, which may contribute to the damage. T cell cross-recognition of bacterial and human homologs was shown functionally as well as by sorting peptide-specific T cells and identifying oligoclonal and largely overlapping TCR V(beta) gene usage. CONCLUSION: These findings represent the first identification of a self epitope in juvenile DM, providing a potential candidate for antigen-specific immune therapy.

Bacterial Proteins↗
PubMed2006

Bactericidal effects of diode laser on Streptococcus mutans after irradiation through different thickness of dentin.

BACKGROUND AND OBJECTIVES: A reliable method to eradicate the bacteria of residual carious dentin has not yet been developed. The aim of this study was to evaluate the antibacterial effect of a diode laser on Streptococcus mutans through different thickness (500, 1,000, and 2,000 microm) of human dentin. The thermal effect of laser irradiation was also investigated. STUDY DESIGN/MATERIALS AND METHODS: Dentin specimens were inoculated with 2 microl of S. mutans on one side and irradiated by a diode laser on the other side with a power output ranging from 0.5 to 7 W. The laser tip was swept with the whole irradiation area of 7 mm x 3 mm at a speed of about 10 mm/second with a total irradiation time of 30 seconds. Cooling with distilled water (30 ml/minute) was applied simultaneously during laser irradiation. After laser irradiation, the bacteria was removed from the dentin surfaces and cultured for 48 hours at 37 degrees C anaerobically to assess the colony forming units (CFU) per ml. The morphology of the lased bacteria and the temperature rise during laser irradiation were observed by scanning electron microscope (SEM) and measured by thermocouple, respectively. RESULTS: The results revealed that 7 W of laser power could kill 97.7% of CFU through 500 microm thickness of dentin. However, the bactericidal efficiency was significantly reduced as the dentin thickness was increased. The morphological changes of lased bacteria ranged from less affected such as loss of their wall bands and existence of minicells to more severely degenerated, such as disintegration and fusion of cells with pores on the cell wall. Only the dentin specimens with a thickness of 500 microm exhibited a temperature rise greater than 5.5 degrees C after receiving 5 or 7 W of laser irradiation. CONCLUSIONS: A diode laser can eliminate the Streptococcus mutans of the residual carious dentin without inducing high pulpal temperature rise when the remaining dentin thickness is greater than 1 mm.

Dental Caries↗
PubMed2003

Application of immunoproteomics to analysis of post-translational processing of the antiphagocytic M protein of Streptococcus.

Post-translational modification of the antiphagocytic M1 protein of Streptococcus pyogenes can influence its binding properties for human immunoglobulin G subclasses and its invasive potential. Current methods of monitoring this modification event involve N-terminal sequencing and are cumbersome, slow and not amenable to routine analysis. In this study we demonstrate that surface enhanced laser desorption/ionization-time of flight mass spectrometry can be used to monitor modification of the M1 protein by the secreted bacterial cysteine protease, SpeB. This method, when combined with a specific antibody capture step provides a specific, rapid and sensitive assay for key virulence factors of the important human pathogen Streptococcus pyogenes.

Amino Acid Sequence↗
PubMed2006

Fibrinogen fragment D is necessary and sufficient to anchor a surface plasminogen-activating complex in Streptococcus pyogenes.

In this study, the importance of different domains of the fibrinogen molecule in the binding and assembly of a surface plasminogen (plgn) activator has been analyzed. This was achieved using SELDI technology that enabled dissociation of bound fragments from intact bacteria and accurate distinction between fibrinogen fragments based on their molecular mass. These studies indicate that Streptococcus pyogenes binds directly to human fibrinogen fragment D but not fragment E. The predominant surface proteins binding to fragment D were associated with the mrp gene product. Surface-associated fibrinogen fragment D was capable of anchoring a functional surface plgn activator complex. Taken together, these data indicated that fragment D of fibrinogen is necessary and sufficient to anchor a plgn activator complex on the surface of Streptococcus pyogenes.

Fibrin Fibrinogen Degradation Products↗
PubMed1980

Mutagenic activation of an antischistosomal drug by enteric Streptococcus sps in vitro and in vivo.

Previous studies have shown that a new antischistosomal drug, 4-isothiocyano-4'-nitro diphenylamine (CGP 4540, amoscanate), is not mutagenic in vitro, but the urines of animals treated with this drug have mutagenic activity. Mutagenicity can be eliminated by coadministration of some antibacterial agents and is not demonstrable in germ-free animals. The present study describes attempts to isolate and identify intestinal microorganisms responsible for the mutagenic activation of amoscanate. Streptococcus equinus, isolated from the intestinal tract of mice, as well as some other species of Streptococcus, were found to produce mutagenic activation of amoscanate when introduced into animals pretreated with antibacterial agents. Similarly, incubation of these strains with amoscanate in vitro resulted in the formation of a mutagenic product.

Aniline Compounds↗
PubMed1994

The fibronectin binding domain of the Sfb protein adhesin of Streptococcus pyogenes occurs in many group A streptococci and does not cross-react with heart myosin.

Sfb protein, a fibronectin binding adhesin of Streptococcus pyogenes (Lancefield group A streptococcus), mediates streptococcal adherence to human epithelial cells via its fibronectin binding domain coded by a repetitive gene region named fnbr. In the present study, Southern blot analysis using the fnbr gene region as a probe to screen genomic DNA from 51 epidemiologically unrelated clinical isolates of S. pyogenes revealed that 70% carried a sequence homologous to the fnbr probe. Among ten other streptococcal strains belonging to serological groups B, C, and G, DNA from only two human S. equisimilis (group C) strains reacted with the probe. Further analysis by PCR-mediated amplification of the binding repeat coding sequences revealed that repeats of different S. pyogenes isolates were identical in size but varied in number, ranging from one to five. Most of the isolates were shown to carry multiple repeats. Presence of the probe-positive sequence correlated strongly with streptococcal binding to purified fibronectin and adherence to HEp2 human epithelial cells; of the 36 probe-positive isolates, 95% bound fibronectin and 89% adhered strongly to epithelial cells, whereas among the 15 probe-negative isolates only 27% had binding activities for fibronectin and 27% showed strong adherence to HEp2 cells. Antibodies raised against the fibronectin binding domain of Sfb protein recognized streptococcal fibronectin binding surface proteins in most of the clinical isolates but did not react with heart or skeletal muscle myosin in an enzyme immunoassay, as is the case with antibodies directed to M protein, another major surface protein of group A streptococci. The results of the present study suggest that Sfb protein could be a potential candidate for a streptococcal vaccine.

Adhesins, Bacterial↗
PubMed1996

Deletion and reintroduction of glucosyltransferase genes of Streptococcus mutans and role of their gene products in sucrose dependent cellular adherence.

Streptococcus mutans has three kinds of glucosyltransferases (GTases), i.e. GTase-I, GTase-SI and GTase-S. These enzymes co-operatively synthesize adhesive glucan from sucrose, which contributes to firm adherence of growing organisms to solid surfaces. In this study, the genes encoding GTase-I (gtfB) and GTase-SI (gtfC) of S. mutans MT8148 (serotype c) were inactivated by the insertion mutagenesis by allelic exchange. Three types of isogenic mutants lacking either GTase-I, GTase-SI or both, respectively were isolated. Sucrose dependent cellular adherence of these mutants were significantly lower than that of the parent. Adherence of GTase-SI deficient mutant was lower than that of GTase-I deficient mutant. We then generated Escherichia coli-Streptococcus shuttle vectors carrying the gtfB and gtfC gene. The shuttle vector containing the gtfB gene was transformed into the GTase-I deficient mutant. Western blot analysis of the transformant revealed that GTase-I protein was fully expressed. Sucrose dependent adherence of the transformant increased but did not reach that of the parent. Similarly, the shuttle vector containing the gtfC gene was transformed into the GTase-SI deficient mutant. The expression of GTase-SI and sucrose dependent adherence of the transformant was revealed to be at a level similar to those by the parent. These results indicated that GTase-SI does play an essential role in the production of adhesive glucan that can lead to firm cellular adherence to solid surfaces.

Bacterial Adhesion↗
PubMed1998

Characterization of a novel insertion sequence, IS1194, in Streptococcus thermophilus.

A novel insertion sequence, IS1194, has been identified in the lactic acid bacterium Streptococcus thermophilus CNRZ368. This 1200-bp element has 16-bp imperfect terminal inverted repeats. The single large open reading frame of this element encodes a 332-amino-acid protein that displays similarities with transposases encoded by bacterial insertion sequences belonging to the IS5 group of the IS4 family. A single copy of IS1194 was detected by hybridization in only 2 of the 19 S. thermophilus strains tested and in 4 of the 13 Lactococcus lactis strains investigated. This suggests that this IS element was acquired by horizontal transfer. The unique IS1194 copy of S. thermophilus CNRZ368 is located in a region of at least 12 kb that was probably acquired by horizontal transfer from L. lactis. Furthermore, the IS1194 right end is identical to sequences found in a broad-host-range conjugative plasmid from Streptococcus pyogenes, pSM19035.

Amino Acid Sequence↗