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PubMed1987

Antibody response and dental caries in the bacterium Streptococcus-mono-associated, caries-resistant and caries-susceptible rats.

Correlations between rat strain, agglutinating antibody responses in serum or saliva and caries incidence, previously observed in Harvard rats mono-associated with Streptococcus faecalis and given diet L128 and 5 per cent sucrose added to drinking water, were not found when experiments were repeated with the low-sucrose diet 305. Mono-association with either Streptococcus mutans 6715 or Strep. faecalis ND547 produced extensive caries in caries-susceptible (HCS) rats and little or no caries in resistant (HCR) ones, but caries incidence did not relate to levels of agglutinating antibodies in serum or saliva. There was markedly less serum antibody to Strep. faecalis in the HCR rats and more antibody in HCS rats, when compared to previous results, but this did not affect caries scores in either strain. No agglutinating antibody to Strep. mutans was detected in serum and indefinite antibody appeared in saliva. Under these conditions, the ability to produce an agglutinating antibody response did not appear to play a role in caries resistance.

Agglutination↗
PubMed1976

Membrane studies of Streptococcus pyogenes and its L-form growing in hypertonic and physiologically isotonic media. An electron spin resonance spectroscopy approach.

Electron spin resonance spectroscopy (ESR) was used to compare the lipid organization, thermal stability and the physical state of the membrane of a human pathogen, Streptococcus pyogenes and its osmotically fragile L-form with this same L-form now adapted to grow under physiologically isotonic conditions (physiological L-form). Comparison of the hyperfine splittings of a derivative of 5-ketostearic acid spin label, I(12, 3), after incorporation into the membrane, revealed that the lipid chain rigidity of these membranes is in the order physiological L-form greater than osmotically fragile L-form greater than streptococcus. The signal intensity (of the center magnetic field line) versus temperature analysis showed two transitions for these membranes. The first with melting points of 45, 26 and 36 degrees C and second transition at 70, 63 and 60 degrees C for the physiological L-form, osmotically fragile L-form and streptococcal membranes, respectively. This same order of membrane lipid chain rigidity was seen from the cooperativities obtained for each of these systems from analysis based on the expression for an n-order reaction. The I(12, 3) and other probes with the paramagnetic group close to the methyl end of the molecule suggested that this difference in lipid chain rigidity between these organisms resides in the environment closer to the lipid head group region rather than in the hydrophobic lipid core. Another major finding was the binding of I(12, 3) at two or more different sites in each of the membranes examined. This change in lipid chain rigidity now provides an explanation to account for the survival of a previously osmotically fragile L-form in physiologically isotonic media by focusing on changes in the physical nature of its membrane. In so doing, it adds to and reinforces the speculation of the potential survival in vivo and involvement in pathogenesis of osmotically fragile aberrant forms of bacteria.

Cell Membrane↗
PubMed1995

Conformational analysis of oligosaccharides corresponding to the cell-wall polysaccharide of the Streptococcus group A by Metropolis Monte Carlo simulations.

Metropolis Monte Carlo simulations have been performed on four substructures from the cell-wall polysaccharide antigen of Streptococcus group A to explore the conformational behaviour of these compounds. The compounds examined are the trisaccharide, propyl 3-O-(2-acetamido-2-deoxy-beta-D-glucopyranosyl)-2-O-(alpha-L-rhamnopyranosyl)- alpha-L-rhamnopyranoside, 1, the tetrasaccharide, propyl 3-O-(3-O-(2-acetamido-2-deoxy-beta-D- glucopyranosyl)-2-O-(alpha-L-rhamnopyranosyl)-alpha-L-rhamnopyranosyl)-alpha-L- rhamnopyranoside, 2, the hexasaccharide, propyl 3-O-(2-O-(3-O-(3-O-(2-acetamido-2-deoxy-beta-D-glucopyranosyl)-alpha-L- rhamnopyranosyl)-alpha-L-rhamnopyranosyl)-3-O-(2-acetamido-2-deoxy-beta-D- glucopyranosyl)-alpha-L-rhamnopyranosyl)-alpha-L-rhamnopyranoside, 3, and the hexasaccharide, propyl 3-O-(2-acetamido-2-deoxy-beta-D-glucopyranosyl)-2-O-(3-O-(3-O-(2-acetamido-2- deoxy-beta-D-glucopyranosyl)-2-O-(alpha-L-rhamnopyranosyl)-alpha-L- rhamnopyranosyl)-alpha-L-rhamnopyranosyl)-alpha-L-rhamnopyranoside, 4. In general, the conformational flexibility of similar glycosidic linkages in different compounds is comparable. However, in a few cases, small differences in the conformations available to these linkages in different structural environments could be detected. Interestingly, a second conformation found for the beta-D-GlcNAc-(1-->3)-alpha-L-Rha linkage in three of the compounds was not populated in the hexasaccharide 4. Furthermore, a conformational locale of the alpha-L-Rha-(1-->3)-alpha-L-Rha linkage found to be populated in the trisaccharide 1, tetrasaccharide 2, and hexasaccharide 4 is negligibly populated in the hexasaccharide 3. Ensemble averaged proton-proton distances compare favourably with experimental average distances obtained from NMR spectroscopy. The trisaccharide branch point in the hexasaccharides is shown to be a highly defined conformational feature. The same unit has been found to be one of the crucial elements recognized by anti-Group A Streptococcus antibodies, a result that has implications for the design of improved immunodiagnostics and vaccines.

Carbohydrate Conformation↗
PubMed1990

Measurement of the humoral immune response against Streptococcus pneumoniae type 14-derived antigens by an ELISA and ELISPOT assay based on biotin-avidin technology.

A Streptococcus pneumoniae type 14-specific ELISA and ELISPOT assay have been developed based on the use of biotinylated type 14 capsular polysaccharide (S14PS-biotin). A major advantage of this application over other methods is the use of 10-100-fold less antigen than that reported in the literature for other similar assays. Moreover, the prepared biotinylated polysaccharides are very stable and it is possible to use the same procedures for other pneumococcal polysaccharide antigens (e.g., S6BPS) with no major changes necessary in the ELISA and ELISPOT protocols. Furthermore, a simple thin layer chromatography method has been developed as a method for quality control of the biotinylated polysaccharide. Immunization with the thymus-independent antigen S14PS resulted in the induction of IgM spot-forming cells (SFC) and antibodies while S14PS-protein conjugates induced a thymus-dependent response. The immune response to the conjugates was enhanced by the addition of the adjuvant Quil A resulting in high levels of both IgG SFC and antibodies at day 14 after immunization. The developed assays are reliable and reproducible tools for studying the humoral immune response against Streptococcus pneumoniae type 14 capsular polysaccharide derived antigens.

Animals↗
PubMed1992

Determination of the solution structures of domains II and III of protein G from Streptococcus by 1H nuclear magnetic resonance.

We have used 1H nuclear magnetic resonance spectroscopy to determine the solution structures of two small (61 and 64 residue) immunoglobulin G (IgG)-binding domains from protein G, a cell-surface protein from Streptococcus strain G148. The two domains differ in sequence by four amino acid substitutions, and differ in their affinity for some subclasses of IgG. The structure of domain II was determined using a total of 478 distance restraints, 31 phi and 9 chi 1 dihedral angle restraints; that of domain III was determined using a total of 445 distance restraints, 31 phi and 9 chi 1 dihedral angle restraints. A protocol which involved distance geometry, simulated annealing and restrained molecular dynamics was used to determine ensembles of 40 structures consistent with these restraints. The structures are found to consist of an alpha-helix packed against a four-stranded antiparallel-parallel-antiparallel beta-sheet. The structures of the two domains are compared to each other and to the reported structure of a similar domain from a protein G from a different strain of Streptococcus. We conclude that the difference in affinity of domains II and III for IgG is due to local changes in amino acid side-chains, rather than a more extensive change in conformation, suggesting that one or more of the residues which differ between them are directly involved in interaction with IgG.

Bacterial Proteins↗
PubMed1992

Postpartum periarticular hip abscess with later coxitis caused by group B streptococcus.

Intrapartum haematogenous spread of vaginal group B Streptococcus is rare, but it can lead to severe complications like abscesses, endocarditis and meningitis postpartum. We report a postpartum periarticular hip abscess caused by group B Streptococcus. Clinically it caused pain in the hip and a compression of the femoral nerve with motor and sensory component. Diagnosis was made by aspiration under computed tomography control. The only sign of infection was an increased sedimentation rate. After antibiotic treatment the symptoms disappeared and the abscess vanished, but it was reactivated 4 months after delivery, leading to arthritis of the hip joint. Another antibiotic treatment was administered for 8 weeks. 17 months postpartum the patient is well, but a development of a secondary coxarthrosis can not be excluded.

Abscess↗
PubMed1975

Periapical destructions caused by experimental pulpal inoculation of Streptococcus mutans in rats.

The development of pulpal and periapical changes in rat molars was studied after inoculation of Streptococcus mutans (GS-5) into the pulp chamber. Before injection into the pulp Streptococcus mutans was cultured on a special collagen substrate and "trained" to break down collagen. The destruction of the alveolar bone periapically could be demonstrated both roentgenologically and histopathologically. Large numbers of inflammatory cells in the pulp chamber and the periapical area, as well as carious dentin, were present. The pulpally inoculated bacteria could also be recovered from the systemic blood. The identity between the pulpally inoculated bacteria and the bacteria recovered from the blood was proved by gel precipitation.

Alveolar Process↗
PubMed1983

An enzyme-linked immunosorbent assay (ELISA) for quantification of antibodies to Streptococcus mutans surface antigens.

An ELISA was developed to quantitate the level of antibodies to various cell surface antigens of the Gram positive bacterium, Streptococcus mutans. Whole cells and purified cell wall components of S. mutans, lipoteichoic acid (LTA) from Streptococcus pyogenes, and dextran T 2000 were employed as coating antigens in this study. Cell walls of S. mutans were purified by mechanical disruption of whole cells followed by differential centrifugation and proteolytic enzyme treatment. Serotype-specific carbohydrate was purified from an autoclaved, lyophilized S. mutans whole cell preparation by column chromatography. LTA was prepared by Sepharose 4B chromatography of a phenol-water extract of S. pyogenes and used for detection of anti-polyglycerophosphate (PGP) antibodies. A rabbit antiserum to S. mutans 6715 (serotype g), which precipitated with purified carbohydrate antigen (RR g), gave good reactions with purified cell walls and whole cells of S. mutans 6715, less activity with RR g and low activity to LTA and dextran when tested by ELISA. Adsorption of this antiserum with whole cells of S. pyogenes resulted in antibody activity with specificity only to the serotype carbohydrate. The specificity of the antibody for homologous coating antigen was RR g greater than cell wall greater than whole cells. An antiserum to S. mutans MT573 (serotype e) contained antibody predominantly to LTA, whereas, anti-S. mutans MT703 (serotype e) reacted with both dextran and LTA; however, the activity to LTA was removed by prior adsorption of the antiserum with S. pyogenes cells. This treatment did not alter the antibody activity to dextran. To establish the sensitivity of ELISA, a purified IgG anti-serotype carbohydrate antibody was prepared by adsorption of anti-S. mutans 6715 antiserum with a mutant of S. mutans which lacks serotype carbohydrate followed by adsorption and elution of specific antibodies from S. mutans 6715 whole cells. The minimum level of sensitivity of ELISA was 12.5 ng of IgG anti-serotype carbohydrate.

Antibodies, Bacterial↗
PubMed1990

Infective endocarditis caused by Streptococcus suis serotype 2.

Infective endocarditis caused by Streptococcus suis serotype 2 is not uncommon in pigs but is rare in human beings. We describe the case of a pig-farmer with endocarditis due to S. suis serotype 2 and in whom prolapse of the mitral valve was the predisposing cardiac lesion. Streptococcus suis, a possible cause of infective endocarditis in endemic areas, may be confused with other group D streptococci. In suspected cases a history of contact with pigs or raw pork should be sought.

Agricultural Workers' Diseases↗
PubMed1991

Multiple brain abscesses caused by Streptococcus bovis.

A case of multiple brain abscesses caused by Streptococcus bovis in a 28-year-old man is described. Infected bronchiectasis is presumed to be the source of infection. Streptococcus bovis infection is a rare cause of brain abscess. The aetiology and manifestations of this infection are discussed.

Adult↗
PubMed1992

Prosthetic hip-joint infection associated with a penicillin-tolerant group B streptococcus.

We report a case of prosthetic hip-joint infection with Streptococcus agalactiae (Lancefield group B streptococcus). The infection recurred after 3 months' treatment with amoxycillin. On further investigation, the isolate was found to be amoxycillin-tolerant. Addition of gentamicin abolished tolerance in vitro and the patient has remained asymptomatic since receiving a 10-day course of amoxycillin and gentamicin followed by amoxycillin alone.

Aged↗
PubMed1993

Antimicrobial susceptibility and serotype distribution of Streptococcus pneumoniae from Rwanda, 1984-1990.

A total of 383 clinical isolates of Streptococcus pneumoniae, obtained from an equal number of patients in Kigali, Rwanda, was tested for resistance to penicillin G with a 1 microgram oxacillin disc. Of these isolates, 99 (25.8%) showed reduced zones of inhibition. By means of an agar dilution method, 21% all isolates were confirmed as relatively resistant (MIC > or = 0.12- < or = 1.0 mg/l) strains of Streptococcus pneumoniae (RRSP). A high degree of resistance to penicillin G (MIC > or = 2 mg/l) was not observed. Resistance to chloramphenicol (MIC > or = 8 mg/l) was found in 31% RRSP and in 6% penicillin susceptible strains (PSSP). Doxycycline resistance was common in both RRSP and PSSP strains. All isolates remained fully susceptible to erythromycin. Children more often harboured a strain giving a reduced inhibition zone than did adults (74/230 versus 25/153; P = 0.0005). A total of 32 serotypes or serogroups were identified, seven of them relating to 64.8% all isolates typed. Of all the isolates 84% belonged to a serotype represented in the 23-valent vaccine or to a cross-reacting serotype. Serotype 25, not included in the vaccine, accounted for 10.7% typed isolates from adults but only for 2.0% typed isolates from children. Results of susceptibility testing and clinical experience suggest that penicillin G, ampicillin and chloramphenicol should not be used alone as empirical treatment for pneumococcal meningitis in patients in Rwanda.

Adult↗
PubMed1995

Influence of recombinant bovine interleukin-1 beta and interleukin-2 in pigs vaccinated and challenged with Streptococcus suis.

An experiment was conducted to determine the adjuvanticity of recombinant bovine IL-1 beta (rBoIL-1 beta) and recombinant bovine IL-2 (rBoIL-2) administered in conjunction with a single Streptococcus suis vaccination in pigs. Sixty 4-week-old pigs were allotted to eight groups: nonvaccinated controls; vaccinated controls; rBoIL-beta at 0.1, 1, and 10 micrograms kg-1; rBoIL-2 at 2.5, 25, and 250 micrograms kg-1. All pigs (except nonvaccinated controls) were vaccinated on Day 0 with a commercial Streptococcus suis vaccine (serotypes 1 and 2). At vaccination, pigs were injected intramuscularly with their respective cytokine treatments. Pigs received additional cytokine injections on 2 consecutive days. On Day 21, all pigs were challenged intravenously with 3.2 x 10(9) colony forming units of a log phase culture of S. suis (serotype 2). The highest dose of rBoIL-1 beta exceeded the maximum tolerable dose for the cytokine; however, this dose of rBoIL-1 beta protected pigs from the S. suis challenge. Pigs administered rBoIL-1 beta at 10 micrograms kg-1 had higher antibody responses to S. suis, less severe clinical signs of the disease after challenge, better growth performance during the infection, and less severe gross pathological lesions caused by the bacteria. No pigs in this treatment group died from the bacterial challenge. These data suggest that rBoIL-1 beta (10 micrograms kg-1), administered intramuscularly for 3 consecutive days at vaccination, is more effective than a single S. suis vaccination alone in protecting pigs against a S. suis challenge.

Adjuvants, Immunologic↗
PubMed1989

Infective endocarditis caused by Streptococcus agalactiae.

We report a series of five cases of infective endocarditis caused by Streptococcus agalactiae (group B streptococcus) in Glasgow over a 30 month period. There were three males and two females mean age 48.6 years (range 28-63 years). Only one patient had previous valvular heart disease. The infections were characterised by an acute presentation and an aggressive course with major arterial emboli. Despite early diagnosis and appropriate intravenous antibiotics three patients died, one after valve replacement and two before surgery could be undertaken. The remaining two patients had successful valve surgery and have recovered. S. agalactiae endocarditis is an uncommon but important condition which carries a high mortality. The infection is difficult to control with antibiotics alone and therefore early surgery may be indicated.

Adult↗
PubMed1990

Streptococcus pyogenes: an outbreak on a burns unit.

An outbreak of infection with Streptococcus pyogenes (Group A beta-haemolytic streptococcus) on a burns unit described. The control measures taken are outlined, and the route of spread of infection is discussed along with possible preventative measures.

Burn Units↗
PubMed1993

Co-existent cross-infection with Streptococcus pneumoniae and group B streptococci on an adult oncology unit.

An outbreak of respiratory infection in an adult oncology unit is described where there was evidence of co-existent cross-infection with Streptococcus pneumoniae serotype 14 and Lancefield group B streptococcus type Ia. The presumed route of transmission was droplet spread from patient to patient. No further cases arose after the ward had been closed to new admissions and all symptomatic patients were treated with erythromycin. We suggest that patients with pneumococcal pneumonia on units housing elderly debilitated patients should be isolated. Infection control teams should be aware of the ability of Lancefield group B streptococci to spread by cross-infection among adult patients.

Adult↗
PubMed1990

Characterization and comparison of virulent bacteriophages of Streptococcus thermophilus isolated from yogurt.

Seven virulent bacteriophages of Streptococcus thermophilus were characterized at the molecular level and classified into 2 subgroups (A and B) by DNA/DNA hybridization experiments and analysis of their structural proteins. Two representatives of subgroups A and B were compared to 3 representatives of Neve's subgroups I, II and III (Neve et al, 1989) by Southern blot experiments. These isometric-headed phages possess a double-stranded DNA genome varying between 30-44 kilobase (kb) pairs. Subgroup A is composed of 3 phages (phi 57 as representative) with similar structural proteins as determined by sodium dodecyl sulfate-poly-acrylamide gel (SDS-PAGE) electrophoresis (estimated molecular weights of 31,000 and 27,500 for phage phi 57 and 32,000 and 27,000 for the 2 others). A common structural protein of 43,000 was found for phages of subgroup B. Phages phi 57 (subgroup A) and a10/J9 or PO (Neve's subgroups I or II, respectively) belonged to the same subgroup as determined by DNA/DNA hybridization experiments. Partial DNA homology was detected among all the phages tested except for phage phi ST27 of AW Jarvis. Phage-host interactions were also investigated by cross-propagation of the 7 studied phages on different indicator strains. A complete lack of correlation existed between the DNA homology grouping of the phages and their host range. Various restriction-modification systems were detected in some of the Streptococcus thermophilus strains.

Bacteriophages↗
PubMed1992

The 23S-5S spacer of two rRNA loci of Streptococcus salivarius subsp thermophilus includes a promoter.

The nucleotide sequence of the 3' part of a ribosomal and transfer RNA locus from Streptococcus salivarius subsp thermophilus NST1403 was determined. The sequenced DNA fragment includes the 3' end of a 23S rRNA gene, a 5S rRNA gene, a tRNA(asn) gene and a potential transcriptional terminator. The tRNA gene does not encode for the CCA 3'terminus of mature tRNA. We compared this sequence to a promoter-carrying DNA fragment sequence (P20) of Streptococcus salivarius subsp thermophilus A054 [1]. We found that the P20 sequence included the 3' end of a 23S rRNA gene, a 5S rRNA gene and the 5' part of a tRNA(val) gene. The two 23S-5S spacer sequences are identical and contain a promoter and a potential 23S rRNA processing site. Therefore, 5S rRNA and tRNA genes could be transcribed from a promoter located within the 23S-5S spacer of at least two of the six rRNA loci.

Base Sequence↗