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PubMed1996

Kinetics and regulation of erythrogenic toxins type A and C during growth of Streptococcus pyogenes.

The production of erythrogenic toxins type A (ETA) and C (ETC) is described as a function of growth kinetics. Group A streptococcal strains C 203 S and NY 5 were cultivated in yeast-peptone extract, Todd-Hewitt medium and a synthetic medium. Two main growth phases occurred during growth: a first logarithmic phase and a second linear phase. These phases were separated by a short stationary interphase caused by limitation of the amino acids L-serine and L-leucine. Maximum production of ETC was observed during the logarithmic phase, it was correlated to a high level of viable cells. ETA was produced mainly during the short stationary interphase. The production of ETC is regulated by L-isoleucine. A stagnation or reduction of the concentration of viable cells was observed during the interphase. The phosphate limitation caused during streptococcal growth induced expression of the extracellular protein phosphatase and surprisingly, of a serine proteinase activity. The association between these results and the pathogenicity of streptococci is discussed.

Acid Phosphatase↗

PubMed1993

Characterization of the effectors required for stable inheritance of Streptococcus pyogenes pSM19035-derived plasmids in Bacillus subtilis.

The low-copy-number and broad-host-range pSM19035-derived plasmid pBT233 is stably inherited in Bacillus subtilis cells. Two distinct regions, segA and segB, enhance the segregational stability of the plasmid. Both regions function in a replicon-independent manner. The maximization of random plasmid segregation is accomplished by the recombination proficiency of the host or the presence of the pBT233 segA region. The segA region contains two open reading frames (orf) [alpha and beta]. Inactivation or deletion of orf beta results in SegA- plasmids. Better than random segregation requires an active segB region. The segB region contains two orfs (orf epsilon and orf zeta). Inactivation of either of the orfs does not lead to an increase in cell death, but orf zeta- plasmids are randomly segregated. These results suggest that pBT233 stabilization relies on a complex system involving resolution of plasmid oligomers (segA) and on the function(s) encoded by the segB region.

Bacillus subtilis↗

PubMed1994

Clonal diversity of Streptococcus pyogenes within some M-types revealed by multilocus enzyme electrophoresis.

Twenty-two reference isolates and 30 local isolates of group A Streptococci were classified into 36 electrophoretic types (ET) on the basis of allozyme variation at 27 enzyme loci. Local isolates were characterized by a high frequency of M-non typable strains. M-type and ET were more closely associated in local isolates from an endemically-infected population; nevertheless, amongst the local isolates there were also strains of the same ET type with different M-types. A possible explanation is that genetic exchange between strains may introduce different M-types into strains of defined ET when these are exposed to strong selection in the presence of heavy loads of infection. In contrast to the reported clustering of strains associated with toxic shock-like syndrome into two closely related ET clones, we found no relationship of ET phenotype to acute poststreptococcal glomerulonephritis or rheumatic fever.

Alleles↗

PubMed2004

Effect of penicillin on surface carbohydrate, hemolysin and morphology of Streptococcus pyogenes during and after the post-antibiotic phase.

The post-antibiotic effect (PAE) of penicillin was measured in vitro against a group A streptococcal strain by the kinetic growth method. The duration of the effect was 2.8 h. The bacterial morphology and some streptococcal products were analyzed during and after the PAE, after being exposed to penicillin in a concentration of 1xMIC for 2 h. Bacteria not previously exposed to penicillin were used as a control culture. Morphological changes and increases in the size of treated streptococci were observed by electronic microscope during the post-antibiotic phase. The post-penicillin effect on the production of cell-bound hemolysin and free hemolysin was examined using sheep red blood cells. Production of cell-bound hemolysin rose sharply, but was inhibited by the antimicrobial agent. The free lysin diminished significantly, and concomitantly with a higher production of free toxin by the treated cells. No effect was observed on the specific carbohydrate group when the antigen was tested with streptococcal group A antiserum.

Carbohydrate Metabolism↗

PubMedDate not supplied

Cellular responses of the mouse to the peptidoglycan of a gram-positive bacterium (Streptococcus pyogenes).

The cellular responses and the stimulation of the reticulo-macrophagic system induced in the mouse by a purified bacterial peptidoglycan (PGL) as previously described, were studied by the changes in the peritoneal cytology, the macrophage-migration-inhibition test and the clearance of colloidal carbon. PGL was submitted to chemical and immunochemical characterization and was shown to be substantially free of contamination by polysaccharides, phospholipids, teichoic acid and nucleic acids, but to contain a detectable amount of peptide contaminants; N-acetylglucosamine and the tetrapeptide (with terminal D-alanine) were shown to be the main antigenic determinants. This substance had no action on polymorphonuclear leucocytes but induced an inhibition of the migration of macrophages. This was due to an immunological reaction rather than to direct cytotoxicity, as shown by the negative cytotoxicity tests and the age and life-environment-dependence of the phenomenon. The reticulomacrophagic system was significantly stimulated after primary inoculation, and still more so after a booster. The possible mechanisms of these activities, which are therefore independent from toxic and/or inflammatory responses, are discussed.

Animals↗

PubMed2006

Group A streptococcal myonecrosis: increased vimentin expression after skeletal-muscle injury mediates the binding of Streptococcus pyogenes.

Necrotizing fasciitis and myonecrosis caused by invasive infection with group A streptococci (GAS) are life-threatening conditions that have reemerged worldwide. Half of all GAS myonecrosis cases have no known portal of entry; yet, for unknown reasons, infection becomes established precisely at the site of a prior, nonpenetrating minor injury, such as a muscle strain. We hypothesized that GAS establishes infection by binding to surface molecules that are up-regulated on injured skeletal-muscle cells. Here, we isolated and identified vimentin as the major skeletal-muscle GAS-binding protein. Furthermore, we found that vimentin expression was up-regulated on injured skeletal-muscle cells in vitro and was expressed in muscle tissues from a patient with GAS myonecrosis who died of streptococcal toxic shock syndrome. These findings provide a molecular mechanism to explain the development of severe GAS soft-tissue infections at the sites of prior minor muscle trauma. This understanding may provide a basis for novel preventive strategies or therapies for patients with this devastating infection.

Amino Acid Sequence↗

PubMed1993

Antigenic diversity of IgA receptors in Streptococcus pyogenes.

In a previous study, group A and group B streptococcal IgA receptors were shown to differ serologically, in agreement with their known structural unrelatedness. The present study was undertaken to serologically compare the IgA binding epitopes of group A streptococcal strains representing various serotypes by the use of antisera to this species. It was found that blocking antibodies occurred in antisera to IgA binding but not to non-binding strains and that binding of IgA to a streptococcal strain was generally blocked by antiserum to the homologous type. However, cross-testing of a panel of 11 IgA binding strains, representing various M and T serotypes, with 10 different antisera to group A streptococci, demonstrated that IgA receptors were inhibited to a highly variable degree and that inhibition patterns were unique for each type. Comparing solubilized IgA receptors of various strains in immunoblot experiments, a variation in the molecular mass, between approximately 35 and 45 kDa, emerged. The IgA binding epitopes, analogous to protective sites of streptococcal M-protein, thus exhibited hypervariability which may suggest that IgA binding also plays a key role for evading host immune defence mechanisms.

Animals↗

PubMed1986

[Isolation and characterization of erythrogenic toxins. VIII. Purification of a biologically active protein of the molecular weight 10,000 (LMP-10k) from filtrates of Streptococcus pyogenes, strain NY-5. Relationship to erythrogenic toxin type A].

The "classical" method for purification of erythrogenic toxin type A results in two products: erythrogenic toxin type A and a low molecular weight protein, m.w. 10,000 (LMP-10k) with mitogenic activities. LMP-10k was purified from culture supernatants of S. pyogenes (group A) by CM-Sepharose CL-6B chromatography and Sephacryl S-200 and Sephadex G75 gel filtration to a high degree of purity with minimal amounts of residual erythrogenic toxin A. The isoelectric point of LMP-10k is the same as for erythrogenic toxin A: 5.2. The immunogenic activity is low, only one of two rabbits produced anti-LMP-10k-antibodies after a prolonged course of immunization. On the other hand it is possible to induce antierythrogenic toxin A-antibodies by immunization with LMP-10k preparations contaminated with small amounts of erythrogenic toxin A. Possibly the data given by some authors for the m.w. of erythrogenic toxin type A as 8 000 D are the results of a mix-up with co-purified LMP-10k.

Amino Acids↗

PubMed2000

Molecular epidemiology of nga and NAD glycohydrolase/ADP-ribosyltransferase activity among Streptococcus pyogenes causing streptococcal toxic shock syndrome.

Severe invasive group A streptococcal (GAS) infections emerged in the late 1980s, yet no single virulence factor has been common to all isolates from infected patients. A strong association was recently found between isolates of such cases (regardless of M type) and the production of NAD glycohydrolase (NADase). Of interest, all M-1 strains isolated after 1988 were positive for NADase, whereas virtually all M-1 GAS were previously negative for NADase. Genetic analysis demonstrated that GAS isolates were >96% identical in nga and >99% identical in their upstream regulatory sequences. Furthermore, because NADase-negative strains did not produce immunoreactive NADase, we concluded that additional regulatory element(s) control NADase production. NADase purified from GAS altered neutrophil-directed migration and chemiluminescence responses and had potent ADP-ribosyltransferase activity. In summary, the temporal relationship of NADase expression, alone or with other streptococcal virulence factors, may contribute to the pathogenesis of invasive GAS infections.

Amino Acid Sequence↗

PubMed1993

Conserved and variable regions in protein Arp, the IgA receptor of Streptococcus pyogenes.

The streptococcal M protein family, a number of cell surface molecules that interact with the human immune system, can be divided into two major classes, A and C, characterized by different types of repeats in the central part of the molecule. Class A and class C molecules are known to have a variable N-terminal region and a more conserved C-terminal region, but little is known about the mechanisms that give rise to this structural variation. In this report, we show that two variants of protein Arp, an IgA receptor in class C of the M protein family, have virtually identical signal sequences and C-terminal halves, but unrelated N-terminal sequences. Comparison of the sequences of the two genes and their flanking regions also demonstrates the presence of well-defined variable and conserved regions. Our results strongly suggest that the N-terminal sequence variation between the two variants of protein Arp was generated through an intergenic recombination event, rather than through intragenic recombination or accumulation of mutations.

Amino Acid Sequence↗

PubMed1995

Distinct profiles of immunoglobulin G-binding-protein expression by invasive serotype M1 isolates of Streptococcus pyogenes.

Analysis of immunoglobulin G (IgG)-binding-protein expression by invasive group A streptococcal isolates of the M1 serotype collected as part of a Centers for Disease Control and Prevention surveillance study revealed two distinct phenotypes. One group of type M1 isolates expressed a surface protein reactive with all four human IgG subclasses (type IIo), while a second group expressed a surface protein demonstrating significant reactivity only with human IgG3 (type IIb). The functional forms of IgG-binding protein were antigenically related, and both were recognized by a rabbit polyclonal antiserum to serotype M1 but not by normal rabbit serum. While the quantities of antigenic M1 protein present in the extracts of representative isolates displaying each phenotype differed, the functional differences were found to be qualitative and not solely quantitative. The IgG-binding properties of these antigenically related M1 proteins could be readily distinguished from those of another IgG-binding protein, protein H. Type M1 isolates of the IIb phenotype differed from those of the IIo phenotype by secreting larger amounts of a casein-hydrolyzing protease into culture supernatants.

Antigens, Bacterial↗

PubMed1997

Identification and characterization of a new protein from Streptococcus pyogenes having homology with fibronectin and fibrinogen binding proteins.

Fibronectin and fibrinogen-binding proteins have been described as possible adhesin in streptococci and staphylococci. Recent published data has demonstrated that Protein F, a fibronectin-binding protein from group A streptococci, is important in adherence to respiratory cells (8). Other similar proteins already described (i.e. SOF, Sfb and SfbII) are able to competitively inhibit the binding of fibronectin to S. pyogenes (9,10,5). Similarly, clumping factor from S. aureus, is known to promote adherence to fibrinogen-coated surfaces (7). When the sequence from SFFBP-12 was compared against all the others fibronectin and fibrinogen-binding proteins described in streptococci and staphylococci (1-10), an identity at the amino acid level, ranging from 38 to 69% was found for the C region. For the repeated region (R), the identity ranged between 47 and 75%. Unlike all the other proteins already described in group A streptococci, the protein we describe here, SFFBP-12, shares a high degree homology (67-75%) with the fibronectin-binding protein B from S. dysgalactiae (6), as well as homology with the S. aureus clumping factor (7) and fibronectin-binding protein B (3), making it a new potential fibronectin-fibrinogen binding protein for group A streptococci. These characteristics would also imply that SFFBP-12 contains two different fibronectin-binding domains (regions B and C), thus enhancing its role as a possible major adhesin molecule. RNA transcription assays showed a transcript with the expected molecular size for the intact SFFBP-12 protein, confirming that the protein is actively expressed during bacterial growth. SFFBP-12 is the largest protein of its kind identified from group A streptococci and is comparable in size to the fibronectin binding protein B from S. dysgalactiae (6). If it is shown that SFFBP-12 does in fact bind both fibronectin and fibrinogen, as the sequence data suggest, it would make this molecule a major virulence determinant for the group A streptococcus.

Adhesins, Bacterial↗

PubMed2002

The in vitro interaction of Streptococcus pyogenes with human pharyngeal cells induces a phage-encoded extracellular DNase.

The role lysogenic bacteriophage play in the pathogenesis of the host bacterium is poorly understood. In a previous study, we found that streptococcal coculture with human pharyngeal cells resulted in the induction of lysogenic bacteriophage as well as the phage-associated streptococcal pyrogenic exotoxin C (SpeC). In this study, we have determined that in addition to SpeC induction, a number of other streptococcal proteins are also released by the bacteria during coculture with pharyngeal cells. Among these, we identified and characterized a novel 27-kDa secreted protein. Sequence analysis of this novel protein demonstrated it to be encoded by the same lysogenic bacteriophage which harbors speC. Protein sequence analysis revealed varied homologies with several streptococcal DNases. Further biochemical characterization of the recombinantly expressed protein verified it to be a divalent cation-dependent streptococcal phage-encoded DNase (Spd1). Although functionally distinct, SpeC and Spd1 are associated by a number of parameters, including genetic proximity and transcriptional regulation. Finally, we speculate on the induction of phage-encoded DNase (Spd1) enhancing the fitness of both bacteria and phage.

Amino Acid Sequence↗

PubMed1987

Streptococcus pyogenes type 12 M protein gene regulation by upstream sequences.

A partial nucleotide sequence that included 1,693 base pairs of the M12 (emm12) gene of group A streptococci (strain CS24) and adjacent upstream DNA was determined. Type 12 M protein-specific mRNA of strain CS24 is transcribed from two promoters (P1 and P3) separated by 30 bases. The transcription start sites of the emm12 gene were located more than 400 bases downstream of a deletion that causes decreased M-protein gene transcription in strain CS64. Deletion analysis of M protein-expressing plasmids indicated that an upstream region greater than 1 kilobase is required for M-protein gene expression. The M-protein gene transcriptional unit appears to be monocistronic. Analysis of the emm12 DNA sequence revealed three major repeat regions. Two copies of each repeat, A and B, existed within the variable 5' end of the gene; repeat C demarcated the 5' end of the constant region shared by emm12 and emm6.

Antigens, Bacterial↗

PubMed1987

Comparative evaluation of medium and atmosphere of incubation for isolation of Streptococcus pyogenes.

To evaluate the effects of medium and atmosphere of incubation for the isolation of group A (GA) streptococci from throat cultures, we compared 1098 throat swabs plated on each of three blood agar plates (BAP). Two plates contained trimethoprim-sulfamethoxazole (SXT) and one had no antibiotics. The antibiotic-free medium and one SXT plate were incubated anaerobically (AnO2) at 35 degrees C, whereas the other SXT plate was incubated in air (O2) at 35 degrees C. The BAP-AnO2 identified 85% of 201 GA compared with 96% for SXT-AnO2 and 92% for SXT-O2. GA were confirmed from only 29% of the beta-hemolytic colonies on BAP-AnO2 compared with 53% from SXT-AnO2 and 44% from SXT-O2. SXT, however, appeared to delay recognition of GA; since 94% of positives were found on day 1 with BAP-AnO2 versus 80% and 62% with SXT-AnO2 and SXT-O2, respectively. We conclude that BAP-SXT (AnO2 or O2) is more sensitive and more specific than BAP-AnO2, but that a second day of incubation is required for optimal recovery of GA on the SXT selective media studied.

Aerobiosis↗

PubMed2006

Prevalence and mechanisms of macrolide resistance in Streptococcus pyogenes in Ankara, Turkey.

From 2002 to 2003, a total of 381 consecutive S. pyogenes isolates were obtained from throat swabs (n = 337) and samples of pus (n = 31), sputum (n=10) and blood (n = 3) at Hacettepe University Hospital. The susceptibility of the isolates to erythromycin was tested by the agar dilution method. Erythromycin resistant strains were then tested for their MICs to azithromycin, clindamycin, and penicillin, their phenotype of resistance to macrolides-lincosamides-streptogramin B (MLSB) and for the presence of macrolide resistance genes. The rate of resistance to erythromycin was 6.8%. Constitutive (cMLSB), inducible (iMLSB), and M phenotypes of resistance were detected in 7.7, 30.8, and 57.7% of resistant strains, respectively. One strain had both cMLSB and iMLSB phenotypes. All M phenotypes carried the mefA gene, all iMLSB phenotype carried the ermTR gene, 1 isolate with cMLSB phenotype harboured the ermB gene, and 1 isolate with cMLSB phenotype carried both the ermB and mefA genes. One strain which showed cMLSB and iMLSB phenotypes harboured the ermB gene.

Azithromycin↗

PubMed2002

[Pharyngotonsillitis caused by Streptococcus pyogenes: clinical and epidemiological aspects and resistance phenotypes towards macrolides].

During 2001 we analyzed 1730 pharyngeal swabs for S. pyogenes (SGA): 1142 children (0-10 years old), 132 adolescent subjects (11-17 years old), and 456 adults (18 or more years old). 994 subjects (664 children, 85 adolescent ones, 245 adults) had acute pharyngotonsillitis. In this last group we observed 321 positivities (32.3 %) for SGA: 40.4 % among children, 24.7 % among adolescent people, 13.1 % among adults. The pharyngotonsillitis prevailed during winter and spring. The resistances (R) towards erythromycin were 27.7 % (89 cases), and among children 30.6 % (82 cases), towards clyndamicin 15.3 % (49 cases, and 17.2 %, 46 cases, among children), towards rokytamicin 11.8 % (38 cases, and 13.1 %, 35 cases, among children). These were the phenotypes of R to erythromycin: 25.8 % M-phenotype, 19.1 % inducible (iMLS), 55.1 % constitutive (cMLS); among children respectively 25.6 %, 18.3 % and 53.7 %. Increased resistances towards 16-C macrolides, increased resistances of cMLS to erythromycin, and the persistence of R to 14-C macrolides around 30 % are discussed.

Adolescent↗

PubMed1982

[Induction of immune interferon by erythrogenic toxins A and B from Streptococcus pyogenes].

By interaction of streptococcal erythrogenic toxins A and B with chick embryo fibroblasts and human amnion (FL) cells an antiviral interferon-like factor was secreted. It inhibited the replication of vesicular stomatitis, vaccinia and Mengo viruses. The streptococcal toxin type B was 50 times more cytotoxic for both cell cultures in comparison with streptococcal toxin A. The maximum tolerated doses of the two types of streptococcal toxins induced approximately the same antiviral protection effect. The production curve of the antiviral factor showed a maximum at the 12th hour after incubation at 37 degrees C with graduate decrease up to the 24th hour using a 6 hours induction time. The interferons induced by the streptococcal erythrogenic toxins A and B were thermostable at 56 degrees C for 30 min and were partially destroyed at pH 2 as tested against Mengo virus in FL cells. The antiviral effect could be reversed by addition of streptococcal erythrogenic toxin A at the maximum tolerated dose simultaneously with the glycosylating inhibitors streptovirudin and D-glucosamine by 90 and 100 per cent, respectively.

Amnion↗