Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Streptococcus pyogenes”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 109 records · Page 6Linked to original sources
PubMed2005

Patterns of virulence gene expression differ between biofilm and tissue communities of Streptococcus pyogenes.

The ability of Streptococcus pyogenes to form biofilm-like bacterial communities during infection of soft tissue has suggested that the capacity to produce biofilm may be important for pathogenesis. To examine this relationship, a panel of mutants was evaluated for their ability to form biofilm on abiotic surfaces in several assays. Several established virulence factors were crucial for biofilm formation, including the M protein, required for initial cell-surface interactions, and the hyaluronic acid capsule, required for subsequent maturation into a three-dimensional structure. Mutants lacking the transcription regulators Mga and CovR (CsrR) also failed to form biofilm. Comparison of transcriptional profiles revealed differential regulation of approximately 25% of the genome upon adaptation to biofilm. During infection of zebrafish, several virulence factors (notably cysteine protease and streptokinase) were regulated in a biofilm-like manner. However, the overall profile of virulence factor expression indicated that tissue communities have a pattern of gene expression different from biofilm. Taken together, these data show that while biofilm and tissue communities have many characteristics in common, that biofilm reproduces only a subset of the myriad cues used by tissue communities for regulation of virulence.

Animals↗
PubMed2002

In vitro and in vivo stability of the epsilon2zeta2 protein complex of the broad host-range Streptococcus pyogenes pSM19035 addiction system.

Streptococcus pyogenes pSM19035-encoded epsilon (10.7 kDa) and zeta (32.4 kDa) proteins are necessary to secure stable plasmid inheritance in bacteria, with zeta acting as toxin that kills plasmid-deprived cells and epsilon as an antitoxin that neutralises the activity of zeta. The epsilon and zeta proteins co-purify as a stable complex that, according to analytical ultracentrifugation and gel filtration, exists as epsilon2zeta2 heterotetramer in solution. Co-crystals of the epsilon2zeta2 complex contain epsilon and zeta in 1:1 molar ratio. Unfolding studies monitoring circular dichroic and fluorescence changes show that the zeta protein has a significantly lower thermodynamic stability than the epsilon protein both in free state and in the complex. Proteolytic studies indicate that zeta protein is more stable in the epsilon2zeta2 complex than in the free state. In vivo studies reveal a short half-life of the epsilon antitoxin (-18 min) and a long lifetime of the zeta toxin (>60 min). When transcription-translation of a plasmid containing the epsilon and zeta genes was inhibited, cell death was observed after a short lag phase that correlates with the disappearance of the epsilon protein from the background.

Algorithms↗
PubMed2001

A secondary RNA polymerase sigma factor from Streptococcus pyogenes.

The important human pathogen Streptococcus pyogenes (the group A streptococcus or GAS) causes diseases ranging from mild, self-limiting pharyngitis to severe invasive infections. Regulation of the expression of GAS genes in response to specific environmental differences within the host is probably key in determining the course of the infectious process, however, little is known of global regulators of gene expression in GAS. Although secondary RNA polymerase sigma factors act as global regulators of gene expression in many other bacteria, none has yet been isolated from the GAS. The newly available GAS genome sequence indicates that the only candidate secondary sigma factor is encoded by two identical open reading frames (ORFS). These ORFS encode a protein that is 40% identical to the transcription factor ComX, believed to act as an RNA polymerase sigma factor in Streptococcus pneumoniae. To test whether the GAS ComX homologue functions as a sigma factor, we cloned and purified it from Escherichia coli. We found that in vitro, this GAS protein, which we call sigmaX, directed core RNA polymerase from Bacillus subtilis to transcribe from two GAS promoters that contain the cin-box region, required for transcription by S. pneumoniae ComX in vivo. On the other hand, GAS sigmaX did not promote transcription of a GAS promoter (hasA) expected to be dependent on sigmaA, the housekeeping or primary RNA polymerase sigma factor. Addition of monoclonal antibody that inhibited sigmaA-directed transcription had no effect on sigmaX-directed transcription, showing that the latter was not the result of contaminating sigmaA. Transcription of both cin-box-containing promoters initiated downstream of the cin-box and two different single basepair substitutions in the cin-box of the cinA promoter each caused a severe reduction of sigmaX-directed transcription in vitro. Thus, the cin-box is required for sigmaX-directed transcription.

Bacillus subtilis↗
PubMed1989

Fibrinogen binding and resistance to phagocytosis of Streptococcus sanguis expressing cloned M protein of Streptococcus pyogenes.

The biological properties of Streptococcus pyogenes M protein cloned and expressed in S. sanguis were investigated. The spm-5 gene previously cloned into Escherichia coli was subcloned into the E. coli-S. sanguis shuttle plasmid pVA838 to produce a newly constructed plasmid, pBK100. Cells of S. sanguis transformed with pBK100 expressed 53-, 55-, and 58-kilodalton polypeptides reacting with type 5 M protein antiserum in immunoblots. The M protein was expressed on the surface of S. sanguis cells as shown by the capacity of the intact cells to (i) inhibit the reactivity of anti-type 5 antibodies with purified M protein as demonstrated by enzyme-linked immunosorbent assay; (ii) inhibit the opsonization by M5 antisera of type 5 S. pyogenes; (iii) express M-protein-like fibrils on the surface of the organisms that react with M5 antisera as revealed by immunoelectron microscopy; (iv) bind plasma fibrinogen and, as a consequence, resist phagocytosis by human blood neutrophils; and (v) be rendered susceptible to phagocytosis by opsonic M5 antisera. These results provide additional evidence that streptococcal M proteins bind host proteins as a ploy to evade host defense mechanisms.

Antigens, Bacterial↗
PubMed1998

Effect of haptoglobin phenotypes on growth of Streptococcus pyogenes.

The haptoglobin (Hp) 2-1 and 2-2 phenotypes have been shown to agglutinate Streptococcus pyogenes carrying the membrane antigen T4. In this study, the growth rate of two strains of Streptococcus pyogenes (T1 and T4) in human serum was compared among haptoglobin phenotypes in vitro. During incubation for 16 hours in serum of different haptoglobin types, only Hp 2-1 and Hp 2-2 sera showed an inhibitory effect on growth, Hp 2-2 being 1.85 times more potent than Hp 2-1. Growth of Streptococcus pyogenes T4 negatively correlated with the serum concentration of Hp 2-1 (r = -0.908) and Hp 2-2 (r = -0.953). Haptoglobin-depleted serum had no inhibitory effect on bacterial growth. Addition of haemoglobin and ferric citrate to the serum accelerated the growth of Streptococcus pyogenes T4 (P <0.05) but not in Hp 2-2 serum. Haptoglobin types 2-1 and 2-2 can be regarded as inhibitors of Streptococcus pyogenes growth in vitro. These data point towards a potential protective role of Hp 2-2 in Streptococcus pyogenes infection in vivo, independently of iron uptake.

Antigens, Bacterial↗
PubMed1998

Emergence of Streptococcus pyogenes strains resistant to erythromycin in Gipuzkoa, Spain.

The aim of this study was to determine the evolution of resistance to macrolides and other antibiotics in strains of Streptococcus pyogenes isolated in the province of Gipuzkoa, Spain. During the period 1984-1996, all 2561 strains of Streptococcus pyogenes studied showed full susceptibility to penicillin. Until 1990, only 1.2% of Streptococcus pyogenes isolates were resistant to erythromycin. Since then, resistance to erythromycin increased every year until 1995, when 34.8% (87/250) of Streptococcus pyogenes strains were found to be resistant. In 1996 the rate of resistance to erythromycin was 17.8% (75/422). During the study period, 96.1% (246/256) of the Streptococcus pyogenes isolates resistant to erythromycin were susceptible to clindamycin. Of the remaining erythromycin-resistant Streptococcus pyogenes strains, resistance to clindamycin was constitutive in seven strains and inducible in three. When investigated by the polymerase chain reaction (PCR), all Streptococcus pyogenes strains resistant to erythromycin and susceptible to clindamycin showed the 1.4 kb fragment of the mefA gene, recently described as the novel macrolide-efflux-resistance determinant. The most frequent T-agglutination patterns among Streptococcus pyogenes resistant to erythromycin were T4 and T8,25. The emergence and rapid spread of erythromycin-resistant Streptococcus pyogenes in Gipuzkoa and its relationship to the presence of the mefA gene are described.

Agglutination↗
PubMed2003

Bacteremic pneumococcal cellulitis compared with bacteremic cellulitis caused by Staphylococcus aureus and Streptococcus pyogenes.

In order to better characterize bacteremic cellulitis caused by Streptococcus pneumoniae, a review was conducted of 10 cases of bacteremic pneumococcal cellulitis, which represented 0.9% of all cases of pneumococcal bacteremia (n=1,076) and 3.2% of all cases of community-acquired bacteremic cellulitis (n=312) that occurred in the Hospital de Bellvitge, Barcelona, from 1984 to 2001. In addition to these 10 cases, 28 cases of bacteremic pneumococcal cellulitis from the literature (Medline 1975-2001) were reviewed. Pneumococcal cellulitis of the face, neck, and trunk was observed more frequently in patients with systemic lupus erythematosus and hematologic disorders, while pneumococcal cellulitis of the limbs was more common in patients with diabetes, alcoholism, and parenteral drug use. In the Hospital de Bellvitge group, bacteremic cellulitis due to Streptococcus pneumoniae was more frequently associated with severe underlying diseases than that due to Staphylococcus aureus or Streptococcus pyogenes (100%, 57%, and 72%, respectively;P=0.01). A concomitant extracutaneous focus of infection (e.g., respiratory tract infection) suggesting hematogenous spread with metastatic cellulitis was more frequent in patients with pneumococcal cellulitis, while a local cutaneous entry of microorganisms was feasible in most patients with Staphylococcus aureus or Streptococcus pyogenes cellulitis. The 30-day mortality was 10% in patients with pneumococcal cellulitis, 13% in patients with Staphylococcus aureus cellulitis, and 23% in patients with Streptococcus pyogenes cellulitis (P=0.3). Thus, bacteremic pneumococcal cellulitis is an unusual manifestation of pneumococcal disease and occurs mainly in patients with severe underlying diseases. In most cases, pneumococcal cellulitis has a different pathophysiologic mechanism than cellulitis caused by Staphylococcus aureus or Streptococcus pyogenes.

Adult↗
PubMed1989

Reliable five-minute test strip method for identification of Streptococcus pyogenes.

A novel and rapid method (Strep Strip, Lab M) for identification of Streptococcus pyogenes was evaluated. The method combines the established test for pyroglutamyl aminopeptidase (PYR) with a rapid chromogenic test for beta-glucosidase on a paper strip. The test was evaluated with 274 clinical isolates and 237 culture collection isolates of beta-haemolytic streptococci. Streptococcus pyogenes was identified with 100% specificity. Six isolates identified as Lancefield group A and which might therefore be assumed to be Streptococcus pyogenes were shown by the test strip method not to be this species. The beta-glucosidase test on the test strip allowed differentiation between enterococci and Streptococcus pyogenes (both PYR positive) in all cases. The test strip method represents an economical and accurate method for identification of Streptococcus pyogenes in clinical material.

Aminopeptidases↗
PubMed2005

Survey of phenotypic and genetic features of streptococcus pyogenes strains isolated in Northwest Italy.

Streptococcus pyogenes (group A Streptococcus [GAS]) is an important pathogen whose virulence is related to the production of exotoxins and the presence of particular surface components. One hundred eighty-two GAS strains were collected in northwestern Italy between 1994 and 2002 and analyzed for phenotypic characteristics (opacity factor, proteolyic activity, and antimicrobial susceptibility) and by polymerase chain reaction for the presence of genes responsible for the production of exotoxins implicated in pathogenesis speA and speF and of prtF(1) (encoding fibronectin-binding protein F1). All strains were speF positive and 19.2% were speA positive and prtF(1) negative, whereas the prtF(1) gene was identified in 39.5% of the other strains. Of these, approximately half revealed the same pulse-field gel electrophoresis (PFGE) pattern but differed in both speA gene and macrolide resistance.

Adhesins, Bacterial↗
PubMed1994

[Invasive Streptococcus pyogenes infection (beta-hemolytic Streptococcus of group A)].

Group A streptococcal infections are frequent and most often benign. Severe invasive infections due to this microorganism have nevertheless been reported with increasing frequency in various countries for several years. Moreover, a toxic shock-like syndrome has recently been recognized and characterized in such infections. Two cases of invasive group A streptococcal infections (one primary peritonitis and one toxic shock syndrome) are reported to increase a better understanding of this disease in the light of a review of the pertinent literature. This is hoped to contribute to better management of what is a growing problem for many physicians who are nowadays no longer familiar with the broad spectrum of group A streptococcal infections.

Abdomen, Acute↗
PubMed1983

Rapid identification of Streptococcus pyogenes by flow cytometry.

Flow cytometry combined with immunofluorescence of Streptococcus pyogenes was used to assay bacteria suspended in buffer solution and in saliva derived from throat swabs of healthy volunteers. The method allowed the enumeration of as few as 5 X 10(3) and 5 X 10(4) CFU per milliliter of buffer and saliva respectively. Controls including Streptococcus salivarius instead of Streptococcus pyogenes or buffer instead of specific antibodies confirmed the specificity of the detection of Streptococcus pyogenes in the samples. The results suggest that flow cytometry may serve as a basis for an automated reliable method for the diagnosis of streptococcal infections.

Culture Media↗
PubMed2001

[Primary peritonitis due to Streptococcus pyogenes].

Most infections causing by Streptococcus pyogenes are known to be putrid both in adults and children, for example laryngitis, impetigo, cellulitis, scarlet fever, septic shock, toxic shock syndrome etc. Their clinical importance relates to a number of causes: 1) about 20% of the population are S. pyogenes carriers; 2) the clinical course of infections is often severe or even fatal; 3) there is real danger of nosocomial outbursts; 4) a world-wide increase in both the rate and invasiveness of the microbe. Acute primary peritonitis due to S. pyogenes seems to be a rare clinical event. In order to stimulate physicians' attention to the issue, we decided to describe the case of a child with the primary peritonitis due to S. pyogenes. Early diagnosis and surgical intervention combined with the proper antibiotic treatment appeared to be life-saving.

Cefuroxime↗
PubMed2006

Proteomic analysis and identification of Streptococcus pyogenes surface-associated proteins.

Streptococcus pyogenes is a gram-positive human pathogen that causes a wide spectrum of disease, placing a significant burden on public health. Bacterial surface-associated proteins play crucial roles in host-pathogen interactions and pathogenesis and are important targets for the immune system. The identification of these proteins for vaccine development is an important goal of bacterial proteomics. Here we describe a method of proteolytic digestion of surface-exposed proteins to identify surface antigens of S. pyogenes. Peptides generated by trypsin digestion were analyzed by multidimensional tandem mass spectrometry. This approach allowed the identification of 79 proteins on the bacterial surface, including 14 proteins containing cell wall-anchoring motifs, 12 lipoproteins, 9 secreted proteins, 22 membrane-associated proteins, 1 bacteriophage-associated protein, and 21 proteins commonly identified as cytoplasmic. Thirty-three of these proteins have not been previously identified as cell surface associated in S. pyogenes. Several proteins were expressed in Escherichia coli, and the purified proteins were used to generate specific mouse antisera for use in a whole-cell enzyme-linked immunosorbent assay. The immunoreactivity of specific antisera to some of these antigens confirmed their surface localization. The data reported here will provide guidance in the development of a novel vaccine to prevent infections caused by S. pyogenes.

Bacterial Proteins↗
PubMed1999

In vitro activity of several antimicrobial agents against 1003 isolates of Streptococcus pyogenes collected from Western Canada.

Streptococcus pyogenes is a common pathogen which may be associated with significant morbidity and mortality. Recent information is not readily available, in Canada, regarding the susceptibility of clinical isolates to penicillin, extended spectrum and/or newer agents. We collected and tested 1003 isolates of S. pyogenes to seven antimicrobial agents and found the following susceptibility rates: azithromycin 97%, ceftriaxone 100%, ciprofloxacin 99.4%, clarithromycin 98.5%, clindamycin 99.9%, erythromycin 96.5% and penicillin 100%. These results indicate that antimicrobial resistance is not yet a problem of S. pyogenes in Canada.

Adolescent↗
PubMed1975

Morphological and immunological characteristics of Streptococcus pyogenes, group A, type 50.

Streptococcus pyogenes, group A, type 50, in contrast to other group A streptococci, causes spontaneous disease in mice thereby providing a suitable experimental model for the study of human streptococcosis. Type 50 possesses various peculiar morphological and immunobiological characteristics and under certain conditions forms and extremely thick non-antigenic capsule which seems to interfere with the binding of antibody. This interference is most likely responsible for the difficulties in detecting type 50 streptococci in the tissues of infected mice by immunofluorescent staining. Whereas the surface components (hyaluronic acid, M-antigen) of the type 50 Streptococcus exhibit several uncommon features, the more deeply located cell wall antigens, like peptidoglycan and C-carbohydrate, do not differ in either their chemical constituents or their serological reactions from the comparable components of other group A streptococci.

Animals↗
PubMed1994

Characterization and distribution of insertion sequence IS1239 in Streptococcus pyogenes.

The human pathogenic bacterium Streptococcus pyogenes causes pharyngitis, acute rheumatic fever, glomerulonephritis and toxic-shock-like syndrome. The bacterium synthesizes several extracellular products, including the recently described streptococcal superantigen SSA, a molecule that shares considerable homology with several Staphylococcus aureus enterotoxins. While studying allelic variation at the ssa locus, six isolates expressing serotypes M4, M23, M33, M41, M43, and provisional type PT4854, were identified that had PCR products about 40-bp larger than expected, and one isolate (M15) had an amplified fragment that was more than 1-kb larger than expected. All six isolates have a 34-bp insert located 103 bp 5' of the ssa start codon. The larger product is a result of a 1110-bp insertion at the analogous location. The complementary strand of this insert has a 981-bp open reading frame that potentially encodes a 326-amino-acid polypeptide with substantial homology to the Escherichia coli IS30 transposase. Results of Southern blot analysis showed that at least twelve copies of the sequence are present in the serotype M15 S. pyogenes isolate. This element, designated IS1239, is the first simple insertion sequence described in group-A streptococci. Results of PCR screening showed that 26 of 78 (33%) S. pyogenes isolates expressing distinct M protein serotypes contained sequences with homology to IS1239, which means that the element is widely distributed in the species.

Amino Acid Sequence↗