Disease relevance of Streptococcus agalactiae

• L-ficolin binding and corresponding levels of C4 turnover were observed on LTA purified from other clinically important bacteria, including Streptococcus pyogenes and Streptococcus agalactiae [1].
• Aztreonam did not affect the activity of nafcillin against Staphylococcus aureus, or of ampicillin against species of Streptococcus group B or D [2].
• U-57930E inhibited methicillin-susceptible Staphylococcus aureus, Streptococcus pyogenes, Streptococcus agalactiae, and Streptococcus viridans at concentrations of less than or equal to 1 microgram/ml [3].
• A latex agglutination test system (Rapid Mastitis Test [RMT]; Immucell, Portland, Maine) containing reagents for the identification of Staphylococcus aureus and Streptococcus agalactiae from bovine intramammary infections was evaluated with 527 staphylococcal and 267 streptococcal isolates [4].
• Oxacillin-susceptible staphylococci (MIC90s, 0.5-2 micrograms/ml), beta-hemolytic Streptococcus group B (MIC90, 0.06 micrograms/ml), and Acinetobacter lwoffii were also susceptible to cefdinir [5].

High impact information on Streptococcus agalactiae

• In the present report, we show that crude extracts of Streptococcus agalactiae catalyze the gamma-GCS and GS reactions and can synthesize GSH from its constituent amino acids [6].
• A eukaryotic type serine/threonine kinase and phosphatase in Streptococcus agalactiae reversibly phosphorylate an inorganic pyrophosphatase and affect growth, cell segregation, and virulence [7].
• Regulation of purine biosynthesis by a eukaryotic-type kinase in Streptococcus agalactiae [8].
• Erythromycin resistance and genetic elements carrying macrolide efflux genes in Streptococcus agalactiae [9].
• Streptococcus agalactiae UCN36 was resistant to lincomycin (MIC = 16 microg/ml) but susceptible to clindamycin (MIC = 0.12 microg/ml) and erythromycin (MIC = 0.06 microg/ml) [10].

Chemical compound and disease context of Streptococcus agalactiae

• Glutathione synthesis in Streptococcus agalactiae. One protein accounts for gamma-glutamylcysteine synthetase and glutathione synthetase activities [6].
• High incidence of erythromycin resistance among clinical isolates of Streptococcus agalactiae in Taiwan [11].
• Opsonization of Streptococcus agalactiae of bovine origin by complement and antibodies against group B polysaccharide [12].
• The rates of resistance to erythromycin and clindamycin among Streptococcus agalactiae strains isolated in our hospital increased from 4.2 and 0.8% in 1993 to 17.4 and 12.1%, respectively, in 2001 [13].
• High-level chromosomal gentamicin resistance in Streptococcus agalactiae (group B) [14].

Biological context of Streptococcus agalactiae

• Immunochemistry of capsular type polysaccharide and virulence properties of type VI Streptococcus agalactiae (group B streptococci) [15].
• The glnA gene from the human pathogen Streptococcus agalactiae was cloned from a genomic library prepared with the lambda phage vector lambdaDASHII [16].
• Expression of phoZ in Escherichia coli, E. faecalis, Streptococcus agalactiae (group B streptococcus [GBS]), or Streptococcus pyogenes (group A streptococcus [GAS]) produces a blue-colony phenotype on plates containing a chromogenic substrate, 5-bromo-4-chloro-3-indolylphosphate (XP or BCIP) [17].
• The TraA relaxase autoregulates the putative type IV secretion-like system encoded by the broad-host-range Streptococcus agalactiae plasmid pIP501 [18].
• Binding of bovine fibronectin to mastitis-causing Streptococcus agalactiae induces adherence to solid substrate but not phagocytosis by polymorphonuclear cells [19].

Anatomical context of Streptococcus agalactiae

• Many group B Streptococcus agalactiae strains and other pathogenic streptococci express a cell-associated peptidase that inactivates C5a (C5a-ase), the major neutrophil chemoattractant produced by activation of the complement cascade [20].
• The type-specific capsular polysaccharide antigen of Streptococcus agalactiae has in previous experimental studies been considered a significant antiphagocytic factor, whereas the lipoteichoic acid moiety has been suggested to be a factor in adherence to human fetal cell lines [21].
• The role of macrophages in experimental arthritis induced by Streptococcus agalactiae sonicate: actions of macrophage colony-stimulating factor (CSF-1) and other macrophage-modulating agents [22].

Gene context of Streptococcus agalactiae

• The nt sequence of tetL from pJH1 was identical to that of the tetL present on pLS1 from Streptococcus agalactiae [23].
• The activities of the C3- and C5-convertases were assessed through the deposition on complement-activating bacteria (Streptococcus agalactiae) of C3 and C5 fragments, respectively [24].
• Cloning and characterization of a novel macrolide efflux gene, mreA, from Streptococcus agalactiae [25].
• Investigation of the translation-initiation factor IF2 gene, infB, as a tool to study the population structure of Streptococcus agalactiae [26].
• A NeuD homologue, Neu(III)D, from serotype III Streptococcus agalactiae (GBS) also restored capsule expression to the neuD deletion strain [27].

Analytical, diagnostic and therapeutic context of Streptococcus agalactiae

• Antibiotic susceptibility and mechanisms of erythromycin resistance in clinical isolates of Streptococcus agalactiae: French multicenter study [28].
• A rapid bioassay for determination of concentrations of clindamycin in serum was developed with use of a strain of Lancefield group B Streptococcus (Streptococcus agalactiae) that is uniformly resistant to aminoglycoside antibiotics, tetracycline, and polymyxin [29].
• The ability of lactoferrin (Lf) bound to Streptococcus agalactiae to interfere with the deposition of complement components on the bacterial surface was investigated by enzyme-linked immunosorbent assay (ELISA) [30].
• Cervical samples collected during speculum examination in 413 women were tested for the presence of Streptococcus agalactiae by Gram staining, a new latex agglutination test and standard cultures [31].
• Hyaluronic acid (HA) was treated with hyaluronate lyase (GBS HA lyase, E.C. 4.2.2.1, from Streptococcus agalactiae strain 4755), and the products have been analyzed by capillary electrophoresis (CE-UV and online CE-ESIMS), gel-permeation chromatography (GPC) and viscosimetric measurements [32].

References