Fermenter Growth of Streptococcus agalactiae and Large-scale Production of CAMP Factor

Huser, Hans; Goeke, L.; Karst, G.; Fehrenbach, F. J.

doi:10.1099/00221287-129-5-1295

Cited by 9 publications

(9 citation statements)

References 25 publications

(7 reference statements)

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“…During this time, bacteria in suspension continued to produce lactate. However, in artificial media such as the BHI broth, S. mutans are known to grow in chains (Huser et al 1983), and when these chains become long enough they precipitate due to increased weight. This requires some time to occur, perhaps a few hours, depending on the experimental conditions.…”

Section: Discussionmentioning

confidence: 99%

The antibacterial effects of silver, titanium dioxide and silica dioxide nanoparticles compared to the dental disinfectant chlorhexidine onStreptococcus mutansusing a suite of bioassays

2012

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Metal-containing nanomaterials have the potential to be used in dentistry for infection control, but little is known about their antibacterial properties. This study investigated the toxicity of silver (Ag), titanium dioxide and silica nanoparticles (NPs) against the oral pathogenic species of Streptococcus mutans, compared to the routine disinfectant, chlorhexidine. The bacteria were assessed using the minimum inhibitory concentration assay for growth, fluorescent staining for live/dead cells, and measurements of lactate. All the assays showed that Ag NPs had the strongest antibacterial activity of the NPs tested, with bacterial growth also being 25-fold lower than that in chlorhexidine. The survival rate of bacteria under the effect of 100 mg l−1 Ag NPs in the media was 2% compared to 60% with chlorhexidine, while the lactate concentration was 0.6 and 4.0 mM, respectively. Silica and titanium dioxide NPs had limited effects. Dialysis experiments showed negligible silver dissolution. Overall, Ag NPs were the best disinfectant and performed better than chlorhexidine. Improvements to the MIC assay are suggested.

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Section: Discussionmentioning

confidence: 99%

The antibacterial effects of silver, titanium dioxide and silica dioxide nanoparticles compared to the dental disinfectant chlorhexidine onStreptococcus mutansusing a suite of bioassays

2012

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“…Fermenter cultivation of group B streptococci was performed in trypticase peptone broth (No. 11921 ; Becton Dickinson & Co., Mountain View, CA) as reported earlier (34).…”

mentioning

confidence: 94%

“…Inactivation of Hemolytic Activity of Protein B by Ig. Hemolytic activity was determined using the kinetic assay as described (34). The interaction of Ig with protein B was detected by inhibition of the CAMP reaction after incubation with individual Ig fractions.…”

mentioning

confidence: 99%

Unspecific binding of group B streptococcal cocytolysin (CAMP factor) to immunoglobulins and its possible role in pathogenicity.

Jürgens¹,

Sterzik²,

Fehrenbach³

1987

The Journal of Experimental Medicine

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The protein B of group B streptococci can bind in a nonimmune reaction to Ig of the IgG and IgM classes of various mammalian species (i.e., human, mouse, rabbit, and bovine). Protein B binding involves the Fc parts of both IgG and IgM molecules. Monoclonal or polyclonal IgG or IgM and the IgM-FC5 mu fragment of human myeloma protein combined with the protein B thereby inhibiting protein B-induced hemolysis in the CAMP reaction. The protein B/Ig complex can be dissociated with 1% Triton or guanidine-HCl (6 M). Mice infected intraperitoneally with sublethal doses of group B streptococci (GBS) and that received seven repeated intravenous injections of highly purified protein B during the first 9 h of infection developed fatal septicemia within 24 h with colony counts of up to 10(8) CFU/ml in the blood. Animals treated in the same way with either PBS or trypsinized protein B recovered. The protein B itself was not pathogenic when injected into healthy mice. Tissue sections of liver or spleen from mice infected with a lethal dose of GBS revealed the presence of protein B together with large numbers of cocci when stained by the peroxidase method using specific antibodies raised against purified protein B in the rabbit.

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“…Fehrenbach et al optimized the cultural conditions for bacterial expression of GBS CAMP-factor [17] and subsequently, the methods for purification [19]. Utilizing the purified protein, they could demonstrate different physico-chemical properties of fragments derived from the CAMP-factor [35] and a nonspecific, weak binding of the protein to IgG and IgM from several mammalian species [20].…”

Section: Introductionmentioning

confidence: 99%

Molecular characterization of the cfb gene encoding group B streptococcal CAMP-factor

Podbielski

Blankenstein

Lütticken

1994

Med Microbiol Immunol

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An internal fragment of the cfb gene from group B streptococcal (GBS) strain R268 was amplified by polymerase chain reaction (PCR) using degenerate primers with sequences derived from the CAMP-factor amino acid (aa) sequence of GBS strain NCTC8181 [Rühlmann et al. (1988) FEBS Lett 235:262-266]. After cloning and sequencing this fragment, the remainder of cfb and the adjacent 5' and 3' sequences were amplified by inverted PCR of genomic DNA and directly sequenced from the PCR product. Within the 1560 bp sequenced, a complete cfb gene deviating in two deduced aa residues from the published sequence was identified. In addition, the cfbR268 sequence contained a 29-aa leader peptide. Using primers directed to the 5' and 3' ends of cfb for PCR, a cfb gene of uniform size could be detected in 19 clinical GBS isolates including three phenotypically CAMP-negative strains. Utilizing Northern blot analysis and primer extension assays, the cfbR268 promoter was located and the length of the cfb transcript was assessed at about 1100 bp. In a parallel experiment, no cfb transcript could be detected from the CAMP-negative GBS strain 74-360. The complete cfbR268 gene and different portions of its 5' and 3' ends were cloned into the plasmid pJLA602 and expressed in E. coli DH5 alpha. The recombinant peptides could be detected by Western immunoblots with polyclonal antiserum. Only the full-sized recombinant CAMP-factor was found to exert co-hemolytic activity in a sheep-blood agar assay. This co-hemolytic activity could be inhibited by anti-CAMP antiserum.

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Fermenter Growth of Streptococcus agalactiae and Large-scale Production of CAMP Factor

Cited by 9 publications

References 25 publications

The antibacterial effects of silver, titanium dioxide and silica dioxide nanoparticles compared to the dental disinfectant chlorhexidine onStreptococcus mutansusing a suite of bioassays

The antibacterial effects of silver, titanium dioxide and silica dioxide nanoparticles compared to the dental disinfectant chlorhexidine onStreptococcus mutansusing a suite of bioassays

Unspecific binding of group B streptococcal cocytolysin (CAMP factor) to immunoglobulins and its possible role in pathogenicity.

Molecular characterization of the cfb gene encoding group B streptococcal CAMP-factor

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