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J Raff

Publications and source records attributed to J Raff.

9 recordsLinked to original sources

Manufacturing and characterization of Pd nanoparticles formed on immobilized bacterial cells.

AIMS: To fabricate and analyse Pd nanoparticles on immobilized bacterial cells. METHODS AND RESULTS: Biological ceramic composites (biocers) were used as a template to produce Pd(0) nanoparticles. The metal-binding cells of the uranium mining waste pile isolate, Bacillus sphaericus JG-A12 were used as a biological component of the biocers and immobilized by using sol-gel technology. Vegetative cells and surface-layer proteins of this strain are known to bind high amounts of Pd(II) that can be reduced to Pd(0) particles by the addition of a reducing agent. Sorption of Pd(II) by the biocers from a metal complex solution was studied by inductively coupled plasma mass spectroscopy analyses. After embedding into sol-gel ceramics, the cells retained their Pd(II)-binding capability. Pd(0) nanoclusters were produced by the addition of hydrogen as reducing agent after the sorption of Pd(II). The interactions of Pd(0) with the biocers and the formed Pd(0) nanoparticles were investigated by extended X-ray absorption fine structure spectroscopy. The particles had a size of 0.6-0.8 nm. CONCLUSIONS: Bacterial cells that were immobilized by embedding into sol-gel ceramics were used as a template to produce Pd nanoclusters of a size smaller than 1 nm. These particles possess interesting physical and chemical properties. SIGNIFICANCE AND IMPACT OF THE STUDY: The use of embedded bacterial cells as template enabled the fabrication of immobilized Pd(0) nanoparticles. These particles are highly interesting for technical applications, such as the development of novel catalysts.

Bacillus↗

Metal binding by bacteria from uranium mining waste piles and its technological applications.

Uranium mining waste piles, heavily polluted with radionuclides and other toxic metals, are a reservoir for bacteria that have evolved special strategies to survive in these extreme environments. Understanding the mechanisms of bacterial adaptation may enable the development of novel bioremediation strategies and other technological applications. Cell isolates of Bacillus sphaericus JG-A12 from a uranium mining waste pile in Germany are able to accumulate high amounts of toxic metals such as U, Cu, Pb, Al, and Cd as well as precious metals. Some of these metals, i.e. U, Cu, Pd(II), Pt(II) and Au(III), are also bound by the highly orderd paracrystalline proteinaceous surface layer (S-layer) that envelopes the cells of this strain. These special capabilities of the cells and the S-layer proteins of B. sphaericus JG-A12 are highly interesting for the clean-up of uranium contaminated waste waters, for the recovery of precious metals from electronic wastes, and for the production of metal nanoclusters. The fabricated nanoparticles are promising for the development of novel catalysts. This work reviews the molecular biology of the S-layer of the strain JG-A12 and the S-layer dependent interactions of the bacterial cells with metals. It presents future perspectives for their application in bioremediation and nanotechnology.

Bacillus↗

Polyanionic (i.e., polysulfonate) dendrimers can inhibit the replication of human immunodeficiency virus by interfering with both virus adsorption and later steps (reverse transcriptase/integrase) in the virus replicative cycle.

Polyanionic dendrimers were synthesized and evaluated for their antiviral effects. Phenyldicarboxylic acid (BRI6195) and naphthyldisulfonic acid (BRI2923) dendrimers were found to inhibit the replication of human immunodeficiency virus type 1 (HIV-1; strain III(B)) in MT-4 cells at a EC(50) of 0.1 and 0.3 microg/ml, respectively. The dendrimers were not toxic to MT-4 cells up to the highest concentrations tested (250 microg/ml). These compounds were also effective against various other HIV-1 strains, including clinical isolates, HIV-2 strains, simian immunodeficiency virus (SIV, strain MAC(251)), and HIV-1 strains that were resistant to reverse transcriptase inhibitors. HIV strains containing mutations in the envelope glycoprotein gp120 (engendering resistance to known adsorption inhibitors) displayed reduced sensitivity to the dendrimers. The compounds inhibited the binding of wild-type virus and recombinant virus (containing wild-type gp120) to MT-4 cells at concentrations comparable to those that inhibited the replication of HIV-1(III(B)) in these cells. Cellular uptake studies indicated that BRI2923, but not BRI6195, permeates into MT-4 and CEM cells. Accordingly, the naphtyldisulfonic acid dendrimer (BRI2923) proved able to inhibit later steps of the replication cycle of HIV, i.e., reverse transcriptase and integrase. NL4.3 strains resistant to BRI2923 were selected after passage of the virus in the presence of increasing concentrations of BRI2923. The virus mutants showed 15-fold reduced sensitivity to BRI2923 and cross-resistance to known adsorption inhibitors. However, these virus mutants were not cross-resistant to reverse transcriptase inhibitors or protease inhibitors. We identified several mutations in the envelope glycoprotein gp120 gene (i.e., V2, V3, and C3, V4, and C4 regions) of the BRI2923-resistant NL4.3 strains that were not present in the wild-type NL4.3 strain, whereas no mutations were found in the reverse transcriptase or integrase genes.

Animals↗

[Effect of primary surgical therapy on the course of C-cell carcinoma of the thyroid gland].

The effect of the type of initial surgery for medullary thyroid carcinoma on the outcome is obscure. Some 40 patients with hereditary medullary thyroid carcinoma underwent either thyroidectomy and modified radical neck dissection (n = 18), subtotal thyroid resection (n = 10), or thyroidectomy (n = 12), partly with selective lymphadenectomy, as initial surgery. Patients who underwent thyroidectomy and modified radical neck dissection as their first operation had higher cure rates and lower morbidity. Thus the initial procedure is decisive for the further outcome in patients with hereditary medullary thyroid carcinoma.

Adolescent↗

Mitosis in motion.

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Journal Article↗

CP60: a microtubule-associated protein that is localized to the centrosome in a cell cycle-specific manner.

DMAP190 is a microtubule-associated protein from Drosophila that is localized to the centrosome. In a previous study, we used affinity chromatography to identify proteins that interact with DMAP190, and identified a 60-kDa protein that we named DMAP60 (Kellogg and Alberts, 1992). Like DMAP190, DMAP60 interacts with microtubules and is localized to the centrosome, and the two proteins associate as part of a multiprotein complex. We now report the cloning and sequencing of the cDNA encoding DMAP60. The amino acid sequence of DMAP60 is not homologous to any protein in the database, although it contains six consensus sites for phosphorylation by cyclin-dependent kinases. As judged by in situ hybridization, the gene for DMAP60 maps to chromosomal region 46A. In agreement with others working on Drosophila centrosomal proteins, we have changed the names for DMAP190 and DMAP60 to CP190 and CP60, respectively, to give these proteins a consistent nomenclature. Antibodies that recognize CP60 reveal that it is localized to the centrosome in a cell cycle-dependent manner. The amount of CP60 at the centrosome is maximal during anaphase and telophase, and then drops dramatically during late telophase or early interphase. This dramatic disappearance of CP60 may be due to specific proteolysis, because CP60 contains a sequence of amino acids similar to the "destruction box" that targets cyclins for proteolysis at the end of mitosis. Starting with nuclear cycle 12, CP60 and CP190 are both found in the nucleus during interphase. CP60 isolated from Drosophila embryos is highly phosphorylated, and dephosphorylated CP60 is a good substrate for cyclin B/p34cdc2 kinase complexes. A second kinase activity capable of phosphorylating CP60 is present in the CP60/CP190 multiprotein complex. We find that bacterially expressed CP60 binds to purified microtubules, and this binding is blocked by CP60 phosphorylation.

Amino Acid Sequence↗