A dimolybdenum paddlewheel as a building block for heteromultimetallic structures

Diphenylphosphine functionalized propionic acid was applied for the synthesis of heteromultimetallic dimolybdenum(II) complexes. The ligand features both carboxylic acid and phosphine functionalities, allowing the selective synthesis of a tetracarboxylate bridged Mo2(II)-paddlewheel structure in a first step. Due to the symmetrically arranged phosphine functionalities, the dimolybdenum(II) complex was utilized as a metalloligand. Subsequent coordination of late transition metal ions, such as gold(I), rhodium(I), iridium(I) or ruthenium(II) to the phosphine moieties allowed the formation of heteromultimetallic structures. The flexibility of the diphenylphosphino propionate ligand system enabled intermolecular aurophilic interactions in the Au(I) functionalized dimolybdenum(II) complexes. Depending on the Au(I) species applied, either a dimeric structure or a 1D coordination polymer was formed in the solid state. These structures represent the first examples of heterometallic dimolybdenum(II) complexes, forming supramolecular structures via aurophilic interactions

Ecto-5’-nucleotidase: Structure function relationships

Ecto-5’-nucleotidase (ecto-5’-NT) is attached via a GPI anchor to the extracellular membrane, where it hydrolyses AMP to adenosine and phosphate. Related 5’-nucleotidases exist in bacteria, where they are exported into the periplasmic space. X-ray structures of the 5’-nucleotidase from E. coli showed that the enzyme consists of two domains. The N-terminal domain coordinates two catalytic divalent metal ions, whereas the C-terminal domain provides the substrate specificity pocket for the nucleotides. Thus, the substrate binds at the interface of the two domains. Here, the currently available structural information on ecto-5’NT is reviewed in relation to the catalytic properties and enzyme function

Ecto-5′-nucleotidase and intestinal ion secretion by enteropathogenic Escherichia coli

Enteropathogenic Escherichia coli (EPEC) triggers a large release of adenosine triphosphate (ATP) from host intestinal cells and the extracellular ATP is broken down to adenosine diphosphate (ADP), AMP, and adenosine. Adenosine is a potent secretagogue in the small and large intestine. We suspected that ecto-5′-nucleotidase (CD73, an intestinal enzyme) was a critical enzyme involved in the conversion of AMP to adenosine and in the pathogenesis of EPEC diarrhea. We developed a nonradioactive method for measuring ecto-5′-nucleotidase in cultured T84 cell monolayers based on the detection of phosphate release from 5′-AMP. EPEC infection triggered a release of ecto-5′-nucleotidase from the cell surface into the supernatant medium. EPEC-induced 5′-nucleotidase release was not correlated with host cell death but instead with activation of phosphatidylinositol-specific phospholipase C (PI-PLC). Ecto-5′-nucleotidase was susceptible to inhibition by zinc acetate and by α,β-methylene-adenosine diphosphate (α,β-methylene-ADP). In the Ussing chamber, these inhibitors could reverse the chloride secretory responses triggered by 5′-AMP. In addition, α,β-methylene-ADP and zinc blocked the ability of 5′-AMP to stimulate EPEC growth under nutrient-limited conditions in vitro. Ecto-5′-nucleotidase appears to be the major enzyme responsible for generation of adenosine from adenine nucleotides in the T84 cell line, and inhibitors of ecto-5′-nucleotidase, such as α,β-methylene-ADP and zinc, might be useful for treatment of the watery diarrhea produced by EPEC infection

The antibody 2B4 directed against the Epstein-Barr virus (EBV)-encoded nuclear antigen I (EBNA I) detects MAGE-4: Implications for studies on the EBV association of human cancers.

We have previously developed two monoclonal antibodies against the Epstein-Barr Virus (EBV) nuclear antigen 1 (EBNA1), designated 1H4 and 2B4. Both detect EBNA1 by in situ staining in established EBV-positive tumours, e.g. Hodgkin's lymphoma and nasopharyngeal carcinoma. An association of EBV with other tumours, notably breast carcinomas, has been reported but remains controversial. Using the antibody 2B4, a nuclear protein has been detected in breast carcinomas that were EBV-negative by other methods, suggesting cross-reactivity with a cellular protein. Furthermore, an association of EBV with various other carcinomas has been reported on the basis of 2B4 immunohistochemistry. Here we show that 2B4 also binds to MAGE-4, a cancer testis antigen expressed in a variety of tumour cells, including breast carcinoma, seminoma and EBV-negative cases of Hodgkin's lymphoma. We conclude that the 2B4 antibody is not suitable for the detection of EBV infection but that additional techniques, particularly in situ hybridization for the detection of the EBV-encoded RNAs (EBERs), should be employed to confirm the presence of EBV. Our results add to the evidence indicating that breast cancer is not an EBV-associated disease

Report from the ISSI team meeting ``A Virtual Observatory for meteoroids''

International audienceThe content and format of the Virtual Meteor Observatory (VMO) was discussed in a one-week team meeting at the International Space Science Institute (ISSI) in Bern, Switzerland, in 2008 November. The current status of the VMO (in 'beta' version) was presented and discussed. The visual and camera sections are ready to be populated with data; a fireball section will be created. The radio/radar section is still open. In the discussion, several points were addressed: The relation to the Planetary Science Archive, treatment of shower catalogues, how to best perform astrometry, how to compute and store orbital data. The meeting ended by producing a list of future work, which is given at the end of the paper

Report from the ISSI team meeting "A Virtual Observatory for meteoroids''

The content and format of the Virtual Meteor Observatory (VMO) was discussed in a one-week team meeting at the International Space Science Institute (ISSI) in Bern, Switzerland, in 2008 November. The current status of the VMO (in 'beta' version) was presented and discussed. The visual and camera sections are ready to be populated with data; a fireball section will be created. The radio/radar section is still open. In the discussion, several points were addressed: The relation to the Planetary Science Archive, treatment of shower catalogues, how to best perform astrometry, how to compute and store orbital data. The meeting ended by producing a list of future work, which is given at the end of the paper

The VMO file format. I. Reduced camera meteor and orbit data

International audienceWe propose a standard XML-based file format for storing and transferring reduced data from photographic and video meteor observations and meteoroid orbits and trajectories. The format is the result of discussions within the Virtual Meteor Observatory (VMO) team, which aims to facilitate collaboration in the meteor science community and increase the scientific impact of combined observational data. The proposed format is extensible and allows meteoroid orbits and trajectories to be traced back to the original observing data and algorithms. We provide a description of the structure of the format and give precise definitions for each data field