Molecular Identification of Cutaneous Alternariosis in a Renal Transplant Patient.

Cutaneous alternariosis is a rare condition, caused by an uncommon opportunistic pathogen. The most frequently affected individuals are immunosuppressed patients, e.g., organ transplant patients on immunosuppressive therapy. Clinical manifestations range from local skin lesions to disseminated disease. We present a case report of cutaneous alternariosis in a renal transplant recipient, confirmed by histological examination and molecular means. In addition, a review of the literature was performed.

Q fever across the Dutch border in Limburg province, Belgium.

Data from three different data sources were compiled to estimate the presence of Coxiella burnetii in the Belgian Limburg province for both humans and livestock. First, serological data of all samples sent to the Belgian reference centre (2003­2010) for human Q fever were analysed, showing evidence for an acute Q fever infection in 1­5% of the cases. Second, a multi-centre prospective survey was conducted in Limburg in 2010 to detect undiagnosed human cases; evidence for a recent infection with Coxiella burnetii was found in three out of 100 patients from which clinicians suspected a Mycoplasma pneumoniae infection. Third, we analyzed data from the Belgian livestock screening program (2009­2010) which consisted of investigating all reported abortions, sampling tank milk, and serological screening of cattle. The results suggest an endemicity in the Limburgian livestock which seems to be especially high in cattle.

Late onset of Strongyloides stercoralis meningitis in a retired Belgian miner.

We report a rare case of Strongyloides stercoralis meningitis in an immunocompromised patient treated for a lung carcinoma. Despite his Belgian origin, he was infected with S. stercoralis due to his former work as a miner. Although mostly prevalent in (sub)tropical areas, there are temperate regions where this nematode can occur.

Activation of trehalase during growth induction by nitrogen sources in the yeast Saccharomyces cerevisiae depends on the free catalytic subunits of cAMP-dependent protein kinase, but not on functional Ras proteins.

Addition of a nitrogen-source to glucose-repressed, nitrogen-starved G0 cells of the yeast Saccharomyces cerevisiae in the presence of a fermentable carbon source induces growth and causes within a few minutes a five-fold, protein-synthesis-independent increase in the activity of trehalase. Nitrogen-activated trehalase could be deactivated in vitro by alkaline phosphatase treatment, supporting the idea that the activation is triggered by phosphorylation. Yeast strains containing only one of the three TPK genes (which encode the catalytic subunit of cAMP-dependent protein kinase) showed different degrees of nitrogen-induced trehalase activation. The order of effectiveness was different from that previously reported for glucose-induced activation of trehalase in glucose-depressed yeast cells. Further reduction of TPK-encoded catalytic subunit activity by partially inactivating point mutations in the remaining TPK gene further diminished nitrogen-induced trehalase activation, while deletion of the BCY1 gene (which encodes the regulatory subunit) in the same strains resulted in an increase in the extent of activation. Deletion of the RAS genes in such a tpkw1 bcy1 strain had no effect. These results are consistent with mediation of nitrogen-induced trehalase activation by the free catalytic subunits alone. They support our previous conclusion that cAMP does not act as second messenger in this nitrogen-induced activation process and our suggestion that a novel nitrogen-induced signaling pathway integrates with the cAMP pathway at the level of the free catalytic subunits of protein kinase A. Western blot experiments showed that the differences in the extent of trehalase activation were not due to differences in trehalase expression. On the other hand, we cannot completely exclude that protein kinase A influences the nitrogen-induced activation mechanism itself rather than acting directly on trehalase. However, any such alternative explanation requires the existence of an additional, yet unknown, mechanism for activation of trehalase besides the well-established regulation by protein kinase A.

Nutrient-induced activation of trehalase in nutrient-starved cells of the yeast Saccharomyces cerevisiae: cAMP is not involved as second messenger.

Starvation of Saccharomyces cerevisiae cells for specific nutrients such as nitrogen, phosphate or sulphate causes arrest in the G1 phase of the cell cycle at a specific point called 'start'. Re-addition of different nitrogen sources, phosphate or sulphate to such starved cells causes activation of trehalase within a few minutes. Nitrogen-source- and sulphate-induced activation of trehalase were not associated with any change in the cAMP level, but in the case of phosphate there was a small transient increase. When nitrogen-source-activated trehalase was isolated by immuno-affinity chromatography from crude extracts, the purified enzyme showed the same activity profile as in the original crude extracts, indicating that post-translational modification is responsible for the activation. In the yeast mutants cdc25-5 and cdc35-10, which are temperature sensitive for cAMP synthesis, incubation at the restrictive temperature lowered but did not prevent nitrogen-, phosphate- or sulphate-induced activation of trehalase. Since under these conditions the cAMP level in the cells is very low, it is unlikely that cAMP acts as a second messenger in this nutrient-induced effect. Nitrogen-source-induced activation of trehalase requires the presence of glucose at a concentration similar to that able to stimulate the RAS-adenylate cyclase pathway. This indicates that the same glucose-sensing system might be involved in both phenomena. Nitrogen-starved cells fractionated according to cell size all showed nitrogen-source-induced activation of trehalase to the same extent, indicating that the nitrogen-induced signalling pathway involved is not dependent on the well-known cell size requirement for progression over the start point of the cell cycle.