Clinical workstations supporting evidence-based medicine.

The application of the principles of evidence-based medicine is based on a rigorous analysis of clinical research tailored to the individual characteristics of a specific patient. Thus the physician must have information about the patient and about the latest results of clinical research simultaneously. We present a computer-based clinical workstation offering sources for both kinds of information: the current patient data is delivered by access to the electronic patient record and the results of research may be searched at the Internet, Intranet, or other online databases. Performing an evaluation study we are testing this configuration in the setting of a university hospital. The physicians are interviewed about their use of the single information sources and their consequences for clinical research and evidence-based medicine. We hope to show that in spite of some technical and methodological problems the clinical workstation is a promising tool for decision-making at the clinical workplace.

ymoA, a Yersinia enterocolitica chromosomal gene modulating the expression of virulence functions.

The virulence functions of Yersinia enterocolitica include the pYV-encoded Yop proteins and YadA adhesin as well as the chromosome-encoded enterotoxin, Yst. The yop and yadA genes form a temperature-activated regulon controlled by the transcriptional activator VirF. Gene virF, also localized on pYV, is itself thermoinduced in the absence of other pYV genes. The enterotoxin yst gene is silent in some collection strains including strain W22703. This paper describes two Tn5-Tc1 chromosomal insertion mutants of W22703 transcribing virF, and hence the yop and yadA genes, at low temperature. These mutants also resumed their production of Yst, with its typical temperature dependence. Both mutations were insertions in the same gene called ymoA for 'Yersinia modulator'. The cloned ymoA gene fully complemented the two mutations. Several properties of the mutants suggest that ymoA encodes a histone-like protein. According to the nucleic acid sequence, the product of ymoA is an 8064 Da protein rich in aspartic acid (9%), glutamic acid (9%) and lysine (10.5%), but the predicted amino acid sequence shows no similarity with any described histone-like protein. This work supports recent reports which propose a role for DNA topology and bacterial chromatin structure in thermoregulation of virulence functions.