0000000000726246
AUTHOR
Peter Saweljew
Membrane-penetrating Domain of Streptolysin O Identified by Cysteine Scanning Mutagenesis
Streptolysin O (SLO), a polypeptide of 571 amino acids, belongs to a family of highly homologous toxins that bind to cell membranes containing cholesterol and then polymerize to form large transmembrane pores. A conserved region close to the C terminus contains the single cysteine residue of SLO and has been implicated in membrane binding, which has been the only clear assignment of function to a part of the sequence. We have used a cysteine-less active mutant of SLO to introduce single cysteine residues at 19 positions distributed throughout the sequence. The cysteines were derivatized with the polarity-sensitive fluorophore acrylodan, and the fluorescence emission of the label was examine…
Case of fatal systemic infection with an Aureobacterium sp.: identification of isolate by 16S rRNA gene analysis
The case of a 75-year-old man who succumbed to a disseminated infection most likely caused by a species of the genus Aureobacterium is reported. Identification of the isolate was achieved by comparative 16S rRNA gene analysis. Aureobacteria are commonly found in the environment. However, only recently have they been recognized as a cause of infections including septicemia and soft tissue infections. To our knowledge, this is the first documentation of a fatal infection caused by an Aureobacterium sp.