Cervical Trident-Shaped Neurofibroma: A Rare Variant.

Spinal nerve root tumors can arise throughout the spine and at multiple levels, likely representing plexiform neurofibromas that grow from the nerve root into the intraspinal space either intradurally or epidurally and exit through the neural foramen, producing a dumbbell-shaped appearance. Although many cases of dumbbell-shaped extramedullary neurofibromas in the cervical spine have been reported, to the best of our knowledge, there are no reports of trident-shaped extramedullary neurofibromas. A 26-year-old woman presented with swelling over the right side of her neck. Diagnostic workup included magnetic resonance imaging (MRI) and contrast-enhanced computed tomography (CECT) of the neck, which revealed an intradural, extramedullary tumor mass at the right C2-C6 level with an extraspinal extension. Spinal cord compression or canal compromise is the most reliable indication for surgery. The solitary cervical neurofibroma was treated surgically in a single stage through laminoplasty and excision of the intradural tumor along with that of the neck component. This was performed without any complications. A single-stage double approach was adopted in this case. After total excision, the shape of the tumor was found to be more like a trident than a dumbbell. Hence, here we would like to suggest a new nomenclature for this neurofibroma, the trident neurofibroma.

What the Hel: recent advances in understanding rifampicin resistance in bacteria.

Rifampicin is a clinically important antibiotic that binds to, and blocks the DNA/RNA channel of bacterial RNA polymerase (RNAP). Stalled, nonfunctional RNAPs can be removed from DNA by HelD proteins; this is important for maintenance of genome integrity. Recently, it was reported that HelD proteins from high G+C Actinobacteria, called HelR, are able to dissociate rifampicin-stalled RNAPs from DNA and provide rifampicin resistance. This is achieved by the ability of HelR proteins to dissociate rifampicin from RNAP. The HelR-mediated mechanism of rifampicin resistance is discussed here, and the roles of HelD/HelR in the transcriptional cycle are outlined. Moreover, the possibility that the structurally similar HelD proteins from low G+C Firmicutes may be also involved in rifampicin resistance is explored. Finally, the discovery of the involvement of HelR in rifampicin resistance provides a blueprint for analogous studies to reveal novel mechanisms of bacterial antibiotic resistance.

Aspergillus Secondary Metabolite Database, a resource to understand the Secondary metabolome of Aspergillus genus.

Aspergillus is a genus of ubiquitous fungi that are pathologically & therapeutically important. Aspergillus Secondary Metabolites Database (A2MDB) is a curated compendium of information on Aspergillus & its secondary metabolome. A2MDB catalogs 807 unique non-redundantsecondary metabolites derived from 675 Aspergillus species. A2MDB has a compilation of 100 cellular targets of secondary metabolites, 44 secondary metabolic pathways, 150 electron and light microscopy images of various Aspergillus species. A phylogenetic representation of over 2500 strains has been provided. A2MDB presents a detailed chemical information of secondary metabolites and their mycotoxins. Molecular docking models of metabolite-target protein interactions have been put together. A2MDB also has epidemiological data representing Aspergillosis and global occurrence of Aspergillus species. Furthermore a novel classification of Aspergillosis along with 370 case reports with images, were made available. For each metabolite catalogued, external links to related databases have been provided. All this data is available on A2MDB, launched through Indian Institute of Chemical Technology, Hyderabad, India, as an open resource http://www.iictindia.org/A2MDB . We believe A2MDB is of practical relevance to the scientific community that is in pursuit of novel therapeutics.