Plant dehydroascorbate reductase moonlights as membrane integrated ion channel.

Plant dehydroascorbate reductases (DHARs) are only known as soluble antioxidant enzymes of the ascorbate-glutathione pathway. They recycle ascorbate from dehydroascorbate, thereby protecting plants from oxidative stress and the resulting cellular damage. DHARs share structural GST fold with human chloride intracellular channels (HsCLICs) which are dimorphic proteins that exists in soluble enzymatic and membrane integrated ion channel forms. While the soluble form of DHAR has been extensively studied, the existence of a membrane integrated form remains unknown. We demonstrate for the first time using biochemistry, immunofluorescence confocal microscopy, and bilayer electrophysiology that Pennisetum glaucum DHAR (PgDHAR) is dimorphic and is localized to the plant plasma membrane. In addition, membrane translocation increases under induced oxidative stress. Similarly, HsCLIC1 translocates more into peripheral blood mononuclear cells (PBMCs) plasma membrane under induced oxidative stress conditions. Moreover, purified soluble PgDHAR spontaneously inserts and conducts ions in reconstituted lipid bilayers, and the addition of detergent facilitates insertion. In addition to the well-known soluble enzymatic form, our data provides conclusive evidence that plant DHAR also exists in a novel membrane-integrated form. Thus, the structure of DHAR ion channel form will help gain deeper insights into its function across various life forms.

AtSWEET11 and AtSWEET12 transporters function in tandem to modulate sugar flux in plants.

The sugar will eventually be exported transporter (SWEET) members in Arabidopsis, AtSWEET11 and AtSWEET12 are the important sucrose efflux transporters that act synergistically to perform distinct physiological roles. These two transporters are involved in apoplasmic phloem loading, seed filling, and sugar level alteration at the site of pathogen infection. Here, we performed the structural analysis of the sucrose binding pocket of AtSWEET11 and AtSWEET12 using molecular docking followed by rigorous molecular dynamics (MD) simulations. We observed that the sucrose molecule binds inside the central cavity and in the middle of the transmembrane (TM) region of AtSWEET11 and AtSWEET12, that allows the alternate access to the sucrose molecule from either side of the membrane during transport. Both AtSWEET11 and AtSWEET12, shares the similar amino acid residues that interact with sucrose molecule. Further, to achieve more insights on the role of these two transporters in other plant species, we did the phylogenetic and the in-silico analyses of AtSWEET11 and AtSWEET12 orthologs from 39 economically important plants. We reported the extensive information on the gene structure, protein domain and cis-acting regulatory elements of AtSWEET11 and AtSWEET12 orthologs from different plants. The cis-elements analysis indicates the involvement of AtSWEET11 and AtSWEET12 orthologs in plant development and also during abiotic and biotic stresses. Both in silico and in planta expression analysis indicated AtSWEET11 and AtSWEET12 are well-expressed in the Arabidopsis leaf tissues. However, the orthologs of AtSWEET11 and AtSWEET12 showed the differential expression pattern with high or no transcript expression in the leaf tissues of different plants. Overall, these results offer the new insights into the functions and regulation of AtSWEET11 and AtSWEET12 orthologs from different plant species. This might be helpful in conducting the future studies to understand the role of these two crucial transporters in Arabidopsis and other crop plants.

Myofibroblastic infiltration of the bowel: A case report and literature review.

INTRODUCTION: Inflammatory myofibroblastic tumours (IMTs), are uncommon tumours which can act with malignant potential. The management of these tumours can be extremely problematic but are often referred to surgical multi-disciplinary team meetings with the intention of surgical and oncological management (Chaudhary [1]). CASE REPORT: A 69-year-old gentleman was admitted with a 2-day history of abdominal pain and vomiting, and a 4-day history of absolute constipation. CT Abdomen Pelvis demonstrated distended loops of small bowel with pronounced fluid levels but no transition point. Intra-operative findings showed a right ileocolic mass adherent to the pelvic side wall and omental caking. Biopsies showed a florid myofibroblastic reaction, not a malignant process. CONCLUSION: IMTS are aggressive lesions but metastases is rare. Abdominal IMTS are difficult to diagnose and manage as they are often initially mistaken for lymphoma or peritoneal metastases. The therapy of choice is surgical resection of the tumour (Firat et al. [3]).

A lengthy primary intramedullary tuberculoma of the spinal cord extending from C4 to D8: A case report.

Spinal intramedullary tuberculoma is a rare cause of spinal cord compression. We report a case that had an intramedullary spinal cord tuberculomas where the diagnosis was made by MRI and biopsy. The clinical presentation was that of a cord compression in a 30-year-old male febrile patient. This case of intramedullary spinal tuberculoma with a longitudinally extending lesion of the cervicothoracic spine from C4 to D8 is presented for the rarity of its presentation.

Above the Sphenoid in to Dermoid-Expanded Endoscopic Two Nostrils Four Hand Technique: A Case Report.

This rare case report presents the 2 nostrils 4 hands expanded endoscopic excision of the suprasellar dermoid through planum sphenoidale approach. This minimally invasive technique through the natural passage offers panaromic view of vital structures, complete excision of the lesion with reconstruction of the skull base defect at the same procedure.

Asymmetric pore occupancy in crystal structure of OmpF porin from Salmonella typhi.

OmpF is a major general diffusion porin of Salmonella typhi, a Gram-negative bacterium, which is an obligatory human pathogen causing typhoid. The structure of S. typhi Ty21a OmpF (PDB Id: 3NSG) determined at 2.8 Å resolution by X-ray crystallography shows a 16-stranded ß-barrel with three ß-barrel monomers associated to form a trimer. The packing observed in S. typhi Ty21a rfOmpF crystals has not been observed earlier in other porin structures. The variations seen in the loop regions provide a starting point for using the S. typhi OmpF for structure-based multi-valent vaccine design. Along one side of the S. typhi Ty21a OmpF pore there exists a staircase arrangement of basic residues (20R, 60R, 62K, 65R, 77R, 130R and 16K), which also contribute, to the electrostatic potential in the pore. This structure suggests the presence of asymmetric electrostatics in the porin oligomer. Moreover, antibiotic translocation, permeability and reduced uptake in the case of mutants can be understood based on the structure paving the way for designing new antibiotics.