Articles by Sonali Chaturvedi in JoVE
Simple and Robust in vivo and in vitro Approach for Studying Virus Assembly Sonali Chaturvedi1, Bongsu Jung2, Sharad Gupta2, Bahman Anvari2, A.L.N. Rao1 1Department of Plant Pathology and Microbiology, University of California, Riverside, 2Department of Bioengineering, University of California, Riverside A simple, efficient and robust way to synchronize the delivery of multiple viral components to plant cells via Agrobacterium-mediated transient expression is described. This approach is amenable for studying replication, encapsidation followed by in vitro reassembly of non-viral components into genome depleted optical viral ghosts suitable for biomedical applications.
Other articles by Sonali Chaturvedi on PubMed
Evaluation of Gastric Tolerability, Antinociceptive and Antiinflammatory Activity of Combination NSAIDs in Rats Indian Journal of Dental Research : Official Publication of Indian Society for Dental Research. Oct-Dec, 2009 | Pubmed ID: 20139563 Non-steroidal antiinflammatory drugs (NSAIDs) are one of the most commonly prescribed drugs in clinical practice. Presently, several varieties of fixed dose combinations (FDCs) of NSAIDs are available over the counter and are being prescribed too. There is paucity of literature regarding comparative efficacy of these combinations against their individual component. Various clinical studies have documented increased incidence of gastric ulcerations with usage of more than one NSAID simultaneously.
Packaging and Structural Phenotype of Brome Mosaic Virus Capsid Protein with Altered N-terminal Î²-hexamer Structure Virology. Oct, 2011 | Pubmed ID: 21864876 The first 45 amino acid region of brome mosaic virus (BMV) capsid protein (CP) contains RNA binding and structural domains that are implicated in the assembly of infectious virions. One such important structural domain encompassing amino acids 28QPVIV32, highly conserved between BMV and cowpea chlorotic mottle virus (CCMV), exhibits a Î²-hexamer structure. In this study we report that alteration of the Î²-hexamer structure by mutating 28QPVIV32 to 28AAAAA32 had no effect either on symptom phenotype, local and systemic movement in Chenopodium quinoa and RNA profile of in vivo assembled virions. However, sensitivity to RNase and assembly phenotypes distinguished virions assembled with CP subunits having Î²-hexamer from those of wild type. A comparison of 3-D models obtained by cryo electron microscopy revealed overall similar structural features for wild type and mutant virions, with small but significant differences near the 3-fold axes of symmetry.