Several approaches have been developed to analyze the entry of highly pathogenic viruses. In this study, we report the implementation of a Bimolecular Multicellular Complementation (BiMuC) assay to safely and efficiently monitor SARS-CoV-2 S-mediated membrane fusion without the need for microscopy-based equipment. Using BiMuC, we screened a library of approved drugs and identified compounds that enhance S protein-mediated cell-cell membrane fusion.
View Article and Find Full Text PDFThe protein C is a small viral protein encoded in an overlapping frame of the P gene in the subfamily Orthoparamyxovirinae. This protein, expressed by alternative translation initiation, is a virulence factor that regulates viral transcription, replication, and production of defective interfering RNA, interferes with the host-cell innate immunity systems and supports the assembly of viral particles and budding. We expressed and purified full-length and an N-terminally truncated C protein from Tupaia paramyxovirus (TupV) C protein (genus Narmovirus).
View Article and Find Full Text PDFSeveral methods have been developed to explore interactions among water-soluble proteins or regions of proteins. However, techniques to target transmembrane domains (TMDs) have not been examined thoroughly despite their importance. Here, we developed a computational approach to design sequences that specifically modulate protein-protein interactions in the membrane.
View Article and Find Full Text PDFBackground: Necrotising fasciitis is a potentially life-threatening soft tissue infection that mainly affects the fascia and deep planes, with a very high mortality rate and severe related complications.
Aim: To evaluate clinical and demographic characteristics of patients with necrotising fasciitis in our hospital and to describe their diagnostic and therapeutic management.
Material And Methods: Retrospective review of medical records of 21 patients diagnosed with necrotising fasciitis with limb involvement between January 2003 and February 2021 in our hospital.