Publications by authors named "Xia-Fei Wei"
The Nucleocapsid Protein (NP) of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is not only the core structural protein required for viral packaging, but also participates in the regulation of viral replication, and its post-translational modifications such as phosphorylation have been shown to be an important strategy for regulating virus proliferation. Our previous work identified NP could be ubiquitinated, as confirmed by two independent studies. But the function of NP ubiquitination is currently unknown.
View Article and Find Full Text PDFHepatitis B virus (HBV) infection is a serious global health problem. After the viruses infect the human body, the host can respond to the virus infection by coordinating various cellular responses, in which mitochondria play an important role. Evidence has shown that mitochondrial proteins are involved in host antiviral responses.
View Article and Find Full Text PDFBiotin proximity labeling is a technique based on the TurboID enzyme that can be used to capture weak or dynamic interactions that had previously not been used to map proteins interacting with a specific DNA sequence. Here, we present a protocol for identifying specific DNA-sequence-binding proteins. We describe steps for biotin labeling of DNA-binding proteins, protein enrichment and sodium dodecyl sulfate polyacrylamide gel electrophoresis separation, and proteomic analysis.
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- Caspases are important proteases involved in cell death and inflammation, and new biosensors called NanoLocks, based on NanoLuc luciferase, were developed to detect their activity.
- The NanoLock sensors operate on a dark-to-bright model and show significant activation responses, achieving a 1233-fold increase in signal with tobacco etch virus protease and over 500-fold with caspase 3.
- These sensors outperform commercial kits in terms of signal-to-noise ratio and convenience, with successful testing in human cells and the establishment of a cell line for screening caspase 6 modulators.
The core promoter (CP) of hepatitis B virus (HBV) is critical for HBV replication by controlling the transcription of pregenomic RNA (pgRNA). Host factors regulating the activity of the CP can be identified by different methods. Biotin-based proximity labeling, a powerful method with the capability to capture weak or dynamic interactions, has not yet been used to map proteins interacting with the CP.
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- The hepatitis B virus capsid is a key target for antiviral therapies against chronic infection.
- Current treatments mainly focus on core protein interactions, but there has been limited research on the interactions between core monomers due to the lack of screening models.
- A new cell-based assay using split luciferase complementation identified Arbidol and 20-deoxyingenol as compounds that can regulate core dimerization and inhibit HBV DNA replication, proving the model's potential for screening new antiviral agents.
Article Synopsis
- Fusion core proteins of Hepatitis B virus (HBV) can aid in understanding core protein functions and their movement within cells.
- A method was developed to create these fusion proteins that retains some functionality by using long Glycine-serine linkers and attaching proteins at the N terminus of HBc.
- The study found that the GFP-GS186-HBc and RFP-G4S47-HBc fusion proteins helped rescue HBV replication but did not support the formation of relaxed circular DNA, indicating their potential use for tracking HBc and capsid activity in research.