In this study, berberine nanoparticles (BerNPs) were prepared using a wet-milling method with zirconium balls to enhance bioavailability and expand potential applications. The particle size and physicochemical properties of the BerNPs were analyzed using field-emission scanning electron microscopy (FE-SEM), UV-vis spectroscopy, X-ray diffraction, and Fourier-transform infrared spectroscopy. The broth dilution method was used to determine the antimicrobial activity of the BerNPs against ().
View Article and Find Full Text PDFHerpes simplex viruses (HSVs) are prevalent human pathogens that establish latency in human neuronal cells and efficiently evade the immune system. It has been a major medical challenge to eradicate them and, despite intensive efforts, an effective vaccine is not available. We previously showed that upon infection of antigen-presenting cells, HSV type 1 (HSV-1) rapidly and efficiently downregulates the major histocompatibility complex class I-like antigen-presenting molecule, CD1d, and potently inhibits its recognition by CD1d-restricted natural killer T (NKT) cells.
View Article and Find Full Text PDFIn human cytomegalovirus (HCMV)-infected cells, the 86 kDa immediate-early (IE) 2 protein plays a key role in transactivating downstream viral genes. Recently, IE2 has been shown to interact with histone deacetylase 1 (HDAC1) and HDAC3. HDAC1 recruited by IE2 was required for IE2-mediated autorepression of the major IE (MIE) promoter, whereas IE2-HDAC3 interaction was suggested to relieve the repressive effect of HDAC3 on viral early promoters.
View Article and Find Full Text PDFWe investigated the subcellular distribution of human ZBP1, which harbors the N-terminal Z-DNA binding domains, Zalpha and Zbeta. ZBP1 was distributed primarily in the cytoplasm and occasionally as nuclear foci in interferon (IFN)-treated primary hepatocellular carcinoma cells, and in several other transfected cell types. In leptomycin B (LMB)-treated cells, endogenous ZBP1 efficiently accumulated in nuclear foci, which overlapped PML oncogenic domains (PODs) or nuclear bodies (NBs).
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