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The class II membrane fusion induced by flavivirus E proteins is a unique pH-dependent membrane fusion process differently from the class I or III membrane fusion by other enveloped virus proteins. The fusion peptide on the DII of the flavivirus E proteins can insert into the cell membrane as a cell entry process besides the receptor bindings. A traditional assay using C6/36 mosquito cells infected by dengue viruses has been previously reported but did not provide efficient quantitation to measure the virus-triggered membrane fusion. Here we reported the development of a quantitative cell fusion assay for four serotypes of dengue viruses and the recently emerged Zika viruses. We used a pCI-neo vector encoding the prME genes of dengue and Zika viruses and investigated the cell fusion in transfected 293, Vero and CHO cells. Donor cells were co-transfection of the prME genes of dengue and Zika prME gene and T7 RNA polymerase to react with the indicator cells transfected with the luciferase gene under the control of the T7 promoter. Quantification of the virus-induced cell fusion was determined by the luciferase expression levels under a switch of pH from 7.4 to 5.4 in the co-cultured donor and indicator cells. The quantitative luciferase-based assay was applied to measure the anti-fusion activity by two monoclonal antibodies mAb 4G2 and mAb DB42 against dengue virus infections. This assay could quality as a quantitative bioassay for testing the potency of anti-fusion monoclonal antibodies.
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http://dx.doi.org/10.1080/21645515.2020.1748989 | DOI Listing |
J Extracell Vesicles
September 2025
IRSD, Université de Toulouse, INSERM, INRAE, ENVT, Toulouse, France.
Outer membrane vesicles (OMVs) are nanosized vesicles naturally secreted by Gram-negative bacteria and represent a promising platform for vaccine development. OMVs possess inherent immunostimulatory properties due to the presence of pathogen-associated molecular patterns (PAMPs), providing self-adjuvanting capabilities and the ability to elicit both innate and adaptive immune responses. This review outlines the advantages of OMVs over traditional vaccine strategies, including their safety, modularity, and the potential for genetic engineering to enable targeted antigen delivery.
View Article and Find Full Text PDFFront Immunol
September 2025
Department of Pediatrics, Division of Infectious Diseases, Emory University School of Medicine, Atlanta, GA, United States.
Introduction: Interferon-induced transmembrane proteins (IFITMs) inhibit the entry of diverse enveloped viruses. The spectrum of antiviral activity of IFITMs is largely determined by their subcellular localization. IFITM1 localizes to and primarily blocks viral fusion at the plasma membrane, while IFITM3 prevents viral fusion in late endosomes by accumulating in these compartments.
View Article and Find Full Text PDFFront Biosci (Landmark Ed)
August 2025
Department of Spine Surgery, Zhongda Hospital Southeast University, 210009 Nanjing, Jiangsu, China.
Background: After spinal cord injury (SCI), pro-inflammatory microglia accumulate and impede axonal regeneration. We explored whether secreted protein acidic and rich in cysteine (Sparc) restrains microglial inflammation and fosters neurite outgrowth.
Methods: Mouse microglial BV2 cells were polarized to a pro-inflammatory phenotype with lipopolysaccharides (LPSs).
Front Biosci (Landmark Ed)
August 2025
University of Angers, MitoLab, Unité MITOVASC, UMR CNRS 6015, INSERM U1083, SFR ICAT, 49330 Angers, France.
The bioenergetic machinery of the cell is protected and structured within two layers of mitochondrial membranes. The mitochondrial inner membrane is extremely rich in proteins, including respiratory chain complexes, substrate transport proteins, ion exchangers, and structural fusion proteins. These proteins participate directly or indirectly in shaping the membrane's curvature and facilitating its folding, as well as promoting the formation of nanotubes, and proton-rich pockets known as cristae.
View Article and Find Full Text PDFDev Biol
September 2025
Department of Biological Sciences, University of Denver, Denver, CO 80208, USA; Department of Biochemistry and Biophysics, AgriLife Research, Texas A&M University, College Station, TX 77843, USA. Electronic address:
During fertilization, sperm and egg membranes signal and fuse to form a zygote and begin embryonic development. As lipids participate in signaling and membrane fusion, we investigated the role of lipid asymmetry in gametogenesis, fertilization, and embryogenesis. We show that the lipid flippase TAT-5, an essential P4-ATPase that maintains phosphatidylethanolamine asymmetry, is required for both oocyte formation and sperm activation, albeit at different levels of flippase activity.
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