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Budded viruses (BVs) of baculovirus such as nucleopolyhedrovirus (AcNPV) have recently been studied as biological nanomaterials, and methods for their longer-term storage without deterioration would be desirable. The cryopreservation of virions with a naturally occurring saccharide like trehalose as a cryoprotectant is known to be useful for maintaining the viral structure and function. In this study, we examined how useful trehalose is as protectant for BV cryopreservation during repeated freeze-thaw cycles: 1) membrane fusion between liposomes (multilamellar vesicles, MLVs) and BVs, 2) infection of insect culture cells (Sf9 cells) by RFP-expressing BVs, and 3) morphologies of these BVs were investigated by fluorescent dequenching assay, fluorescence microscopy, and transmission electron microscopy (TEM), respectively. The results suggest that the BVs deteriorate in quality with each freeze-thaw cycle, and this deterioration can be diminished with the use of trehalose to an extent similar to that seen with storage on ice.
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http://dx.doi.org/10.1080/09168451.2019.1704396 | 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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