Probing and pressing surfaces of hepatitis C virus-like particles
| Autor: | Simon Collett, Linda Earnest-Silveira, Aaron Elbourne, Paul A. Ramsland, Joseph Torresi, Dale Christiansen |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
Viral Hepatitis Vaccines
Genotype Surface Properties viruses Hepatitis C virus Hepacivirus Nanoparticle 02 engineering and technology Microscopy Atomic Force 010402 general chemistry medicine.disease_cause complex mixtures 01 natural sciences Virus Cell Line Biomaterials Colloid and Surface Chemistry Immune system Viral Envelope Proteins Lectins medicine Humans Particle Size chemistry.chemical_classification biology Biomolecule Virion virus diseases Biological Transport biochemical phenomena metabolism and nutrition 021001 nanoscience & nanotechnology biology.organism_classification Elasticity 0104 chemical sciences Surfaces Coatings and Films Electronic Optical and Magnetic Materials chemistry Biophysics Nanoparticles Particle size Carrier Proteins 0210 nano-technology Glycoprotein |
| Zdroj: | Journal of Colloid and Interface Science. 545:259-268 |
| ISSN: | 0021-9797 |
| Popis: | Hepatitis C virus-like particles (VLPs) are being developed as a quadrivalent vaccine candidate, eliciting both humoral and cellular immune responses in animal trials. Biophysical, biomechanical and biochemical properties are important for virus and VLP interactions with host cells and recognition by the immune system. Atomic force microscopy (AFM) is a powerful tool for visualizing surface topographies of cells, bionanoparticles and biomolecules, and for determining biophysical and biomechanical attributes such as size and elasticity. In this work, AFM was used to define morphological and nanomechanical properties of VLPs representing four common genotypes of hepatitis C virus. Significant differences in size of the VLPs were observed, and particles demonstrated a wide range of elasticity. Ordered packing of the core and potentially envelope glycoproteins was observed on the surfaces of the VLPs, but detailed structural characterization was hindered due to intrinsic dynamic fluctuations or AFM probe-induced damage of the VLPs. All VLPs were shown to be glycosylated in a manner similar to native viral particles. Together, the results presented in this study further our understanding of the nanostructure of hepatitis C VLPs, and should influence their uptake as viable vaccine candidates. |
| Databáze: | OpenAIRE |
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