Objective: Hepatitis E virus (HEV) infection is a major cause of acute hepatitis worldwide. The aim of the study is the development of plant expression system for the production of virus-like particles formed by HEV capsid and the characterization of their immunogenicity.
Results: Open reading frame (ORF) 2 encodes the viral capsid protein and possesses candidate for vaccine production. In this study, we used truncated genotype 3 HEV ORF 2 consisting of aa residues 110 to 610. The recombinant protein was expressed in Nicotiana benthamiana plants using the self-replicating potato virus X-based vector pEff up to 10% of the soluble protein fraction. The yield of HEV 110-610 after purification was 150-200 µg per 1 g of green leaf biomass. The recombinant protein formed nanosized virus-like particles. The immunization of mice with plant-produced HEV 110-610 protein induced high levels of HEV-specific serum antibodies.
Conclusions: HEV ORF 2 (110-610 aa) can be used as candidate for the development of a plant-produced vaccine against Hepatitis E.
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http://dx.doi.org/10.1007/s10529-020-02995-x | DOI Listing |
Elife
January 2025
Institute of Parasitology, Faculty of Agricultural and Environmental Sciences, McGill University, Montreal, Canada.
Paramyxovirus membrane fusion requires an attachment protein for receptor binding and a fusion protein for membrane fusion triggering. Nipah virus (NiV) attachment protein (G) binds to ephrinB2 or -B3 receptors, and fusion protein (F) mediates membrane fusion. NiV-F is a class I fusion protein and is activated by endosomal cleavage.
View Article and Find Full Text PDFJ Virol
December 2024
Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts, USA.
Unlabelled: Flavivirus envelope (E) and precursor M (prM) proteins, when ectopically expressed, assemble into empty, virus-like particles (VLPs). Cleavage of prM to M and loss of the pr fragment converts the VLPs from immature to mature particles, mimicking a similar maturation of authentic virions. Most of the VLPs obtained by prM-E expression are smaller than virions; early, low-resolution cryo-EM studies suggested a simple, 60-subunit, icosahedral organization.
View Article and Find Full Text PDFSubcell Biochem
December 2024
Centro de Biología Molecular "Severo Ochoa" (CSIC-UAM), and Department of Molecular Biology, Universidad Autónoma de Madrid, Madrid, Spain.
Virus particles (VPs) are naturally evolved nanomachines. Their outstanding molecular structures, physical and chemical properties, and biological activities make them potentially useful for many biomedical or technological applications. Natural VPs such as virions or capsids must, however, be modified by genetic and/or chemical engineering in order to become adequate for many specific uses.
View Article and Find Full Text PDFSubcell Biochem
December 2024
Centro de Investigación en Sanidad Animal (CISA-INIA/CSIC), Madrid, Spain.
Virus-like particles (VLPs) are formed by viral proteins that, when overexpressed, spontaneously self-assemble into particles that structurally are similar to infectious virus or subviral particles (e.g. the viral capsid).
View Article and Find Full Text PDFSci Rep
December 2024
Department of Anatomy, Faculty of Science, Mahidol University, 272 Rama VI Road, Ratchathewi, Bangkok, 10400, Thailand.
SARS-CoV-2, the cause of COVID-19, primarily targets lung tissue, leading to pneumonia and lung injury. The spike protein of this virus binds to the common receptor on susceptible tissues and cells called the angiotensin-converting enzyme-2 (ACE2) of the angiotensin (ANG) system. In this study, we produced chimeric Macrobrachium rosenbergii nodavirus virus-like particles, presenting a short peptide ligand (ACE2tp), based on angiotensin-II (ANG II), on their outer surfaces to allow them to specifically bind to ACE2-overexpressing cells called ACE2tp-MrNV-VLPs.
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