June 12 – 17, 2022
Virus-like Particles (VLPs) are supramolecular arrangements of one or more viral proteins that resemble the structure of the native virus but are not infective, due the fact that they lack the viral genome. They have become very important in the field of novel recombinant vaccines, because of their biosafety and improved immunogenicity over subunit vaccines due to their particulate nature and highly repetitive epitope display. Moreover, they can elicit immune responses against heterologous antigens by the incorporation of epitopes by genic fusion to the viral proteins, constituting chimeric VLPs (cVLPs). In a previous work, by recombinant expression of the rabies G glycoprotein (RVG) in HEK293 cells, we stablished a platform to produce rabies VLPs as a new generation vaccine candidate 1–3. The main goal of this work was to generate a platform for heterologous antigen presentation based on RVG cVLPs. The heterologous epitope chosen for this study was the immunodominant site of Foot-and-Mouth Disease Virus (FMDV), named G-H loop (that is part of the capsid protein VP1), which is responsible of virus entry into the cell 4.
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Ernesto Garay, Diego Fontana, Lautaro Leschiutta, Ricardo Kratje, and Claudio Prieto, "Rational design, expression and characterization of chimeric rabies VLPs displaying the major antigenic site of Foot and Mouth Disease Virus" in "Vaccine Technology VIII", Tarit Mukhopadhyay, Merck Research Laboratories, USA; Charles Lutsch, Sanofi Pasteur, France; Linda Hwee-Lin Lua, University of Queensland, Australia; Francesc Godia, Universitat Autònoma de Barcelona, Spain Eds, ECI Symposium Series, (2022). https://dc.engconfintl.org/vaccine_viii/105