In silico and in vitro studies on the assembling mechanism and structural stability of the capsid and VLP experimental production of the porcine Circovirus type 2b

• Grant number: 21/12487-8
• Support Opportunities: Regular Research Grants
• Start date: April 01, 2022
• End date: September 30, 2024
• Field of knowledge: Agronomical Sciences - Veterinary Medicine - Preventive Veterinary Medicine
• Principal Investigator: Angelo José Magro
• Grantee: Angelo José Magro
• Host Institution: Faculdade de Ciências Agronômicas (FCA). Universidade Estadual Paulista (UNESP). Campus de Botucatu. Botucatu , SP, Brazil
• Associated researchers: João Pessoa Araújo Junior
• Associated scholarship(s): 22/04023-4 - In silico studies on the assembling mechanism and structural stability of the capsid and VLP experimental production of the porcine circovirus type 2b, BP.TT

Abstract

Swine breeding has achieved a high development based on genetic improvement, nutrition, management and sanity. However, due to the intensive breeding methods, swine have become more susceptible to a higher number of infectious diseases. Among the most important pathogens that affect the swine world industry is the porcine circovirus 2 (PCV2), a small, icosahedral, non-enveloped virus, ambisense single-stranded circular DNA, composed by 1,767-1,768 nucleotides. This virus is highly resistant to environmental variations and disinfecting agents, endemic worldwide and has been associated to several distinct clinical manifestations that entail important economic losses to the producers. One of the factors possibly implicated in the PCV2 pathogenicity is the Cap protein, the fundamental unity that constitutes this virus capsid. Preliminary computational simulations conducted by our team indicated that certain interactions seem to be important for the cohesion of the PCV2 capsid and, possibly, assembling of this structure during the viral replication process. Thus, new in silico simulations and experimental tests aiming the confection of PCV2 artificial genomes will be conducted to identify the main intermolecular interactions present in the PCV2 capsid and test modifications that can lead to the production of enhanced structurally-stable viral particles and/or VLPs for the possible production of more immunogenic vaccine antigens. Furthermore, the production of VLPs more resistant to temperature variations is especially interesting for the production of vaccines used under field conditions. Therefore, the results of this work may provide extremely useful information for the future development of antiviral drugs and vaccines against PCV2. Further, this information and the standardization of the proposed procedures could be extremely useful for other similar studies involving the assembling mechanism of another virus responsible for diseases in humans and domestic animals. (AU)