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Structural study of components of the classical nuclear transport pathway related to porcine circovirus type 2 (PCV2) using artificial intelligence techniques

Grant number: 20/14277-8
Support type:Scholarships in Brazil - Scientific Initiation
Effective date (Start): January 01, 2021
Effective date (End): December 31, 2021
Field of knowledge:Agronomical Sciences - Veterinary Medicine - Preventive Veterinary Medicine
Principal researcher:Angelo José Magro
Grantee:Lucas Hecker Vasques
Home Institution: Faculdade de Ciências Agronômicas (FCA). Universidade Estadual Paulista (UNESP). Campus de Botucatu. Botucatu , SP, Brazil

Abstract

In recent years, Brazil has achieved a prominent position in the production of pork. Although intensive breeding methods provide high productivity, there are many challenges in pig farming, including infectious diseases. Porcine Circovirus Type 2 (PCV2) is a viral pathogen associated with a series of clinical manifestations in swine. Importins are proteins responsible for transporting other proteins to the cell nucleus, being classified into Importins-alfa (Imp alfa) and Importins-beta (Imp beta). In the classic nuclear import pathway, for a protein to be transported, it must contain a Nuclear Localization Sequence (NLS), which interacts with an Imp±. Site-directed mutagenesis experiments demonstrated that the 41 N-terminal amino acid residues of the PCV2 capsid protein are essential for it to be imported into the nucleus, checking for the presence of an NLS in that sequence. Despite this, studies on the interaction between residues of this sequence and Imp± are not yet available. Thus, in order to characterize this possible complex, we propose to carry out structural computational studies based on artificial intelligence (deep learning), in order to determine the occurrence of interaction or not between the PCV2 NLS and the alfa2 isoform of the Importine-alfa Mus musculus. In the case of confirmation of the possibility of interaction, also intend to classify the most probable complexes based on thermodynamic and structural parameters and to identify the most important interface contacts for the formation of this complex. The results of this project may contribute to the understanding of how PCV2 interacts with host cell proteins and have the potential to generate useful knowledge for the future development of antiviral drugs and/or other products of biotechnological interest.

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