Abstract:

[Objective] This study aimed to analyze the structure and function of African swine fever virus （ASFV） pI215L protein. [Method] A total of 29 pI215L gene sequences of different ASFV strains were downloaded from the African Swine Fever Virus Database （ASFVdb）. Bioinformatics tools were used to analyze the homology and genetic evolution of pI215L gene of different ASFV strains, and to predict the physicochemical properties, secondary structure, linear epitope, and three-dimensional spatial location of pI215L protein. [Result] The pI215L gene sequences had high homology among different ASFV strains. The pI215L protein was unstable and hydrophilic. Its secondary structure mainly contained four forms, including α-helix, extend strand, β-turn, and random coil, and had a domain of E2 Ubiqutin-conjugating enzyme. A total of 16 peptide fragments were potential linear epitopes. SWISS-MODEL was used to complete homology modeling of the tertiary structure of pI215L protein, and its homology with 6NYO.1 （ubiquitin-conjugating enzyme E2 R2 and ubiquitin） in the PDB database was 46.06%. The PyMOL software was used to predict the conformational epitopes of pI215L protein to accurately locate the distribution of the predicted three-dimensional spatial position of the epitopes in the model. [Conclusion] Our results provided references for unravelling the structure and function of pI215L protein, as well as developing vaccines and drugs for prevention and control of ASFV.

Key words: African swine fever virus, bioinformatics, pI215L protein, structure and function