Additional file 1 of Stability and integrity of self-assembled bovine parvovirus virus‑like particles (BPV‑VLPs) of VP2 and combination of VP1VP2 assisted by baculovirus-insect cell expression: a potential logistical platform for vaccine deployment

Additional file 1: Fig. S1. Virus particles (natural virus) and Virus-like particles (VLPs) have comparable structures, are easily recognized by the immune system, and deliver viral antigens in a manner similar to the legitimate conformation, eliciting a robust immune response. Fig. S2. The BPV genome, depicted above in schematic form, is approximately 5.5 kilobases in size and is framed by a pair of nonidentical palindromic terminal hairpins. ORF1, ORF2, and ORF3 are the three largest open reading frames. In the genome (740–5307 kb) , ORF1 (740-2920 bp; left ORF) encodes a nonstructural protein (involved in DNA replication). ORF2 (middle ORF) encodes a nuclear phosphoprotein (2661-3302 bp) involved in viral RNA processing during gene expression. Two viral capsid proteins, VP1 and VP2, are encoded by ORF3 (right ORF) (3286-5307 bp) due to alternative splicing events. Together, VP1 and VP2 account for the bulk of the genome, approximately 2022 base pairs (bp), and VP2 is also responsible for the vast majority of capsid formation. There are flip inversion areas and hairpin loop stem loops at both the N and C termini (Agbandje-McKenna, 1998; Sukhu et al., 2013).