Poliovirus viral production and assembly
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Upon release into the cytoplasm, the viral RNA is translated by the host cell machinery into a single polyprotein. The 5’ end of poliovirus is long compared to the host cell’s mRNA, about 700 nucleotides, and highly structured. That region directs translation of the viral RNA, and is known as the internal ribosome entry site.
The polyprotein is processed co-translationally by viral proteases into the viral proteins. It then undergoes myristoylation, the addition of a myristoyl group, and the N terminus of the protein chain. Viral 2A protease then cleaves the polyprotein to release a precursor protein myristoyl-P1 from the N terminus. The P1 protein contains all capsid protein sequences.
It is subsequently cleaved by viral 3CD protease into capsid proteins VP1 and VP3 and the immature capsid protein myristoyl-VP0.
After translation, viral genome replication occurs, producing positive sense copies of the original genome. That process involves production of multiple negative sense copies, which are then used as templates for the positive sense strands. The protein VPg serves as a primer for both positive and negative sense strands.
At this point the proteins form a pentameric assembly intermediate, which then becomes an empty capsid with 60 copies each of VP0, VP3, and VP1. During that process, five copies each of VP1, VP3, VP1 and VP4 become the interior surface of the capsid. Each capsid is assembled with a copy of the genome inside.
Assembled polioviruses are released from the host cell through lysis of the cell, about 4 to 6 hours after infection. Each cell can release as many as 10,000 copies of the virus.
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