Key result
Recombinant vaccinia virus system enables cleaved VP1 to self-assemble into VLPs in mammalian cells.
Why the study?
The mechanism of SaV VP1 production and self-assembly into virus-like particles in mammalian cells was not fully understood.
Demonstrates that sapovirus VP1 cleaved from ORF1 polyprotein can self-assemble into virus-like particles in mammalian cells.
May enable sapovirus VLP vaccines; extends expression systems but remains hypothesis-generating.
The SaV genome is a positive-sense, non-segmented single-strand RNA molecule of approximately 7.5 kb that is polyadenylated at its 3' terminus. The major capsid (VP1) of SaV is thought to be produced as the ORF1 polyprotein followed by cleavage, or translation from subgenomic RNA (3'-coterminal with the virus genome), or both. We have recently reported the formation of SaV VLP from subgenomic-like RNA in mammalian cells. In the present study, we demonstrated that the VP1 cleaved from a part of ORF1 polyprotein self-assembled into VLP in mammalian cells when a transient expression system using a recombinant vaccinia virus encoding T7 RNA polymerase was used.
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T et al. (2009) studied Sapovirus. Transient expression system using a recombinant vaccinia virus encoding T7 RNA polymerase was evaluated on Formation of SaV VLP from ORF1 polyprotein in mammalian cells. VP1 cleaved from a part of ORF1 polyprotein self-assembled into virus-like particles in mammalian cells using a transient expression system with recombinant vaccinia virus encoding T7 RNA polymerase.
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