Self-assembly of sapovirus recombinant virus-like particles from polyprotein in mammalian cells.
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.
Oka
Tomoichiro
T
Department of Virology II, National Institute of Infectious Diseases, Gakuen 4-7-1, Musashi-murayama, Tokyo 208-0011, Japan. oka-t@nih.go.jp
Yamamoto
Mami
M
Miyashita
Kana
K
Ogawa
Satoko
S
Katayama
Kazuhiko
K
Wakita
Takaji
T
Takeda
Naokazu
N
D000818:Animals; D019556:COS Cells; D036022:Capsid Proteins / Q000235:genetics / Q000378:metabolism*; D002522:Chlorocebus aethiops; D020815:Polyproteins / Q000235:genetics / Q000378:metabolism*; D029341:Sapovirus / Q000235:genetics / Q000502:physiology*; D014771:Virion / Q000235:genetics / Q000502:physiology*; D019065:Virus Assembly
D036022:Capsid Proteins; D020815:Polyproteins