Sapovirus-like particles derived from polyprotein.
We expressed full-length sapovirus genome constructs in insect cells and analyzed their products. The capsid protein was cleaved from the ORF1 polyprotein from a native-like genome construct and two full-length genome constructs with mutations in an active polymerase motif, whereas the capsid protein was not cleaved from a full-length genome construct with a mutation in an active protease motif. Our results showed that the sapovirus protease-polymerase precursor protein cleaved the capsid protein from the polyprotein at the putative conserved capsid start. Importantly, the cleaved capsid protein formed empty virus-like particles that were morphologically and antigenically similar to native sapovirus.
Hansman
Grant S
GS
Department of Virology II, National Institute of Infectious Diseases, Japan. g@nih.go.jp
Oka
Tomoichiro
T
Takeda
Naokazu
N
D000818:Animals; D017250:Caliciviridae Infections / Q000821:virology*; D036022:Capsid Proteins / Q000235:genetics / Q000378:metabolism; D002460:Cell Line; D016679:Genome, Viral; D006801:Humans; D007223:Infant; D008297:Male; D016366:Open Reading Frames; D010447:Peptide Hydrolases / Q000378:metabolism; D020815:Polyproteins / Q000235:genetics / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D029341:Sapovirus / Q000235:genetics / Q000302:isolation & purification / Q000502:physiology*; D014764:Viral Proteins / Q000235:genetics / Q000378:metabolism*; D019065:Virus Assembly
D036022:Capsid Proteins; D020815:Polyproteins; D014764:Viral Proteins; D010447:Peptide Hydrolases