A comparison of methods for purification and concentration of norovirus GII-4 capsid virus-like particles.
Noroviruses (NoVs) are one of the leading causes of acute gastroenteritis worldwide. NoV GII-4 VP1 protein was expressed in a recombinant baculovirus system using Sf9 insect cells. Several methods for purification and concentration of virus-like particles (VLPs) were evaluated. Electron microscopy (EM) and histo-blood group antigen (HBGA) binding assays showed that repeated sucrose gradient purification followed by ultrafiltration resulted in intact VLPs with excellent binding to H type 3 antigens. VLPs were stable for at least 12 months at 4°C, and up to 7 days at ambient temperature. These findings indicate that this method yielded stable and high-quality VLPs.
Huhti
L
L
Vaccine Research Center, University of Tampere Medical School, Finland. lllete@uta.fi
Blazevic
V
V
Nurminen
K
K
Koho
T
T
Hytönen
V P
VP
Vesikari
T
T
D000818:Animals; D001789:Blood Group Antigens / Q000737:chemistry; D036022:Capsid Proteins / Q000737:chemistry* / Q000378:metabolism; D002460:Cell Line; D006358:Hot Temperature; D007313:Insecta; D008854:Microscopy, Electron; D029322:Norovirus / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D055550:Protein Stability; D013395:Sucrose
D001789:Blood Group Antigens; D036022:Capsid Proteins; D013395:Sucrose