title: A comparison of methods for purification and concentration of norovirus GII-4 capsid virus-like particles.
abstract: 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.
authors: Vaccine Research Center, University of Tampere Medical School, Finland. lllete@uta.fi
authors: L
authors: L
authors: Huhti
authors: V
authors: V
authors: Blazevic
authors: K
authors: K
authors: Nurminen
authors: T
authors: T
authors: Koho
authors: V P
authors: VP
authors: Hytönen
authors: T
authors: T
authors: Vesikari
mesh_terms: 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
chemical_list: D001789:Blood Group Antigens; D036022:Capsid Proteins; D013395:Sucrose