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 (...

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Autores principales: Huhti, L., Blazevic, V., Nurminen, K., Koho, T., Hytönen, V. P., Vesikari, T.
Formato: Texto
Lenguaje:English
Publicado: Springer Vienna 2010
Materias:
Brief Report
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2970802/
https://www.ncbi.nlm.nih.gov/pubmed/20721592
http://dx.doi.org/10.1007/s00705-010-0768-z
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author Huhti, L.
Blazevic, V.
Nurminen, K.
Koho, T.
Hytönen, V. P.
Vesikari, T.
author_facet Huhti, L.
Blazevic, V.
Nurminen, K.
Koho, T.
Hytönen, V. P.
Vesikari, T.
author_sort Huhti, L.
collection PubMed
description 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.
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spelling pubmed-29708022010-11-29 A comparison of methods for purification and concentration of norovirus GII-4 capsid virus-like particles Huhti, L. Blazevic, V. Nurminen, K. Koho, T. Hytönen, V. P. Vesikari, T. Arch Virol Brief Report 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. Springer Vienna 2010-08-19 2010 /pmc/articles/PMC2970802/ /pubmed/20721592 http://dx.doi.org/10.1007/s00705-010-0768-z Text en © The Author(s) 2010 https://creativecommons.org/licenses/by-nc/4.0/ This article is distributed under the terms of the Creative Commons Attribution Noncommercial License which permits any noncommercial use, distribution, and reproduction in any medium, provided the original author(s) and source are credited.
spellingShingle Brief Report
Huhti, L.
Blazevic, V.
Nurminen, K.
Koho, T.
Hytönen, V. P.
Vesikari, T.
A comparison of methods for purification and concentration of norovirus GII-4 capsid virus-like particles
title A comparison of methods for purification and concentration of norovirus GII-4 capsid virus-like particles
title_full A comparison of methods for purification and concentration of norovirus GII-4 capsid virus-like particles
title_fullStr A comparison of methods for purification and concentration of norovirus GII-4 capsid virus-like particles
title_full_unstemmed A comparison of methods for purification and concentration of norovirus GII-4 capsid virus-like particles
title_short A comparison of methods for purification and concentration of norovirus GII-4 capsid virus-like particles
title_sort comparison of methods for purification and concentration of norovirus gii-4 capsid virus-like particles
topic Brief Report
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2970802/
https://www.ncbi.nlm.nih.gov/pubmed/20721592
http://dx.doi.org/10.1007/s00705-010-0768-z
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