Purification of norovirus-like particles (VLPs) by ion exchange chromatography

Tiia Koho; Tuomas Mäntylä; Pasi Laurinmäki; Leena Huhti; Sarah J. Butcher; Timo Vesikari; Markku S. Kulomaa; Vesa P. Hytönen

doi:10.1016/j.jviromet.2012.01.003

Purification of norovirus-like particles (VLPs) by ion exchange chromatography

Tiia Koho, Tuomas Mäntylä, Pasi Laurinmäki, Leena Huhti, Sarah J. Butcher, Timo Vesikari, Markku S. Kulomaa, Vesa P. Hytönen

Department of Clinical Chemistry

Research output: Contribution to journal › Article › Scientific › peer-review

35 Citations (Scopus)

Abstract

Recombinant expression of the norovirus capsid protein VP1 leads to self-assembly of non-infectious virus-like particles (VLPs), which are recognized as promising vaccine candidates against norovirus infections. To overcome the scalability issues connected to the ultracentrifugation-based purification strategies used in previous studies, an anion exchange-based purification method for norovirus VLPs was developed in this study. The method consists of precipitation by polyethylene glycol (PEG) and a single anion exchange chromatography step for purifying baculovirus-expressed GII.4 norovirus VLPs, which can be performed within one day. High product purity was obtained using chromatography. The purified material also contained fully assembled monodispersed VLPs, which were recognized by human sera containing polyclonal antibodies against norovirus GII.4.

Original language	English
Pages (from-to)	6-11
Number of pages	6
Journal	JOURNAL OF VIROLOGICAL METHODS
Volume	181
Issue number	1
DOIs	https://doi.org/10.1016/j.jviromet.2012.01.003
Publication status	Published - 2012
Publication type	A1 Journal article-refereed

Keywords

Ion exchange chromatography
Norovirus
Vaccines
Virus-like particle

Publication forum classification

Publication forum level 1

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/j.jviromet.2012.01.003

Cite this

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title = "Purification of norovirus-like particles (VLPs) by ion exchange chromatography",

abstract = "Recombinant expression of the norovirus capsid protein VP1 leads to self-assembly of non-infectious virus-like particles (VLPs), which are recognized as promising vaccine candidates against norovirus infections. To overcome the scalability issues connected to the ultracentrifugation-based purification strategies used in previous studies, an anion exchange-based purification method for norovirus VLPs was developed in this study. The method consists of precipitation by polyethylene glycol (PEG) and a single anion exchange chromatography step for purifying baculovirus-expressed GII.4 norovirus VLPs, which can be performed within one day. High product purity was obtained using chromatography. The purified material also contained fully assembled monodispersed VLPs, which were recognized by human sera containing polyclonal antibodies against norovirus GII.4.",

keywords = "Ion exchange chromatography, Norovirus, Vaccines, Virus-like particle, Ion exchange chromatography, Norovirus, Vaccines, Virus-like particle",

author = "Tiia Koho and Tuomas M{\"a}ntyl{\"a} and Pasi Laurinm{\"a}ki and Leena Huhti and Butcher, {Sarah J.} and Timo Vesikari and Kulomaa, {Markku S.} and Hyt{\"o}nen, {Vesa P.}",

year = "2012",

doi = "10.1016/j.jviromet.2012.01.003",

language = "English",

volume = "181",

pages = "6--11",

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TY - JOUR

T1 - Purification of norovirus-like particles (VLPs) by ion exchange chromatography

AU - Koho, Tiia

AU - Mäntylä, Tuomas

AU - Laurinmäki, Pasi

AU - Huhti, Leena

AU - Butcher, Sarah J.

AU - Vesikari, Timo

AU - Kulomaa, Markku S.

AU - Hytönen, Vesa P.

PY - 2012

Y1 - 2012

N2 - Recombinant expression of the norovirus capsid protein VP1 leads to self-assembly of non-infectious virus-like particles (VLPs), which are recognized as promising vaccine candidates against norovirus infections. To overcome the scalability issues connected to the ultracentrifugation-based purification strategies used in previous studies, an anion exchange-based purification method for norovirus VLPs was developed in this study. The method consists of precipitation by polyethylene glycol (PEG) and a single anion exchange chromatography step for purifying baculovirus-expressed GII.4 norovirus VLPs, which can be performed within one day. High product purity was obtained using chromatography. The purified material also contained fully assembled monodispersed VLPs, which were recognized by human sera containing polyclonal antibodies against norovirus GII.4.

AB - Recombinant expression of the norovirus capsid protein VP1 leads to self-assembly of non-infectious virus-like particles (VLPs), which are recognized as promising vaccine candidates against norovirus infections. To overcome the scalability issues connected to the ultracentrifugation-based purification strategies used in previous studies, an anion exchange-based purification method for norovirus VLPs was developed in this study. The method consists of precipitation by polyethylene glycol (PEG) and a single anion exchange chromatography step for purifying baculovirus-expressed GII.4 norovirus VLPs, which can be performed within one day. High product purity was obtained using chromatography. The purified material also contained fully assembled monodispersed VLPs, which were recognized by human sera containing polyclonal antibodies against norovirus GII.4.

KW - Ion exchange chromatography

KW - Norovirus

KW - Vaccines

KW - Virus-like particle

KW - Ion exchange chromatography

KW - Norovirus

KW - Vaccines

KW - Virus-like particle

U2 - 10.1016/j.jviromet.2012.01.003

DO - 10.1016/j.jviromet.2012.01.003

M3 - Article

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JF - JOURNAL OF VIROLOGICAL METHODS

IS - 1

ER -

Purification of norovirus-like particles (VLPs) by ion exchange chromatography

Abstract

Keywords

Publication forum classification

UN SDGs

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