Production and purification of VP2 protein of porcine parvovirus expressed in an insect-baculovirus cell system

<p>Abstract</p> <p>The porcine parvovirus (PPV) VP2 protein was expressed in an insect-baculovirus cell system and was purified using Ni-NTA affinity column chromatography. The recombinant 6-His-tagged VP2 protein with molecular mass (Mr) of about 64 kDa was detected by anti-his an...

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Main Authors: Cui Shangjin, Yao Guizhe, Zhou Hongchao
Format: Article
Language:English
Published: BMC 2010-12-01
Series:Virology Journal
Online Access:http://www.virologyj.com/content/7/1/366
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author Cui Shangjin
Yao Guizhe
Zhou Hongchao
author_facet Cui Shangjin
Yao Guizhe
Zhou Hongchao
author_sort Cui Shangjin
collection DOAJ
description <p>Abstract</p> <p>The porcine parvovirus (PPV) VP2 protein was expressed in an insect-baculovirus cell system and was purified using Ni-NTA affinity column chromatography. The recombinant 6-His-tagged VP2 protein with molecular mass (Mr) of about 64 kDa was detected by anti-his antibody and anti-PPV serum. Electron microscopy showed that the purified VP2 protein assembled into spherical particles with diameters ranging from 20 to 22 nm. The expressed VP2 was antigenically similar to the native capsid protein according to HA and a Western blotting assay performed with polyclonal antibodies collected from an outbreak of PPV in one farm. This study provides a foundation for the application of VP2 protein in the clinical diagnosis of PPV or in the vaccination against PPV in the future.</p>
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spelling doaj.art-777bad0bb74b436a800af771511ab3d12022-12-22T01:51:58ZengBMCVirology Journal1743-422X2010-12-017136610.1186/1743-422X-7-366Production and purification of VP2 protein of porcine parvovirus expressed in an insect-baculovirus cell systemCui ShangjinYao GuizheZhou Hongchao<p>Abstract</p> <p>The porcine parvovirus (PPV) VP2 protein was expressed in an insect-baculovirus cell system and was purified using Ni-NTA affinity column chromatography. The recombinant 6-His-tagged VP2 protein with molecular mass (Mr) of about 64 kDa was detected by anti-his antibody and anti-PPV serum. Electron microscopy showed that the purified VP2 protein assembled into spherical particles with diameters ranging from 20 to 22 nm. The expressed VP2 was antigenically similar to the native capsid protein according to HA and a Western blotting assay performed with polyclonal antibodies collected from an outbreak of PPV in one farm. This study provides a foundation for the application of VP2 protein in the clinical diagnosis of PPV or in the vaccination against PPV in the future.</p>http://www.virologyj.com/content/7/1/366
spellingShingle Cui Shangjin
Yao Guizhe
Zhou Hongchao
Production and purification of VP2 protein of porcine parvovirus expressed in an insect-baculovirus cell system
Virology Journal
title Production and purification of VP2 protein of porcine parvovirus expressed in an insect-baculovirus cell system
title_full Production and purification of VP2 protein of porcine parvovirus expressed in an insect-baculovirus cell system
title_fullStr Production and purification of VP2 protein of porcine parvovirus expressed in an insect-baculovirus cell system
title_full_unstemmed Production and purification of VP2 protein of porcine parvovirus expressed in an insect-baculovirus cell system
title_short Production and purification of VP2 protein of porcine parvovirus expressed in an insect-baculovirus cell system
title_sort production and purification of vp2 protein of porcine parvovirus expressed in an insect baculovirus cell system
url http://www.virologyj.com/content/7/1/366
work_keys_str_mv AT cuishangjin productionandpurificationofvp2proteinofporcineparvovirusexpressedinaninsectbaculoviruscellsystem
AT yaoguizhe productionandpurificationofvp2proteinofporcineparvovirusexpressedinaninsectbaculoviruscellsystem
AT zhouhongchao productionandpurificationofvp2proteinofporcineparvovirusexpressedinaninsectbaculoviruscellsystem