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

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 m...

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Autores principales: Zhou, Hongchao, Yao, Guizhe, Cui, Shangjin
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2010
Materias:
Short Report
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3022681/
https://www.ncbi.nlm.nih.gov/pubmed/21143963
http://dx.doi.org/10.1186/1743-422X-7-366
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author Zhou, Hongchao
Yao, Guizhe
Cui, Shangjin
author_facet Zhou, Hongchao
Yao, Guizhe
Cui, Shangjin
author_sort Zhou, Hongchao
collection PubMed
description 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.
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spelling pubmed-30226812011-01-19 Production and purification of VP2 protein of porcine parvovirus expressed in an insect-baculovirus cell system Zhou, Hongchao Yao, Guizhe Cui, Shangjin Virol J Short Report 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. BioMed Central 2010-12-10 /pmc/articles/PMC3022681/ /pubmed/21143963 http://dx.doi.org/10.1186/1743-422X-7-366 Text en Copyright ©2010 Zhou et al; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (<url>http://creativecommons.org/licenses/by/2.0</url>), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Short Report
Zhou, Hongchao
Yao, Guizhe
Cui, Shangjin
Production and purification of VP2 protein of porcine parvovirus expressed in an insect-baculovirus cell system
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
topic Short Report
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3022681/
https://www.ncbi.nlm.nih.gov/pubmed/21143963
http://dx.doi.org/10.1186/1743-422X-7-366
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AT yaoguizhe productionandpurificationofvp2proteinofporcineparvovirusexpressedinaninsectbaculoviruscellsystem
AT cuishangjin productionandpurificationofvp2proteinofporcineparvovirusexpressedinaninsectbaculoviruscellsystem

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