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Endotoxin-free purification for the isolation of Bovine Viral Diarrhoea Virus E2 protein from insoluble inclusion body aggregates

Cavallaro, A. S., Mahony, D., Commins, M., Mahony, T. J. and Mitter, N. (2011) Endotoxin-free purification for the isolation of Bovine Viral Diarrhoea Virus E2 protein from insoluble inclusion body aggregates. Microbial Cell Factories, 10 (1). p. 57. ISSN 1475-2859

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Article Link(s): http://doi.org/10.1186/1475-2859-10-57

Publisher URL: https://doi.org/10.1186/1475-2859-10-57

Abstract

Protein expression in Escherichia coli may result in the recombinant protein being expressed as insoluble inclusion bodies. In addition, proteins purified from E. coli contain endotoxins which need to be removed for in vivo applications. The structural protein, E2, from Bovine Viral Diarrhoea Virus (BVDV) is a major immunogenic determinant, and is an ideal candidate as a subunit vaccine. The E2 protein contains 17 cysteine residues creating difficulties in E. coli expression. In this report we outline a procedure for successfully producing soluble and endotoxin-free BVDV E2 protein from inclusion bodies (IB).

Item Type:Article
Keywords:Inclusion Body, Bovine Viral Diarrhoea Virus, Disulphide Bond, Subunit Vaccine, Japanese Encephalitis Virus
Subjects:Veterinary medicine > Veterinary virology
Veterinary medicine > Communicable diseases of animals (General)
Deposited On:26 Mar 2019 00:55
Last Modified:26 Mar 2019 00:55

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