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Immunogenicity and protective efficacy of the E. coli-expressed domain III of Japanese encephalitis virus envelope protein in mice

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Abstract

Domain III of Japanese encephalitis virus (JEV) envelope protein (E-DIII) was synthesized in E. coli as a fusion protein containing maltose-binding protein (MBP-E-DIII) or six contiguous histidine residues (His-E-DIII) at its N-terminus. MBP-E-DIII was found both in the soluble as well as the insoluble fraction of the bacterial lysate, while His-E-DIII was found exclusively in the inclusion bodies. These purified proteins were examined in mice for their immunogenicity in presence of an aluminium hydroxide based-adjuvant Alhydrogel and Freund’s adjuvant. While both proteins generated anti-JEV antibodies that neutralized JEV activity in vitro, His-E-DIII generated higher antibody titers than MBP-E-DIII. Mice immunized with His-E-DIII in presence of Alhydrogel generated antibody titers similar to those induced by the commercial vaccine and protected mice against lethal JEV challenge.

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Acknowledgments

This work was supported by the Department of Biotechnology, Government of India grant no. BT/PR2765/Med/14/329/2001 and the core grant of the National Institute of Immunology, New Delhi.

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Correspondence to Sudhanshu Vrati.

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Alka and Kaushik Bharati contributed equally to this work.

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Alka, Bharati, K., Malik, Y.P.S. et al. Immunogenicity and protective efficacy of the E. coli-expressed domain III of Japanese encephalitis virus envelope protein in mice. Med Microbiol Immunol 196, 227–231 (2007). https://doi.org/10.1007/s00430-007-0043-4

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  • DOI: https://doi.org/10.1007/s00430-007-0043-4

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