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Surface display of domain III of Japanese encephalitis virus E protein on Salmonella typhimurium by using an ice nucleation protein

  • Published:
Virologica Sinica

Abstract

A bacterial cell surface display technique based on an ice nucleation protein has been employed for the development of live vaccine against viral infection. Due to its ubiquitous ability to invade host cells, Salmonella typhimurium might be a good candidate for displaying viral antigens. We demonstrated the surface display of domain III of Japanese encephalitis virus E protein and the enhanced green fluorescent protein on S. typhimurium BRD509 using the ice nucleation protein. The effects of the motif in the ice nucleation protein on the effective display of integral protein were also investigated. The results showed that display motifs in the protein can target integral foreign protein on the surface of S. typhimurium BRD509. Moreover, recombinant strains with surface displayed viral proteins retained their invasiveness, suggesting that the recombinant S. typhimurium can be used as live vaccine vector for eliciting complete immunogenicity. The data may yield better understanding of the mechanism by which ice nucleation protein displays foreign proteins in the Salmonella strain.

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Authors and Affiliations

  1. Key Laboratory of Agricultural and Environmental Microbiology, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan, 430071, China

    Jian-lin Dou, Jing-jing Fan & Zhi-ming Yuan

  2. Institute of Pathogenic biology, School of Basic Medical Sciences, Lanzhou University, Lanzhou, 730000, China

    Jian-lin Dou & Tao Jing

Authors
  1. Jian-lin Dou
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  2. Tao Jing
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  3. Jing-jing Fan
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  4. Zhi-ming Yuan
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Correspondence to Zhi-ming Yuan.

Additional information

Foundation item: The Knowledge Innovation Program Key Project (KSCX1-YW-R-07).

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Dou, Jl., Jing, T., Fan, Jj. et al. Surface display of domain III of Japanese encephalitis virus E protein on Salmonella typhimurium by using an ice nucleation protein. Virol. Sin. 26, 409–417 (2011). https://doi.org/10.1007/s12250-011-3216-7

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  • DOI: https://doi.org/10.1007/s12250-011-3216-7

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