4.7 Article

Self-assembly of virus-like particles of canine parvovirus capsid protein expressed from Escherichia coli and application as virus-like particle vaccine

期刊

APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
卷 98, 期 8, 页码 3529-3538

出版社

SPRINGER
DOI: 10.1007/s00253-013-5485-6

关键词

Canine parvovirus; Prokaryotic expression; Virus-like particles; Immunogenicity; Capsid protein

资金

  1. Fundamental Research Funds for the Chinese Academy of Agricultural Sciences [2013ZL035]
  2. Gansu Provincial Sci. & Tech. Department [1102NKDA033, 1102NKDA034, 1104WCGA185]
  3. National Natural Science Foundation of China [31100688, 31101838]
  4. Scientific Research Foundation for the Returned Overseas Chinese Scholars, State Education Ministry

向作者/读者索取更多资源

Canine parvovirus disease is an acute infectious disease caused by canine parvovirus (CPV). Current commercial vaccines are mainly attenuated and inactivated; as such, problems concerning safety may occur. To resolve this problem, researchers developed virus-like particles (VLPs) as biological nanoparticles resembling natural virions and showing high bio-safety. This property allows the use of VLPs for vaccine development and mechanism studies of viral infections. Tissue-specific drug delivery also employs VLPs as biological nanomaterials. Therefore, VLPs derived from CPV have a great potential in medicine and diagnostics. In this study, small ubiquitin-like modifier (SUMO) fusion motif was utilized to express a whole, naturalVP2 protein of CPV in Escherichia coli. After the cleavage of the fusion motif, the CPV VP2 protein has self-assembled into VLPs. The VLPs had a size and shape that resembled the authentic virus capsid. However, the self-assembly efficiency of VLPs can be affected by different pH levels and ionic strengths. The mice vaccinated subcutaneously with CPV VLPs and CPV-specific immune responses were compared with those immunized with the natural virus. This result showed that VLPs can effectively induce anti-CPV specific antibody and lymphocyte proliferation as a whole virus. This result further suggested that the antigen epitope of CPV was correctly present on VLPs, thereby showing the potential application of a VLP-based CPV vaccine.

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