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- Title
Eliciting cross-neutralizing antibodies in mice challenged with a dengue virus envelope domain III expressed in.
- Authors
Yang, Jie; Zhang, Junlei; Chen, Wei; Hu, Zhen; Zhu, Junmin; Fang, Xin; Yuan, Wenchang; Li, Ming; Hu, Xiaomei; Tan, Yinling; Hu, Fuquan; Rao, Xiancai
- Abstract
Dengue viruses (DENVs) are mosquito-borne infectious pathogens that pose a serious global public health threat, and at present, no therapy or effective vaccines are available. Choosing suitable units as candidates is fundamental for the development of a dengue subunit vaccine. Domain III of the DENV-2 E protein (EDIII) was chosen in the present study and expressed in by N-terminal fusion to a bacterial leader (pelB), and C-terminal fusion with a 6×His tag based on the functions of DENV structure proteins, especially the neutralizing epitopes on the envelope E protein. After two-step purification using Ni-NTA affinity and cation-exchange chromatography, the His-tagged EDIII was purified up to 98% homogenicity. This recombinant EDIII was able to trigger high levels of neutralizing antibodies in both BALB/c and C57BL/6 mice. Both the recombinant EDIII and its murine antibodies protected Vero cells from DENV-2 infection. Interestingly, the recombinant EDIII provides at least partial cross-protection against DENV-1 infection. In addition, the EDIII antibodies were able to protect suckling mice from virus challenge in vivo. These data suggest that a candidate molecule based on the small EDIII protein, which has neutralizing epitopes conserved among all 4 DENV serotypes, has important implications.
- Subjects
IMMUNOGLOBULINS; DENGUE; DENGUE viruses; GENE expression; EPITOPES; RECOMBINANT proteins; ION exchange chromatography; LABORATORY mice; VACCINATION
- Publication
Canadian Journal of Microbiology, 2012, Vol 58, Issue 4, p369
- ISSN
0008-4166
- Publication type
Article
- DOI
10.1139/w11-137