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Soluble prokaryotic expression of varicella-zoster virus glycoprotein E without N-terminal signal peptide and its immunogenicity evaluation |
WEI Mingtong1, XIA Bingbing2, HE Zhiyuan2, ZHOU Wei2, LIU Xingdong3, ZHAO Jun2,4, CHEN Jingxian4, WANG Mingli2,4 |
1. The First Clinical Medical College of Anhui Medical University, Hefei 230032, Anhui Province, China; 2. Wuhu Interfell Research Institute, Wuhu 241000, Anhui Province, China; 3. Second Clinical Medical College of Anhui Medical University, Hefei 230032, Anhui Province, China; 4. Institute of Clinical Virology, Anhui Medical University, Hefei 230000, Anhui Province, China |
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Abstract Varicella zoster virus (VZV) glycoprotein E (gE) is the main candidate protein for VZV subunit vaccine. Unfortunately, the expression of gE in prokaryotic expression was mainly found in the inclusion body. In this study, a deletion of N-terminal 30 amino acids of gE was constructed on pET32a, expressed in BL21 (DE3). The soluble gE was purified and used to make polyclonal antibodies in BALB/c mice. The titer and specificity of polyclonal antibodies were determined by enzyme linked immunosorbent assay (ELISA) and indirect immunofluorescence. The results showed that the soluble recombinant gE produced by BL21/pET32a-VZV gE system is a practical way for vaccine development.
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Received: 02 January 2020
Published: 25 December 2020
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Corresponding Authors:
WANG Mingli
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