scholarly journals Intramuscular Immunization with a Plasmid DNA Vaccine Encoding prM-E Protein from Japanese Encephalitis Virus: Enhanced Immunogenicity by Co-Administration of GM-CSF Gene and Genetic Fusions of prM-E Protein and GM-CSF

Intervirology ◽  
2009 ◽  
Vol 52 (3) ◽  
pp. 152-163 ◽  
Author(s):  
Yong-zhen Zhai ◽  
Xi-mei Li ◽  
Yan Zhou ◽  
Li Ma ◽  
Guo-he Feng
Intervirology ◽  
2006 ◽  
Vol 50 (2) ◽  
pp. 93-98 ◽  
Author(s):  
Guo-he Feng ◽  
Ning Liu ◽  
Yan Zhou ◽  
Yong-zhen Zhai ◽  
Xi-mei Li ◽  
...  

2006 ◽  
Vol 8 (11) ◽  
pp. 2578-2586 ◽  
Author(s):  
Chang Jer Wu ◽  
Tsung Lin Li ◽  
Hui Wen Huang ◽  
Mi Hua Tao ◽  
Yi Lin Chan

2012 ◽  
Vol 93 (6) ◽  
pp. 1185-1192 ◽  
Author(s):  
Shyan-Song Chiou ◽  
Yi-Chin Fan ◽  
Wayne D. Crill ◽  
Ruey-Yi Chang ◽  
Gwong-Jen J. Chang

Group and serocomplex cross-reactive epitopes have been identified in the envelope (E) protein of several flaviviruses and have proven critical in vaccine and diagnostic antigen development. Here, we performed site-directed mutagenesis across the E gene of a recombinant expression plasmid that encodes the Japanese encephalitis virus (JEV) premembrane (prM) and E proteins and produces JEV virus-like particles (VLPs). Mutations were introduced at I135 and E138 in domain I; W101, G104, G106 and L107 in domain II; and T305, E306, K312, A315, S329, S331, G332 and D389 in domain III. None of the mutant JEV VLPs demonstrated reduced activity to the five JEV type-specific mAbs tested. Substitutions at W101, especially W101G, reduced reactivity dramatically with all of the flavivirus group cross-reactive mAbs. The group and JEV serocomplex cross-reactive mAbs examined recognized five and six different overlapping epitopes, respectively. Among five group cross-reactive epitopes, amino acids located in domains I, II and III were involved in one, five and three epitopes, respectively. Recognition by six JEV serocomplex cross-reactive mAbs was reduced by amino acid substitutions in domains II and III. These results suggest that amino acid residues located in the fusion loop of E domain II are the most critical for recognition by group cross-reactive mAbs, followed by residues of domains III and I. The amino acid residues of both domains II and III of the E protein were shown to be important in the binding of JEV serocomplex cross-reactive mAbs.


2020 ◽  
Author(s):  
Ran Wang ◽  
Xiaozheng Yu ◽  
Yan Wang ◽  
Xiaoyan Zheng

Abstract Background The incidence of Japanese encephalitis (JE) has been dramatically reduced in China after the coverage of the vaccine. It is believed that the live-attenuated Japanese encephalitis virus (JEV) vaccine SA14-14-2 has contributed a lot. Another vaccine that seems to have faded out of the public is an inactivated vaccine based on the JEV P3 strain, which is still considered to have certain modifiability, such as being transformed into a DNA vaccine to improve its immunogenicity. Methods In this study, the protective efficacy induced by a Japanese encephalitis DNA vaccine candidate pV-JP3ME encoding pre-membrane (prM) and envelope (E) proteins of P3 strain in BALB/c mice. The prM/E genes of the JEV P3 strain were subcloned into vector pVAX1 (pV) to construct pV-JP3ME. Results The plasmid DNA was immunized BALB/c mice, high titers of IgG antibody and neutralizing antibody (nAb) against JEV were detected. The key cytokines in splenocytes upon stimulation with JEV antigens were secreted. Finally, complete protective efficacy was generated after challenge with the JEV P3 strain in mice. Conclusions The DNA vaccine pV-JP3ME based on JEV P3 strain in this study can induce specific humoral immune and cytokine responses in mice, and provide complete protection for mice against JEV.


2013 ◽  
Vol 94 (1) ◽  
pp. 90-96 ◽  
Author(s):  
Yukie Yamaguchi ◽  
Yoko Nukui ◽  
Akira Kotaki ◽  
Kyoko Sawabe ◽  
Masayuki Saijo ◽  
...  

Amino acid position 123 in the E protein of Japanese encephalitis virus (JEV) determines viral growth properties and pathogenicity. The majority of JEV strains have a serine residue at this position (E123S); however, JEV with an asparagine residue (E123N) has also been isolated. To compare the growth properties and pathogenicity of E123S and E123N JEV, we produced recombinant JEV with a serine-to-asparagine substitution at position 123 (rJEV-Mie41-ES123N) in the E123S-type strain Mie/41/2002 background. The growth rate of rJEV-Mie41-ES123N was similar to that of Mie/41/2002 in mammalian and mosquito cell lines. Mouse challenge experiments showed that there was only a slight difference in neuroinvasiveness between the parent strain (Mie/41/2002) and rJEV-Mie41-ES123N. Thus, our results indicate that the Ser-to-Asn substitution in the JEV E protein has weak impact on viral growth properties in vitro or on pathogenicity in vivo.


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