scholarly journals Antigenic analysis of Japanese encephalitis virus by using monoclonal antibodies.

1984 ◽  
Vol 44 (1) ◽  
pp. 117-123 ◽  
Author(s):  
Y Kobayashi ◽  
H Hasegawa ◽  
T Oyama ◽  
T Tamai ◽  
T Kusaba
1983 ◽  
Vol 57 (6) ◽  
pp. 519-530
Author(s):  
Yuzuru KOBAYASHI ◽  
Hitoshi HASEGAWA ◽  
Takashi OYAMA ◽  
Tomonori TAMAI ◽  
Tomoo SHIROGUCHI ◽  
...  

1994 ◽  
Vol 2 (3) ◽  
pp. 191-199 ◽  
Author(s):  
Anita Desai ◽  
A. Chandramuki ◽  
M. Gourie-Devi ◽  
V. Ravi

2013 ◽  
Vol 32 (6) ◽  
pp. 382-385 ◽  
Author(s):  
Xindi Ruan ◽  
Shaomei Huang ◽  
Lin Shao ◽  
Jing Ye ◽  
Zheng Chen ◽  
...  

2012 ◽  
Vol 3 (2) ◽  
pp. 17
Author(s):  
Ashok Kumar Gupta ◽  
Attiyaril Abraham Koshy ◽  
Vaibhavi Jawahar Lad

A combination of at least three hemagglutination- inhibition-positive (HAI) and virus-specific (Hs) monoclonal antibodies (MAbs) to glycoprotein E (gpE) of Japanese encephalitis virus (JEV) fully protected (100%) mice against JEV strain 733913 infections (group 1). However, these representative epitopes are reported to have been lost on JEV group II strains. In the present study, therefore, the protective effect of various combinations of anti-gpE MAbs representing antigenic epitopes other than Hs was studied on mice infections with JEV group II strains: JEV strains 641686 and 691004. MAbs used in the protective experiments were characterized as HAI-negative virus-specific (NHs) and HAI-positive flavivirus cross-reactive (Hx). Additionally, one of the Hs MAbs (MAb Hs-3) was included in the experiments. Mice were first administered single MAbs or their combinations intraperitoneally and 24 h later, infected with the virus intracerebrally. Protection rates of 70-75% were obtained with a combination of four MAbs: MAbs NHs-1, Hx-1, Hx-3 and Hs-3. However, protection rates of only 20-40% were obtained with three MAbs but none was observed with single or two MAbs. There was, however, a substantial increase in mice survival. The protective effect of several combinations of anti-gpE MAbs representing different antigenic epitopes might be due to the enhancement of binding within the same group and also between different MAb groups. The present results indicate that NHs and Hx epitopes should be incorporated with three Hs epitopes in a JEV vaccine that would have an added advantage, particularly in the flaviviral endemic areas with JEV strain variations.


2008 ◽  
Vol 82 (14) ◽  
pp. 7009-7021 ◽  
Author(s):  
Ana P. Goncalvez ◽  
Cheng-Hsin Chien ◽  
Kamolchanok Tubthong ◽  
Inna Gorshkova ◽  
Carrie Roll ◽  
...  

ABSTRACT Japanese encephalitis virus (JEV)-specific Fab antibodies were recovered by repertoire cloning from chimpanzees initially immunized with inactivated JE-VAX and then boosted with attenuated JEV SA14-14-2. From a panel of 11 Fabs recovered by different panning strategies, three highly potent neutralizing antibodies, termed Fabs A3, B2, and E3, which recognized spatially separated regions on the virion, were identified. These antibodies reacted with epitopes in different domains: the major determinant for Fab A3 was Lys179 (domain I), that for Fab B2 was Ile126 (domain II), and that for Fab E3 was Gly302 (domain III) in the envelope protein, suggesting that these antibodies neutralize the virus by different mechanisms. Potent neutralizing antibodies reacted with a low number of binding sites available on the virion. These three Fabs and derived humanized monoclonal antibodies (MAbs) exhibited high neutralizing activities against a broad spectrum of JEV genotype strains. Demonstration of antibody-mediated protection of JEV infection in vivo is provided using the mouse encephalitis model. MAb B2 was most potent, with a 50% protective dose (ED50) of 0.84 μg, followed by MAb A3 (ED50 of 5.8 μg) and then MAb E3 (ED50 of 24.7 μg) for a 4-week-old mouse. Administration of 200 μg/mouse of MAb B2 1 day after otherwise lethal JEV infection protected 50% of mice and significantly prolonged the average survival time compared to that of mice in the unprotected group, suggesting a therapeutic potential for use of MAb B2 in humans.


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