Unknown

Dataset Information

0

A functional epitope determinant on domain III of the Japanese encephalitis virus envelope protein interacted with neutralizing-antibody combining sites.


ABSTRACT: The envelope (E) protein of Japanese encephalitis virus (JEV) is associated with viral binding to cellular receptors, membrane fusion, and the induction of protective neutralizing-antibody responses in hosts. Most previous studies have not provided detailed molecular information about the spatial configuration of the functional epitopes on domain III of the E protein. Here site-directed mutagenesis was performed to demonstrate that the functional epitope determinants at Ser331 and Asp332 on domain III of the JEV E protein interacted with neutralizing monoclonal antibody (MAb) E3.3. Bacterial expression of the recombinant Fab E3.3 confirmed the molecular interactions of Arg94 in complementary determining region H3 with Ser331 and Asp332 on domain III. This study elucidates the detailed molecular structures of the neutralizing epitope determinants on JEV domain III, which can provide useful information for designing new vaccines.

SUBMITTER: Lin CW 

PROVIDER: S-EPMC141121 | biostudies-literature | 2003 Feb

REPOSITORIES: biostudies-literature

altmetric image

Publications

A functional epitope determinant on domain III of the Japanese encephalitis virus envelope protein interacted with neutralizing-antibody combining sites.

Lin Cheng-Wen CW   Wu Suh-Chin SC  

Journal of virology 20030201 4


The envelope (E) protein of Japanese encephalitis virus (JEV) is associated with viral binding to cellular receptors, membrane fusion, and the induction of protective neutralizing-antibody responses in hosts. Most previous studies have not provided detailed molecular information about the spatial configuration of the functional epitopes on domain III of the E protein. Here site-directed mutagenesis was performed to demonstrate that the functional epitope determinants at Ser331 and Asp332 on doma  ...[more]

Similar Datasets

| S-EPMC4619746 | biostudies-literature
| S-EPMC5510626 | biostudies-literature
| S-EPMC8618745 | biostudies-literature
| S-EPMC4592203 | biostudies-literature
| S-EPMC3302414 | biostudies-literature
| S-EPMC7243247 | biostudies-literature
| S-EPMC11320570 | biostudies-literature
| S-EPMC7111294 | biostudies-literature
| S-EPMC7354527 | biostudies-literature
| PRJNA855038 | ENA