Structural Basis of a Flavivirus Recognized by Its Neutralizing Antibody.

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Title: Structural Basis of a Flavivirus Recognized by Its Neutralizing Antibody.
Authors: Kuen-Phon Wu, Maria Silvia1, Chih-Wei Wu, Maria Silvia1, Ya-Ping Tsao1, Ting-Wei Kuo, Maria Silvia1, Yuan-Chao Lou1, Cheng-Wen Lin1, Suh-Chin Wu1, Jya-Wei Cheng1 jwcheng@life.nthu.edu.tw
Source: Journal of Biological Chemistry. 11/14/2003, Vol. 278 Issue 46, p46007-46013. 7p. 3 Diagrams, 1 Chart, 1 Graph.
Subject Terms: *FLAVIVIRUSES, *PROTEINS, *ANTIGENS
Abstract: The flavivirus envelope protein is the dominant antigen in eliciting neutralizing antibodies and plays an important role in inducing immunologic responses in the infected host. We have determined the solution structure of the major antigenic domain (domain III) of the Japanese encephalitis virus (JEV) envelope protein. The JEV domain III forms a β-barrel type structure composed of six antiparallel β-strands resembling the immunoglobulin constant domain. We have also identified epitopes of the JEV domain III to its neutralizing antibody by chemical shift perturbation measurements. Site-directed mutagenesis experiments are performed to confirm the NMR results. Our study provides a structural basis for understanding the mechanism of immunologic protection and for rational design of vaccines effective against flaviviruses. [ABSTRACT FROM AUTHOR]
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  Data: Structural Basis of a Flavivirus Recognized by Its Neutralizing Antibody.
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  Data: <searchLink fieldCode="AR" term="%22Kuen-Phon+Wu%2C+Maria+Silvia%22">Kuen-Phon Wu, Maria Silvia</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Chih-Wei+Wu%2C+Maria+Silvia%22">Chih-Wei Wu, Maria Silvia</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Ya-Ping+Tsao%22">Ya-Ping Tsao</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Ting-Wei+Kuo%2C+Maria+Silvia%22">Ting-Wei Kuo, Maria Silvia</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Yuan-Chao+Lou%22">Yuan-Chao Lou</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Cheng-Wen+Lin%22">Cheng-Wen Lin</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Suh-Chin+Wu%22">Suh-Chin Wu</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Jya-Wei+Cheng%22">Jya-Wei Cheng</searchLink><relatesTo>1</relatesTo><i> jwcheng@life.nthu.edu.tw</i>
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  Data: <searchLink fieldCode="JN" term="%22Journal+of+Biological+Chemistry%22">Journal of Biological Chemistry</searchLink>. 11/14/2003, Vol. 278 Issue 46, p46007-46013. 7p. 3 Diagrams, 1 Chart, 1 Graph.
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  Data: *<searchLink fieldCode="DE" term="%22FLAVIVIRUSES%22">FLAVIVIRUSES</searchLink><br />*<searchLink fieldCode="DE" term="%22PROTEINS%22">PROTEINS</searchLink><br />*<searchLink fieldCode="DE" term="%22ANTIGENS%22">ANTIGENS</searchLink>
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  Label: Abstract
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  Data: The flavivirus envelope protein is the dominant antigen in eliciting neutralizing antibodies and plays an important role in inducing immunologic responses in the infected host. We have determined the solution structure of the major antigenic domain (domain III) of the Japanese encephalitis virus (JEV) envelope protein. The JEV domain III forms a β-barrel type structure composed of six antiparallel β-strands resembling the immunoglobulin constant domain. We have also identified epitopes of the JEV domain III to its neutralizing antibody by chemical shift perturbation measurements. Site-directed mutagenesis experiments are performed to confirm the NMR results. Our study provides a structural basis for understanding the mechanism of immunologic protection and for rational design of vaccines effective against flaviviruses. [ABSTRACT FROM AUTHOR]
– Name: AbstractSuppliedCopyright
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  Data: <i>Copyright of Journal of Biological Chemistry is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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        Value: 10.1074/jbc.M307776200
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        Text: English
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              Text: 11/14/2003
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