Antigenic epitopes mapping and functional analysis of domain III of Japanese encephalitis virus envelope protein

文献类型： 外文期刊

第一作者： Yan Li-Ping

作者： Yan Li-Ping;Hua Rong-Hong;Tong Guang-Zhi;Yan Li-Ping;Qi Wen-Bao

作者机构：

关键词： Japanese encephalitis virus;envelope protein (E-protein);epitope

期刊名称：PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS （ 影响因子：0.351； 五年影响因子：0.272 ）

ISSN： 1000-3282

年卷期： 2008 年 35 卷 3 期

页码：

收录情况： SCI

摘要： Japanese encephalitis virus (JEV) (family Flaviviridae, genus Flavivirus) is an arbovirus of public health importance. The envelope glycoprotein of JEV is associated with viral attachment and fusion with host cell, determine the virus' s hemagglutination ability, cellular tropism, viral virulence, and induction of protective immune response. The domain III of envelope protein (E protein) is an important region in inducing neutralizing antibodies against JEV. In order to study the antigenic structure of domain III on E protein, domain III of the envelope protein was expressed by fusion with GST in a pGEX-6p-1 vector. Western blot demonstrated that expressed fusion protein could be recognized by anti-JEV sera. To map the antigenic epitope of this region, a set of 14 partially overlapping short peptides spanning the domain I were designed and expressed in fusing with GST. Then Western blot and ELISA reactivity of these short peptide fusion proteins to anti-JEV sera were surveyed, respectively. Four linear antigenic epitopes, E39 ((305)TEKFSFAKNPVDTGHG(320)), E45-1 ((355)VTVNPFVATSSA(366)), E48-1 ((377)PFGDSYIV(384)) and E49 ((385)VGRGDKQINHHWHCAG(400)) were identified. Immunization of mice with epitope fusion proteins revealed that all four proteins could elicit short peptide specific antibody. And in vitro neutralization test verified that E39 was linear neutralizing epitope. This result provides important basis for further structural and functional study of domain III of JEV envelope protein, and development of diagnostic techniques and vaccines.

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