根據過去文獻報導，細胞表面的醣胺素(GAGs)對於導引日本腦炎病毒（JEV）之感染上扮演重要的角色，但是其過程所牽扯的範圍上及鍵結結構功能的部分相對地仍未清楚。因此我們建立一套特異性分子附著力的系統介於日本腦炎病毒套膜蛋白和已定義其結構性之醣胺素，藉以研究醣胺素在日本腦炎病毒感染中扮演的角色。
日本腦炎目前為法定傳染病之一，依過去的研究顯示，其套膜蛋白為進入細胞的關鍵。我們利用分子生物技術分別製作了重組日本腦炎套膜蛋白第三區，包括：以含有可溶性融合蛋白Thioredoxin的pEt32a載體為基礎的pEt32a、E261-420、E277-420、 E292-420、E292-402及以未含Thioredoxin的pRsetA載體為基礎的E261-420等蛋白胜肽片段，再利用表面電漿共振技術（SPR）偵測其分子間動力學的參數。實驗結果顯示，在含有E261-291的胜肽有較強的結合能力，其為前端預測醣胺素鍵結區，而後端E403-420則較弱。雖然單純pEt32a也對肝素有相當的結合能力，但對照於以pRsetA載體為基礎的蛋白胜肽片段，可清楚地證明JEV E對於肝素有較強結合的能力。
本研究探討醣胺素和日本腦炎病毒套膜蛋白第三區之結合專一性，並由三維結構觀點瞭解病毒進入細胞之過程，並證明這對於病毒感染提供一有效可行過程的觀察方向，可作為未來發展新的抗病毒藥物之基礎。

In our recent studies, cell surface glycosaminoglycans (GAGs) play an important role in inducing Japanese encephalitis virus (JEV) infection, the extent to which GAGs are initially involved in JEV infection and the function of binding structure are relatively unknown.Understanding the role that GAGs play in JEV infection requires establishing a specific recognition between the JEV envelope protein and structurally defined GAGs.
In our recent studies, JEV is still one of the statutory contagions, which envelope protein is the entrance key of cell membrane, especially the domain III is the most interested. Using molecular biotech, we created a kind of reconstructed JEV E domain III protein based on vector pEt32a with thioredoxin which contains pEt32a、E261-420、E277-420、E292-420、E292-402 and vector pRsetA without thioredoxin which contains E261-420. We detect the kinetic constants between molecules immediately by using SPR which is biomolecular binding technology. The present studies show about the recombinant GAG-binding proteins of JEV, the binding ability is stronger in anterior predictive GAGs binding peptide E261-291 than inferior E403-420. Otherwise, pure pEt32a (thioredoxin control) also got binding ability with heparin, but we took a protein section of vector pRsetA(without thioredoxin), obtained a clear binding demonstration between JEV E261-420 and heparin.
This projection is discussing between GAGs and JEV envelope protein domain III in the binding specificity, and virus entry process in 3D structure view, and proving an effective and available research direction of virus infection. Thus it is meaningful contribution in further researching of new antivirus medicine and biology.

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