Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/36231
標題: 傳染性華氏囊炎病毒VP2次病毒粒子與固定化鎳離子吸附之點突變分析
Effect of Point-mutation on the Adsorption of VP2 Subvinal Particles of Infectious Bursal Disease Virus to the Immobilized Nickel ions.
作者: 卓子暄
Cho, Tz-Shiuan
關鍵字: IMAC;固定化金屬親和性層析法;immobilized nickel ions;infectious bursal disease virus;VP2 SVP;固定化鎳離子;傳染性華氏囊炎病毒;VP2次病毒
出版社: 生物科技學研究所
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摘要: 
固定化金屬離子親和性層析法(Immobilized-Metal ion Affinity Chromatography,IMAC),因具有單一步驟純化、再生容易優點,可做為大量純化蛋白質之方式。先前研究,以IMAC可直接純化未融合His-tag的VP2蛋白,發現位於P domain DE loop結構上的His 253胺基酸可與IMAC的鎳離子形成配位鍵結,做為病毒顆粒與IMAC管柱結合的重要位置。
本研究為尋找可取代His 253位置與固定化金屬離子結合的胺基酸位置,先利用軟體分析蛋白的暴露面積篩選,在His 253為丙胺酸的情形下,將其個別突變為組胺酸(Histidine),經篩選後可Gln221、Ser222、Ser251、Ser317、Gln320及Ala321六個位置。分別以大腸桿菌表現系統與昆蟲桿狀病毒表現系統表現各突變株重組蛋白,並進行不同酸鹼值的緩衝溶液及不同濃度之咪唑沖提,結果顯示VP2-P domain 的Loop結構上人工His能取代His 253與鎳離子結合,且透過多種實驗觀察證實經突變後蛋白並不影響其構形、密度等物理特性。

The advantage of Immobilized-Metal ion Affinity Chromatography (IMAC) - one- step purification, recycling is easy, etc.- are decisive when developing large-scale purification procedures for industrial applications. Previous results indicated that SVPs can be purified directly by IMAC and the His 253 on DE loop of P domain plays an important role binding Ni2+ ions. Besides His 253, outward superficial residues on P domain of SVPs provide higher chances for Ni2+ ions binding.

In this study, to search the residues this can be substituted for the binding of immobilized Ni2+ ions. First, the calculation of exposure areas of residues on the loop was performed by Surface Racer 5.0 software. Six resides - Gln221, Ser222, Ser251, Ser317, Gln320 and Ala321-have been chosen, than been substituted with histidine. Recombinant proteins was expressed in Escherichia coli and Bac-to-Bac baculovirus expression system, and then purified by IMAC. The binding strength of these variants with immobilized Ni2+ ion was measured by quantitating the unbound VP2 protein after a series of wash with various pH and immidazole concentrations. The results have shown some residues on the loop structure of P domains of SVPs substituted and complement the mutation of H253A to bind Ni2+ ion, and don't affect density and other physical characteristics.
URI: http://hdl.handle.net/11455/36231
其他識別: U0005-0202201116104200
Appears in Collections:生物科技學研究所

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