蛋白質(zhì)組學(xué)技術(shù)在流感病毒與宿主細胞相互作用研究中的應(yīng)用
發(fā)布時間:2018-05-05 16:43
本文選題:流感病毒 + 蛋白質(zhì)組學(xué)。 參考:《吉林大學(xué)》2017年碩士論文
【摘要】:流感病毒是流行性感冒(流感)的病原體。其中甲型流感病毒的抗原性易發(fā)生變異,已經(jīng)多次引起世界性大流行。對禽流感病毒的重視源于1918年到1919年之間在全球殺死5000萬到1億人的西班牙大流感。正是由于這種災(zāi)難性的事情一次次出現(xiàn),激發(fā)了廣大的國內(nèi)外專家學(xué)者對其進行研究的濃厚興趣,科研工作者們前赴后繼爭相研究流感病毒的奧秘。本學(xué)位論文充分利用了蛋白質(zhì)組學(xué)技術(shù),詳細研究了流感病毒與宿主細胞的相互作用,在流感病毒侵染Vero細胞的實驗中,找到15個新表達的差異蛋白,發(fā)現(xiàn)了其特異性表達的蛋白質(zhì)翻譯后修飾。在對三組樣品進行液相-質(zhì)譜聯(lián)用分析后發(fā)現(xiàn)了更多的差異,找到上調(diào)蛋白36個,下調(diào)蛋白19個。而在棕櫚;揎椀膶嶒炛,又對流感病毒的蛋白進行了分析鑒定,結(jié)果發(fā)現(xiàn)利用酰基-生物素置換反應(yīng)、親和層析和質(zhì)譜技術(shù),鑒定出A型流感病毒血凝素蛋白胞質(zhì)尾區(qū)的兩個棕櫚酰化位點(Cys562和Cys565)。也就是在這兩個位點上發(fā)生了脂質(zhì)共價修飾。正是由于棕櫚;梢陨婕安《旧芷诘亩鄠階段,特別是初始階段和最終階段,才使得A型流感病毒血凝素蛋白S-棕櫚;揎椀难芯勘毁x予了重要的意義。本實驗的研究也為完善流感病毒感染機制及發(fā)現(xiàn)新的作用靶點提供了相應(yīng)的信息。
[Abstract]:Influenza virus is the pathogen of influenza. The antigenicity of influenza A virus is easy to mutate and has caused worldwide pandemic many times. The emphasis on avian influenza virus stems from the Spanish pandemic that killed 50 million to 100 million people worldwide between 1918 and 1919. It is precisely because this kind of catastrophic thing appears time after time, has aroused the domestic and foreign experts and scholars to carry on the research intense interest, the scientific research worker goes on to study the influenza virus mystery one after another. In this dissertation, the interaction between influenza virus and host cell was studied in detail by using proteomics technique. In the experiment of influenza virus infecting Vero cells, 15 new differentially expressed proteins were found. It was found that the protein expressed specifically was modified after translation. Three groups of samples were analyzed by liquid phase mass spectrometry and 36 up-regulated proteins and 19 down-regulated proteins were found. In the experiment of palmitoacylation modification, the protein of influenza virus was analyzed and identified. The results showed that using acyl-biotin replacement reaction, affinity chromatography and mass spectrometry, Two palmitoacylation sites, Cys562 and Cys565, were identified in the cytoplasmic tail region of hemagglutinin protein of influenza A virus. In other words, lipid covalent modification occurs at these two sites. It is precisely because palm acylation can involve many stages of the virus life cycle, especially the initial stage and the final stage, that the study on the modification of hemagglutinin protein S- palm acylation of influenza A virus is of great significance. This study also provides information for the improvement of influenza virus infection mechanism and the discovery of new targets.
【學(xué)位授予單位】:吉林大學(xué)
【學(xué)位級別】:碩士
【學(xué)位授予年份】:2017
【分類號】:R373
【參考文獻】
相關(guān)期刊論文 前3條
1 方彩云;張曉勤;陸豪杰;;蛋白質(zhì)棕櫚酰化修飾的分析方法進展[J];分析化學(xué);2014年04期
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3 曾嶸,夏其昌;蛋白質(zhì)組學(xué)研究進展與趨勢[J];中國科學(xué)院院刊;2002年03期
,本文編號:1848467
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