Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/90065
標題: The Structural Analysis of Bamboo Mosaic Virus
竹嵌紋病毒的結構分析
作者: 陳俊杰
Chun-Chieh Chen
關鍵字: 竹嵌紋病毒;外鞘蛋白;病毒結構;低溫冷凍電子顯微鏡技術;X-ray繞射技術;Bamboo mosaic virus;coat protein;virion structure;cryo-elctron microscopy;X-ray diffraction
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摘要: 
Potexvirus病毒群為單股正極性的植物 RNA 病毒,它具有短絲狀外形,長 約 490 nm、直徑約15 nm,為農業和生物科技應用上重要的病毒。竹嵌紋病毒 (Bamboo mosaic virus, BaMV) 經國內不同實驗室多年研究,已成此病毒群模式 病毒之一。本實驗室之前研究發現,BaMV外鞘蛋白 (coat protein, CP) 在二維 電泳分析呈現多型性,其中一型為N端缺失35個氨基酸(ΔN35),此區域為獨 特的glycine-rich motif (GRM)。將竹嵌紋病毒全長具感染力之cDNA株去除此35 個氨基酸的序列 (BaMV-Nd35-mCP),並不影響它在寄生植物中的複製,因此 已將BaMV-Nd35-mCP病毒成功的發展為一穩定的病毒載體,可在病毒表面大量 表達口蹄疫病毒的 VP1抗原胜肽,並成功免疫?隻保護口蹄疫病毒感染 (Yang et al., 2007)。本計畫擬進一步探討BaMV外鞘蛋白N端氨基酸序列在病毒生活史 的生物功能,藉由構築N端氨基酸序列缺失株,測試其對病毒複製、包被、病徵 表現與細胞內定位的影響。並利用蛋白質表現系統,純化全長及N端氨基酸缺失 外鞘蛋白,在in vitro情況下,測試其自我組裝能力 (self-assembly)。同時,本 計畫擬利用低溫冷凍電子顯微鏡技術及單一病毒顆粒分析 (single particle analysis) 的3-D立體影像重組技術,以及配合X-ray繞射技術進一步解析BaMV 病毒顆粒的構造與其鞘蛋白的排列。此計劃所獲得的結果,不僅有助於了解絲狀 病毒N端鞘蛋白的功能,亦有助於有效率病毒載體之研發。

Most viruses use a hollow protein shell, the capsid, to package the viral genome, either RNA or DNA. Virus capsids are large, symmetric oligomers made of many copies of one or a few types of protein subunits. Self-assembly of a viral capsid is a complex oligomerization process that proceeds along a pathway regulated by ordered interactions between the participating protein subunits, and that involves a series of (usually transient) assembly intermediates. Assembly of many virus capsids requires the assistance of scaffolding proteins or the viral nucleic acid, which interact with the capsid subunits to promote and direct the process. Once assembled, many capsids undergo a maturation reaction that involves covalent modification and/or conformational rearrangements, which may increase the stability of the virus particle. The final, mature capsid is a relatively robust protein complex able to protect the viral genome from physicochemical aggressions; however, it is also a metastable, dynamic structure poised to undergo controlled conformational transitions required to perform biologically critical functions during virus entry into cells, intracellular trafficking, and viral genome unloading. The function-driven conformation transitions are affected by temperature, pH, ionic strength, solvent, ligands and effector molecules, and interactions with other molecules. Thus, the structural analysis of viruses forms a basis for understanding viral functions in its life cycle.
Bamboo mosaic virus (BaMV) is a single-stranded RNA virus with a flexible filamentous morphology. It has become one of the model Potexvirus for basic research not only because of its impacts on agriculture, but also its application in biotechnology through great efforts by several research groups in Taiwan pioneered by Dr. Lin, Na-Sheng and Dr. Hsu, Yau-Heiu. However, its lack of the atomic structure model limited the understanding in its virion assembly, structural stability, virus infectious cycle, and the further applications in nano-technology in bio-engineering. In order to fill the structural knowledge of BaMV, several BaMV-CP mutants were analyzed in this 8-years-long research.
At the early attempts of the research, we used various technologies including tilt-pair single particle analysis (Part 2), x-ray fiber diffraction, cryo-electron microscopy (CryoEM) with charge-coupled device (CCD) and atomic force microscopy (AFM) (part 3) without conclusive results. Until a direct-detector-device (DDD) was introduced to capture CryoEM images followed by 3D reconstruction using the iterative helical real space reconstruction (IHRSR) algorithm and Rosetta program, the near-atomic structure of BaMV was obtained (Part 4). Combining protein and RNA structural data, the first near atomic structural model of flexible filamentous virus was finally determined. According to the model, the RNA and CP subunits of BaMV follow a left-handed path, instead of a right-handed as proposed. In contrast to the compact assembly of Tobacco mosaic virus (TMV) subunits, BaMV contains a compact core with extended N- and C-terminal portions that make contacts with surrounding subunits in both the same and adjacent turns. The flexible links between the core and the extensions allow the virion to bend and twist while still maintaining its structural integrity.
The new finding will help the understanding BaMV, a flexible filamentous virus, in its CP interaction with viral RNA, its virion assembly, its structural stability, the development of viral vectors and can be potentially useful for biotechnology, such as in vaccines, biomaterials for drug delivery or imaging, or recombinant protein production in plants.
URI: http://hdl.handle.net/11455/90065
Rights: 同意授權瀏覽/列印電子全文服務,2015-08-31起公開。
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