Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/36313
標題: 參與竹嵌紋病毒衛星核酸複製之寄主因子的鑑定與特性分析
Identification and characterization of host factors involved in satBaMV RNA replication
作者: 潘士安
Prasanth, K.Reddisiva
關鍵字: Bamboo mosaic virus;竹嵌紋病毒;satBaMV;RNA-dependent RNA polymerase;host factors;GAPDH;竹嵌紋病毒衛星核酸
出版社: 生物科技學研究所
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摘要: 
Positive-strand RNA [(+) RNA] viruses are the largest genetic class of viruses and can only multiply their genomes in their host organisms. A successful viral infection requires an intimate interaction between the viral genomes/genome-encoded products and host cellular factors. RNA viruses replication is mediated by a virus-specific replicase complexes (RC) (Buck, 1996), which are membrane structures derived from cell organelles. These membrane structures recruit several host proteins and provide a suitable environment for viral RNA synthesis. Therefore, identification of host factors and analyses of their functions during virus replication could facilitate our understanding of the mechanism of virus infection.

Bamboo mosaic virus (BaMV), a member of the potexvirus group, contains a single stranded, positive-sense RNA genome with flexuous rod shaped morphology. In addition to the viral RNAs, BaMV strains may have a satellite RNA (satBaMV RNA) associated with them. SatBaMV RNAs are completely dependent on BaMV for replication, encapsidation and systemic movement, but they share little sequence homology with the BaMV virus genome. It is the only example of satRNA associated with the potexvirus group. In vitro BaMV RNA dependent RNA polymerase systems have been exploited for analyses of host and viral protein components enclosed in the RdRp complexes and the same complexes can be used for the replication of satBaMV RNA. Here, we report the identification of BaMV replicase complexes associated host proteins interacting with cis-acting RNA elements of satBaMV corresponding to the 5' and 3' UTRs of positive-strand by UV crosslinking assay [55 and 35 kDa (GAPDH) proteins were specifically cross-linked with both 5' and 3' UTR sequences, where as proteins of 22 (OEC 23 kDa subunit protein) and 20 kDa only with 5' end of satBaMV] and 3' end (-)159 nt of negative-strand satBaMV RNA using RNA affinity chromatography [ATP synthase CF1 beta subunit, 60S ribosomal protein L5, Photosystem II protein D1, NTP-binding helicase (ORFII of BaMV) and 40S ribosomal protein S9].

The potential function of the (+) 3' UTR-interacting protein (GAPDH) in BaMV and satBaMV replication was studied in detail by cloning the full length cDNA of cytosolic GAPDH from N. benthamiana and overexpressing it in E. coli. In vitro binding assays with the purified GAPDH showed that GAPDH binds preferably to the plus strand more efficiently than to the minus strand of BaMV and satBaMV RNAs. The binding regions of the GAPDH proteins were mapped to SLC and poly(A) containing region of satBaMV and pseudoknot and poly(A) containing region of BaMV 3' UTR RNA. Knockdown of GAPDH enhanced the BaMV and satBaMV RNA accumulation, consequently overexpression in Nicotiana benthamiana inhibited the accumulation of satBaMV and BaMV replication by 2-3 folds. The purified recombinant-GAPDH inhibited the synthesis of viral RNAs in in vitro RdRP assay. Knockdown of GAPDH in N. benthamiana enhances the replication of poly(A) containing viruses. These observations indicates that cytosolic-GAPDH negatively regulates the replication of BaMV and satBaMV RNA and also other poly(A) containing viruses.
URI: http://hdl.handle.net/11455/36313
其他識別: U0005-2807201116035000
Appears in Collections:生物科技學研究所

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