臺灣博碩士論文加值系統

Ａ型流感病毒在分類學上屬於正黏液病毒科，每年都會造成季節性的大流行，是一種常見的流行性病原。由於Ａ型流感病毒具有高致病性及高變異性，目前並沒有理想的藥物及疫苗能夠有效治療並控制病毒傳播，因此必須了解病毒致病原理才能找到更有效的防疫方法。2001年發現的PB1-F2被認為是流感病毒毒性蛋白的一種，主要功能在抑制干擾素生成及增加二次細菌感染的風險，但PB1-F2在不同病毒株中，不論是表現量或是功能差異都相當大，換言之，PB1-F2在流感致病性上可能也扮演程度不一的重要性。
由於蛋白質穩定度決定病毒蛋白功能是否能夠有效發揮，我們針對分別來自於A/Hong Kong/156/1997 (H5N1) 及A/Puerto Rico/8/1934 (H1N1)不同病毒株、且表現量差異相當大的PB1-F2進行序列比對。經由互換序列製造PB1-F2鑲嵌蛋白，測試蛋白質穩定度及在細胞中的分佈位置，發現胺基酸序列I68, L69, V70, 及 F71使PB1-F2較為穩定，且提升PB1-F2分佈在細胞粒線體的比例。根據前人的研究，已知PB1-F2座落在粒線體時，可改變粒線體內外膜電位差、進而抑制干擾素生成；根據此一觀察，我們也進行實驗證實，當PB1-F2帶有ILVF序列時、其較為穩定及粒線體座落的特性,同時也強化了PB1-F2抑制IFN-β啟動子的功能。相對於宿主細胞來說，病毒感染時毒性蛋白PB1-F2的表現會對細胞造成的傷害，因此必須有效率地清除病原蛋白以降低細胞傷害。我們藉由觀察PR8 PB1-F2在細胞中的降解途徑，以了解宿主清除病毒蛋白的機制。發現在病毒感染時，宿主細胞可分別利用RIG-I 訊息傳遞鏈、以及粒線體自噬,活化特定的泛素酶以調節病毒蛋白降解。我們利用病毒感染、轉染RLR上游RIG-I、MAVS誘發的RLR訊息傳遞、或是利用羰基氰化物間氯苯腙（CCCP）模擬PB1-F2破壞粒線體膜電位，強化細胞自噬現象，可促進PB1-F2病毒蛋白降解。我們更進一步經由轉染RLR訊號鏈下游E3泛素酶RNF125或粒線體自噬關鍵蛋白Parkin-E3泛素酶，證明上述兩種E3泛素酶皆可強化PB1-F2的降解。我們的研究提供證據證明E3泛素酶不僅作用於蛋白酶體降解，同時也幫助宿主細胞調節先天性免疫反應及細胞自噬現象、並具有對抗流感病毒感染的重要功能。

Influenza A viruses (IAVs) belong to orthomyxoviridae that are enveloped viruses with eight negative sense, single stranded segmented RNA genomes. IAVs are highly contagious pathogens that cause seasonal epidemics and occasional pandemics in human. IAVs evolve easily and frequently, but current antiviral drugs or vaccines are yet to achieve satisfaction in controlling viral transmission or elimination of infection. In order to prevent and control IAV infection, comprehensive study on interplays between virus and host is therefore required to tackle the pathogenic mechanism. Since 2001, several novel IAV proteins including PB1-F2 have been identified, however their functions in pathogenesis remain elusive. PB1-F2 was considered a pro-apoptotic protein of IAVs, while the major function of PB1-F2 was suggested to inhibit type I interferon expression and enhance secondary bacterial infection. Intriguingly, PB1-F2 proteins isolated from different IAV strains vary largely in expression level, molecular weight, subcellular distribution, and function, implicating a role of PB1-F2 in supporting pathogenic diversity and adaptation to new host.
Recent studies have suggested that 2009pdm H1N1 virus does not express PB1-F2, and the attempt to rescue the full-length genetic codons by reverse genetics was shown to be unsuccessful to express the PB1-F2 protein. In order to pinpoint the critical sequence for stable expression of PB1-F2, we designed and compared serial chimeric PB1-F2 proteins by swapping PB1-F2 fragments from A/Hong Kong/156/1997 (H5N1) and A/Puerto Rico/8/1934 (H1N1), two strains of IAVs expressing qualitatively different PB1-F2 proteins. We have compared the protein stability, mitochondrial distribution, and IFN antagonist function of those PB1-F2 chimeras, and found that I68, L69, V70, and F71 are critical for mitochondrial functions of PB1-F2. Such mitochondria-resident PB1-F2 impairs mitochondrial function and triggers cytochrome c-mediated apoptosis, thus has been considered a virulent factor during IAV infection. We ask how infected cells sequester this virulent effect by tackling cellular factors towards degradation of PB1-F2 protein. We demonstrated that both RIG-signaling and Parkin mediated mitophagy significantly modulated PB1-F2 degradation. Our results not only revealed a modulated degradation of PR8-PB1-F2 by cellular innate immnune signaling alongside dysfunctional mitochrodria upon virus infection, but also a functional link between mitophagy and IAV infection.

Table of Contents
Chinese Abstract i
English Abstract ii
Table of Contents iii
List of Figures and tables v
Chapter 1. Introduction and research background 1
1.1 Influenza A virus 1
1.1.1 Classification of influenza viruses 1
1.1.2 influenza A virus infections in human 2
1.1.3 The structure of influenza A viruses 3
1.1.4 Viral proteins of Influenza A viruses 4
1.1.5 Influenza A virus life cycle: 16
1.2 Influenza A virus PB1-F2 18
1.2.1 The structure of PB1-F2 18
1.2.2 PB1-F2 regulates influenza A virus polymerase activity 19
1.2.3 Alternative functions of PB1-F2 19
1.3 Virus-host interaction of IAVs 20
1.3.1 Influenza A virus and apoptosis 20
1.3.2 Influenza A virus infection and innate immune responses 22
1.3.2.1 Ubiquitination regulates RLR signaling 25
1.3.3 PB1-F2 cross-talks with innate immunity 26
1.3.4 Influenza A virus infection and mitophagy 27
1.3.5 Interplay between PB1-F2 and Parkin in mitophagy 28
1.4 Parkin regulates autophagy 29
1.4.1 PINK1 interacts with Parkin 29
1.4.2 Parkin substrates and their regulations 30
1.4.2.1 Parkin mediates mitophagy 31
1.4.2.2 Parkin regulates the aggresome-autophagy pathway 32
1.4.2.3 Parkin mediates the mitochondrial-derived vesicles (MDVs) formation 33
1.5 References 34
Chapter 2. Amino acid residues 68-71 contribute to Influenza A virus PB1-F2 protein stability and functions 51
2.1 Abstract 51
2.2 Introduction 51
2.3 Materials and Methods 53
2.4 Results 57
2.5 Discussion 61
2.6 Figures and tables 65
2.7 References 78
Chapter 3. RIG-I signaling modulates degradation of Influenza A virus PB1-F2 protein. 80
3.1 Abstract 80
3.2 Introduction 80
3.3 Materials and Methods 82
3.4 Results 84
3.5 Discussion 89
3.6 Figures 92
3.7 References 103
Chapter 4. Parkin modulates degradation of Influenza A virus PB1-F2 protein via mitophagy 105
4.1 Abstract 105
4.2 Introduction 105
4.3 Materials and Methods 108
4.4 Results 111
4.5 Discussion 116
4.6 Figures 119
4.7 References 135

List of Figures and tables
Figure 2-1. Measurement of PB1-F2 half-life. 65
Figure 2-2. Mapping motif affecting PB1-F2 half-life. 67
Figure 2-3. Effects of K to R mutation on PB1-F2 half-life. 68
Figure 2-4. PB1-F2 (PR8) colocalized with ubiquitin signals. 69
Figure 2-5. Sensitivity to MG132 of PB1-F2 variants. 70
Figure 2-6. Cellular localization by immunofluorescence confocal microscopy. 71
Figure 2-7. IFN-β modulation by PB1-F2 variants. 72
Figure 2-8. Production of PB1-F2 during infection. 73
Table 2-1. Primer used for constructing PB1-F2 plasmids. 74
Table 2-2. Primer sequences. 75
Table 2-3. Primers and used for constructing PB1-F2 K to R mutants and PB1-F2 sequence comparison between wild-types and mutants. 76
Table 2-4. Primer sequences used for constructing PB1-F2 K to R mutants. 77
Figure 3-1. RIG-I induction caused PB1-F2 degradation. 92
Figure 3-2. NS1 expression rescued viral protein degradation. 93
Figure 3-3. MG132 treatment blocked the N-RIG-induced PB1-F2 degradation 94
Figure 3-4. The degradation of PB1-F2 was inhibited by expression of ubiquitin (K48R). 95
Figure 3-5. RNF125 enhanced PB1-F2 degradation. 97
Figure 3-6. PB1-F2 colocalized with RNF125 and ubiquitin. 98
Figure 3-8. 3-MA and bafilomycin blocked the N-RIG-induced PB1-F2 degradation 100
Figure 3-9. RNF125 overexpression inhibits virus production. 101
Figure 3-10. Schematic presentation of proposed model for negative regulation of PB1-F2 stability upon RIG-I activation. 102
Figure 4-1. PB1-F2 protein induces loss of MMP in transfected cells. 119
Figure 4-2. IAV infection induces mCherry-Parkin punctate formation and EGFP-LC3 colocalization. 121
Figure 4-3. Viral infection induced Parkin clustering at the mitochondria. 123
Figure 4-4. CCCP-induced mitophagy enhanced Parkin-mediated PB1-F2 degradation. 124
Figure 4-5 Parkin overexpression promotes PB1-F2 degradation. 125
Figure 4-6. Parkin-mediated PB1-F2 degradation was rescued by lysosomal inhibitors. 127
Figure 4-7. Parkin associated with EGFP-PB1-F2 for the ubiquitination. 129
Figure 4-8. Parkin modulated K63-linked poly-ubiquitination of PB1-F2. 130
Figure 4-9. EGFP-PB1-F2 mobilizes with the mCherry-Parkin and lysosome. 131
Figure 4-10. Parkin expression inhibits IAV RdRp activity and virus replication. 133
Figure 4-11. Schematic model of proteolysis mechanism of PB1-F2 via Parkin-modulated mitophgy. 134

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