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完整後設資料紀錄
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.advisor | 陳培哲(Pei-Jer Chen) | |
dc.contributor.author | Ya-Wen Chang | en |
dc.contributor.author | 張雅雯 | zh_TW |
dc.date.accessioned | 2021-06-13T00:28:39Z | - |
dc.date.available | 2008-08-08 | |
dc.date.copyright | 2007-08-08 | |
dc.date.issued | 2007 | |
dc.date.submitted | 2007-07-26 | |
dc.identifier.citation | 1. Beck, J., and M. Nassal. 2007. Hepatitis B virus replication. World J Gastroenterol 13:48-64.
2. Blumberg, B. S., B. J. Gerstley, D. A. Hungerford, W. T. London, and A. I. Sutnick. 1967. A serum antigen (Australia antigen) in Down's syndrome, leukemia, and hepatitis. Ann Intern Med 66:924-31. 3. Bruss, V. 2007. Hepatitis B virus morphogenesis. World J Gastroenterol 13:65-73. 4. Budkowska, A., C. Quan, F. Groh, P. Bedossa, P. Dubreuil, J. P. Bouvet, and J. Pillot. 1993. Hepatitis B virus (HBV) binding factor in human serum: candidate for a soluble form of hepatocyte HBV receptor. J Virol 67:4316-22. 5. Chan, S. Y., C. J. Empig, F. J. Welte, R. F. Speck, A. Schmaljohn, J. F. Kreisberg, and M. A. Goldsmith. 2001. Folate receptor-alpha is a cofactor for cellular entry by Marburg and Ebola viruses. Cell 106:117-26. 6. Cheng, D., C. C. Hoogenraad, J. Rush, E. Ramm, M. A. Schlager, D. M. Duong, P. Xu, S. R. Wijayawardana, J. Hanfelt, T. Nakagawa, M. Sheng, and J. Peng. 2006. Relative and absolute quantification of postsynaptic density proteome isolated from rat forebrain and cerebellum. Mol Cell Proteomics 5:1158-70. 7. Cooper, A., N. Paran, and Y. Shaul. 2003. The earliest steps in hepatitis B virus infection. Biochim Biophys Acta 1614:89-96. 8. Dantzig, J. A., T. Y. Liu, and Y. E. Goldman. 2006. Functional studies of individual myosin molecules. Ann N Y Acad Sci 1080:1-18. 9. Dash, S., K. V. Rao, and S. K. Panda. 1992. Receptor for pre-S1(21-47) component of hepatitis B virus on the liver cell: role in virus cell interaction. J Med Virol 37:116-21. 10. De Falco, S., M. G. Ruvoletto, A. Verdoliva, M. Ruvo, A. Raucci, M. Marino, S. Senatore, G. Cassani, A. Alberti, P. Pontisso, and G. Fassina. 2001. Cloning and expression of a novel hepatitis B virus-binding protein from HepG2 cells. J Biol Chem 276:36613-23. 11. Fantin, V. R., J. St-Pierre, and P. Leder. 2006. Attenuation of LDH-A expression uncovers a link between glycolysis, mitochondrial physiology, and tumor maintenance. Cancer Cell 9:425-34. 12. Funk, A., M. Mhamdi, H. Will, and H. Sirma. 2007. Avian hepatitis B viruses: molecular and cellular biology, phylogenesis, and host tropism. World J Gastroenterol 13:91-103. 13. Glebe, D., and S. Urban. 2007. Viral and cellular determinants involved in hepadnaviral entry. World J Gastroenterol 13:22-38. 14. Glebe, D., S. Urban, E. V. Knoop, N. Cag, P. Krass, S. Grun, A. Bulavaite, K. Sasnauskas, and W. H. Gerlich. 2005. Mapping of the hepatitis B virus attachment site by use of infection-inhibiting preS1 lipopeptides and tupaia hepatocytes. Gastroenterology 129:234-45. 15. Gripon, P., I. Cannie, and S. Urban. 2005. Efficient inhibition of hepatitis B virus infection by acylated peptides derived from the large viral surface protein. J Virol 79:1613-22. 16. Gripon, P., S. Rumin, S. Urban, J. Le Seyec, D. Glaise, I. Cannie, C. Guyomard, J. Lucas, C. Trepo, and C. Guguen-Guillouzo. 2002. Infection of a human hepatoma cell line by hepatitis B virus. Proc Natl Acad Sci U S A 99:15655-60. 17. Gygi, S. P., B. Rist, S. A. Gerber, F. Turecek, M. H. Gelb, and R. Aebersold. 1999. Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat Biotechnol 17:994-9. 18. Hartmann-Stuhler, C., and R. Prange. 2001. Hepatitis B virus large envelope protein interacts with gamma2-adaptin, a clathrin adaptor-related protein. J Virol 75:5343-51. 19. Hemmerich, P., A. von Mikecz, F. Neumann, O. Sozeri, G. Wolff-Vorbeck, R. Zoebelein, and U. Krawinkel. 1993. Structural and functional properties of ribosomal protein L7 from humans and rodents. Nucleic Acids Res 21:223-31. 20. Jacobelli, J., S. A. Chmura, D. B. Buxton, M. M. Davis, and M. F. Krummel. 2004. A single class II myosin modulates T cell motility and stopping, but not synapse formation. Nat Immunol 5:531-8. 21. Kim, H., H. Arakawa, N. Hatae, Y. Sugimoto, O. Matsumoto, T. Osada, A. Ichikawa, and A. Ikai. 2006. Quantification of the number of EP3 receptors on a living CHO cell surface by the AFM. Ultramicroscopy 106:652-62. 22. Kock, J., M. Nassal, S. MacNelly, T. F. Baumert, H. E. Blum, and F. von Weizsacker. 2001. Efficient infection of primary tupaia hepatocytes with purified human and woolly monkey hepatitis B virus. J Virol 75:5084-9. 23. Kuroki, K., R. Cheung, P. L. Marion, and D. Ganem. 1994. A cell surface protein that binds avian hepatitis B virus particles. J Virol 68:2091-6. 24. Kuroki, K., F. Eng, T. Ishikawa, C. Turck, F. Harada, and D. Ganem. 1995. gp180, a host cell glycoprotein that binds duck hepatitis B virus particles, is encoded by a member of the carboxypeptidase gene family. J Biol Chem 270:15022-8. 25. Lambert, C., and R. Prange. 2003. Chaperone action in the posttranslational topological reorientation of the hepatitis B virus large envelope protein: Implications for translocational regulation. Proc Natl Acad Sci U S A 100:5199-204. 26. Lee, B., M. Sharron, L. J. Montaner, D. Weissman, and R. W. Doms. 1999. Quantification of CD4, CCR5, and CXCR4 levels on lymphocyte subsets, dendritic cells, and differentially conditioned monocyte-derived macrophages. Proc Natl Acad Sci U S A 96:5215-20. 27. Levert, K. L., G. L. Waldrop, and J. M. Stephens. 2002. A biotin analog inhibits acetyl-CoA carboxylase activity and adipogenesis. J Biol Chem 277:16347-50. 28. Li, W., M. J. Moore, N. Vasilieva, J. Sui, S. K. Wong, M. A. Berne, M. Somasundaran, J. L. Sullivan, K. Luzuriaga, T. C. Greenough, H. Choe, and M. Farzan. 2003. Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus. Nature 426:450-4. 29. Menne, S., and P. J. Cote. 2007. The woodchuck as an animal model for pathogenesis and therapy of chronic hepatitis B virus infection. World J Gastroenterol 13:104-24. 30. Metspalu, A., A. Rebane, S. Hoth, M. Pooga, J. Stahl, and J. Kruppa. 1992. Human ribosomal protein S3a: cloning of the cDNA and primary structure of the protein. Gene 119:313-6. 31. Nassal, M. 1999. Hepatitis B virus replication: novel roles for virus-host interactions. Intervirology 42:100-16. 32. Negrete, O. A., E. L. Levroney, H. C. Aguilar, A. Bertolotti-Ciarlet, R. Nazarian, S. Tajyar, and B. Lee. 2005. EphrinB2 is the entry receptor for Nipah virus, an emergent deadly paramyxovirus. Nature 436:401-5. 33. Neurath, A. R., S. B. Kent, N. Strick, and K. Parker. 1986. Identification and chemical synthesis of a host cell receptor binding site on hepatitis B virus. Cell 46:429-36. 34. Neurath, A. R., B. Seto, and N. Strick. 1989. Antibodies to synthetic peptides from the preS1 region of the hepatitis B virus (HBV) envelope (env) protein are virus-neutralizing and protective. Vaccine 7:234-6. 35. Petit, M. A., F. Capel, S. Dubanchet, and H. Mabit. 1992. PreS1-specific binding proteins as potential receptors for hepatitis B virus in human hepatocytes. Virology 187:211-22. 36. Pontisso, P., M. A. Petit, M. J. Bankowski, and M. E. Peeples. 1989. Human liver plasma membranes contain receptors for the hepatitis B virus pre-S1 region and, via polymerized human serum albumin, for the pre-S2 region. J Virol 63:1981-8. 37. Pontisso, P., M. G. Ruvoletto, W. H. Gerlich, K. H. Heermann, R. Bardini, and A. Alberti. 1989. Identification of an attachment site for human liver plasma membranes on hepatitis B virus particles. Virology 173:522-30. 38. Prive, G. G. 2007. Detergents for the stabilization and crystallization of membrane proteins. Methods 41:388-97. 39. Puig, O., F. Caspary, G. Rigaut, B. Rutz, E. Bouveret, E. Bragado-Nilsson, M. Wilm, and B. Seraphin. 2001. The tandem affinity purification (TAP) method: a general procedure of protein complex purification. Methods 24:218-29. 40. Schaefer, S. 2007. Hepatitis B virus taxonomy and hepatitis B virus genotypes. World J Gastroenterol 13:14-21. 41. Schaefer, S. 2005. Hepatitis B virus: significance of genotypes. J Viral Hepat 12:111-24. 42. Stebbins, C. E., A. A. Russo, C. Schneider, N. Rosen, F. U. Hartl, and N. P. Pavletich. 1997. Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent. Cell 89:239-50. 43. Steven, A. C., and P. G. Spear. 2006. Biochemistry. Viral glycoproteins and an evolutionary conundrum. Science 313:177-8. 44. Tong, S., J. Li, and J. R. Wands. 1999. Carboxypeptidase D is an avian hepatitis B virus receptor. J Virol 73:8696-702. 45. Urban, S., K. M. Breiner, F. Fehler, U. Klingmuller, and H. Schaller. 1998. Avian hepatitis B virus infection is initiated by the interaction of a distinct pre-S subdomain with the cellular receptor gp180. J Virol 72:8089-97. 46. Urban, S., C. Schwarz, U. C. Marx, H. Zentgraf, H. Schaller, and G. Multhaup. 2000. Receptor recognition by a hepatitis B virus reveals a novel mode of high affinity virus-receptor interaction. Embo J 19:1217-27. 47. Wakil, S. J. 1989. Fatty acid synthase, a proficient multifunctional enzyme. Biochemistry 28:4523-30. | |
dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/28901 | - |
dc.description.abstract | 人類B型肝炎病毒(HBV)為世界性的流行病原,在亞洲地區尤其嚴重。它會在人體引發肝臟疾病,而慢性肝炎的病人後期可能轉變為肝硬化、肝腫瘤等。HBV早期感染過程的研究十分困難,因缺乏良好的感染細胞株或小動物模式,直到目前,HBV的細胞受器仍屬未知。HBV外套膜上具有三種表面抗原,分別為大型(large)、中型(middle)、小型(small)蛋白,其中大型表面抗原具有可能的受器結合位置。
本文實驗中,使用兩階段親合性標籤純化(TAP)系統來純化大量的大型表面抗原以及與大型表面抗原結合的蛋白質聚合體,希望從與大型表面抗原結合的細胞蛋白質中發現可能的HBV細胞受器。首先,使用動物細胞株來大量表現含有親合性標籤的重組大型表面抗原,並利用TAP系統純化出大量的重組蛋白。再將重組蛋白與人類原始肝細胞的細胞膜蛋白進行結合實驗,人類原始肝細胞確定可感染HBV並含有HBV細胞受器。之後再次進行TAP純化實驗,純化出與重組大型表面抗原結合的蛋白質聚合體,並利用質譜儀分析,辨認這些結合的蛋白質。 經過多次的改善純化方式與結合實驗,找到了一些會與重組大型表面抗原結合的蛋白質,但並未發現可能的HBV細胞受器,找到的結合蛋白可能與大型表面抗原在細胞中的轉譯後修飾相關。 | zh_TW |
dc.description.abstract | Human hepatitis B virus (HBV) is endemic in many places in the world, especially in Asian. It may cause serious liver diseases, like liver fibrosis, cirrhosis, and hepatocellular carcinoma (HCC). HBV cellular receptor is not yet known. Lacking of proper susceptible culture system and animal model makes it difficult to study the early process of virus infection. There are three glycoproteins in HBV surface antigens: large, middle, and small. The large protein is thought contain the cellular receptor binding site.
In my study, I use the mammalian tandem affinity purification (TAP) system to purify the recombinant large HBV surface antigen and the interaction complex, to find the recombinant large HBsAg interaction protein. There might be receptor candidates in these interaction proteins. First, purify tagged large protein expressed in mammalian cells. Then, incubate the purified recombinant proteins with human primary hepatocyte membrane proteins, which contain the cellular receptor of HBV. Use TAP system again to purify the interaction protein complexes of large protein. Utilize mass spectrometer to identify these interaction proteins. After several experimental improvements in purification and binding assay, I find some cellular proteins interact with recombinant large protein. But it’s not found any receptor candidate in these interaction proteins. The found interaction proteins are probably related with large protein post-translational modification. | en |
dc.description.provenance | Made available in DSpace on 2021-06-13T00:28:39Z (GMT). No. of bitstreams: 1 ntu-96-R94445105-1.pdf: 2137359 bytes, checksum: 10c7fc81da19bdab7d5c5e596aabc6a0 (MD5) Previous issue date: 2007 | en |
dc.description.tableofcontents | 口試委員會審定書………………………………………………………………. i
誌謝………………………………………………………………………………. ii 中文摘要…………………………………………………………………………. iii 英文摘要…………………………………………………………………………. iv 目錄………………………………………………………………………………. v 圖次………………………………………………………………………………. vi 表次………………………………………………………………………………. vii 壹、序論…………………………………………………………………………. 1 B型肝炎病毒簡介…………………………………………………………. 1 B型肝炎病毒構造與基因…………………………………………………. 2 B型肝炎病毒生活史………………………………………………………. 3 過去對於B型肝炎受器的研究…………………………………………… 4 鴨肝病毒(DHBV)研究……………………………………………………... 5 其他病毒與非病毒受器的研究……………………………………………. 6 研究目的與假設……………………………………………………………. 7 實驗設計……………………………………………………………………. 8 貳、實驗材料與方法…………………………………………………………….. 9 表現重組HBV表面抗原蛋白之DNA質體製備(cloning)……………….. 9 表現重組蛋白之動物細胞株(cell line)……………………………………. 10 質體轉染(plasmid transfection)…………………………………………….. 10 兩階段親合性標籤純化系統Tandem affinity purification system (TAP)… 10 西方墨點法(Western blotting)……………………………………………… 11 銀染色法(silver staining)…………………………………………………… 12 肝細胞膜蛋白純化…………………………………………………………. 13 重組病毒抗原蛋白與肝細胞膜蛋白作用…………………………………. 13 參、結果…………………………………………………………………………… 15 大量表現重組B型肝炎表面抗原…………………………………………. 15 兩階段親合性標籤純化(TAP)…………………………………………….. 16 改善TAP純化系統………………………………………………………… 17 純化肝細胞膜蛋白…………………………………………………………. 20 與純化後重組L蛋白互相影響之肝細胞膜蛋白…………………………. 20 肆、討論………………………………………………………………………….. 25 附圖……………………………………………………………………………….. 30 附表……………………………………………………………………………….. 51 伍、參考文獻…………………………………………………………………….. 54 附錄……………………………………………………………………………….. 60 | |
dc.language.iso | zh-TW | |
dc.title | 辨識與重組B型肝炎大型表面抗原互相影響之細胞蛋白 | zh_TW |
dc.title | Identification of cellular proteins associated with the recombinant chimeric HBV large surface antigen | en |
dc.type | Thesis | |
dc.date.schoolyear | 95-2 | |
dc.description.degree | 碩士 | |
dc.contributor.oralexamcommittee | 陳玉如(Yu-Ju Chen),黃麗華(Lih-Hwa Hwang) | |
dc.subject.keyword | B型肝炎病毒,表面抗原,受器, | zh_TW |
dc.subject.keyword | HBV,surface antigen,receptor, | en |
dc.relation.page | 73 | |
dc.rights.note | 有償授權 | |
dc.date.accepted | 2007-07-26 | |
dc.contributor.author-college | 醫學院 | zh_TW |
dc.contributor.author-dept | 微生物學研究所 | zh_TW |
顯示於系所單位: | 微生物學科所 |
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