Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/12951
標題: 羊傳染性化膿性病毒ATPase活性及功能區塊分析
Activity and functional motifs of ATPase of orf virus
作者: 林峰源
Lin, Fong-Yuan
關鍵字: orf virus
羊傳染性化膿性病毒
A32L protein
ATPase
A32L蛋白
ATPase
出版社: 獸醫學系暨研究所
引用: chapter 1 1. Baxby, D., and M. Bennett. 1997. Poxvirus zoonoses. J Med Microbiol 46:17-20, 28-33. 2. Cassetti, M. C., M. Merchlinsky, E. J. Wolffe, A. S. Weisberg, and B. Moss. 1998. DNA packaging mutant: Repression of the vaccinia virus A32 gene results in noninfectious, DNA-deficient, spherical, enveloped particles. Journal of Virology 72:5769-5780. 3. Chan, K. W., J. W. Lin, S. H. Lee, C. J. Liao, M. C. Tsai, W. L. Hsu, M. L. Wong, and H. C. Shih. 2007. Identification and phylogenetic analysis of orf virus from goats in Taiwan. Virus Genes 35:705-12. 4. Chan, K. W., C. H. Yang, J. W. Lin, H. C. Wang, F. Y. Lin, S. T. Kuo, M. L. Wong, and W. L. Hsu. 2009. Phylogenetic analysis of parapoxviruses and the C-terminal heterogeneity of viral ATPase proteins. Gene 432:44-53. 5. Damon, I. K. 2007. Poxviruses, p. 2947-2975. In D. M. Knipe, D. E. Griffin, M. A. Martin, R. A. Lamb, B. Roizman, and S. E. Straus (ed.), Fields Virology, 5 ed. Lippincott, Williams and Wilkins, Philadelphia, PA. 6. Fenner, F. 1996. Poxviruses, p. 2673-2702. In B. N. Fields, Knipe, D.M., Howley, P.M. (ed.), Fields Virology, 3 ed. Lippincott-Raven, Philadelphia, PA. 7. Fleming, S. B., D. M. Haig, P. Nettleton, H. W. Reid, C. A. McCaughan, L. M. Wise, and A. Mercer. 2000. Sequence and functional analysis of a homolog of interleukin-10 encoded by the parapoxvirus orf virus. Virus Genes 21:85-95. 8. Gumbrell, R. C., and D. A. McGregor. 1997. Outbreak of severe fatal orf in lambs. Vet Rec 141:150-1. 9. Haig, D. M., and A. A. Mercer. 1998. Orf. Veterinary Research 29:311-326. 10. Haig, D. M., and A. A. Mercer. 1998. Ovine diseases. Orf. Vet Res 29:311-26. 11. Inoshima, Y., A. Morooka, and H. Sentsui. 2000. Detection and diagnosis of parapoxvirus by the polymerase chain reaction. J Virol Methods 84:201-8. 12. Johannessen, J. V., H. K. Krogh, I. Solberg, A. Dalen, H. van Wijngaarden, and B. Johansen. 1975. Human orf. J Cutan Pathol 2:265-83. 13. Koonin, E. V., T. G. Senkevich, and V. I. Chernos. 1993. Gene A32 product of vaccinia virus may be an ATPase involved in viral DNA packaging as indicated by sequence comparisons with other putative viral ATPases. Virus Genes 7:89-94. 14. Kuroda, Y., M. Yoshida, T. Shibahara, T. Matsui, T. Nakane, H. Hara, Y. Inoshima, and H. Sentsui. 1999. An epidemic of parapoxvirus infection among cattle: isolation and antibody survey. J Vet Med Sci 61:749-53. 15. Lyttle, D. J., K. M. Fraser, S. B. Fleming, A. A. Mercer, and A. J. Robinson. 1994. Homologs of vascular endothelial growth factor are encoded by the poxvirus orf virus. J Virol 68:84-92. 16. McKeever, D. J., D. M. Jenkinson, G. Hutchison, and H. W. Reid. 1988. Studies of the pathogenesis of orf virus infection in sheep. J Comp Pathol 99:317-28. 17. McKeever, D. J., and H. W. Reid. 1986. Survival of orf virus under British winter conditions. Vet Rec 118:613-4. 18. Mercer, A. A., K. M. Fraser, and J. J. Esposito. 1996. Gene homology between orf virus and smallpox variola virus. Virus Genes 13:175-8. 19. Moss, B. 1996. The viruses and their replication, p. 1163-1197. In F. B.N. and K. P.M. (ed.), Fundamental Virology. Lippencott Raven publishers, Philadelphia. 20. Nitsche, A., M. Buttner, S. Wilhelm, G. Pauli, and H. Meyer. 2006. Real-time PCR detection of parapoxvirus DNA. Clin Chem 52:316-9. 21. Robinson, A. J., and A. A. Mercer. 1995. Parapoxvirus of red deer: evidence for its inclusion as a new member in the genus parapoxvirus. Virology 208:812-5. 22. Robinson, A. J. L., D. J. 1992. Parapoxviruses: their biology and potential as recombinant vaccines, p. 285-327. In M. B. G. L. S. B. Raton (ed.), Recombinant Poxviruses. FL:CRC Press. 23. Savory, L. J., S. A. Stacker, S. B. Fleming, B. E. Niven, and A. A. Mercer. 2000. Viral vascular endothelial growth factor plays a critical role in orf virus infection. J Virol 74:10699-706. 24. Tsai, S. M., K. W. Chan, W. L. Hsu, T. J. Chang, M. L. Wong, and C. Y. Wang. 2009. Development of a loop-mediated isothermal amplification for rapid detection of orf virus. J Virol Methods 157:200-4. 25. Valencia, A., P. Chardin, A. Wittinghofer, and C. Sander. 1991. The ras protein family: evolutionary tree and role of conserved amino acids. Biochemistry 30:4637-48. 26. Walker, J. E., M. Saraste, M. J. Runswick, and N. J. Gay. 1982. Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J 1:945-51. 27. Wittek, R., C. C. Kuenzle, and R. Wyler. 1979. High C + G content in parapoxvirus DNA. J Gen Virol 43:231-4. 28. Yirrell, D. L., J. P. Vestey, and M. Norval. 1994. Immune responses of patients to orf virus infection. Br J Dermatol 130:438-43. chapter 2 1. Bayliss, C. D., and R. C. Condit. 1995. The vaccinia virus A18R gene product is a DNA-dependent ATPase. J Biol Chem 270:1550-6. 2. Cassetti, M. C., M. Merchlinsky, E. J. Wolffe, A. S. Weisberg, and B. Moss. 1998. DNA packaging mutant: repression of the vaccinia virus A32 gene results in noninfectious, DNA-deficient, spherical, enveloped particles. J Virol 72:5769-80. 3. Chan, K. W., W. L. Hsu, C. Y. Wang, C. H. Yang, F. Y. Lin, S. Chulakasian, and M. L. Wong. 2009. Differential diagnosis of orf viruses by a single-step PCR. J Virol Methods 160:85-9. 4. Chan, K. W., C. H. Yang, J. W. Lin, H. C. Wang, F. Y. Lin, S. T. Kuo, M. L. Wong, and W. L. Hsu. 2009. Phylogenetic analysis of parapoxviruses and the C-terminal heterogeneity of viral ATPase proteins. Gene 432:44-53. 5. Damon, I. K. 2007. Poxviruses, p. 2947-2975. In D. M. Knipe, D. E. Griffin, M. A. Martin, R. A. Lamb, B. Roizman, and S. E. Straus (ed.), Fields Virology, 5 ed. Lippincott, Williams and Wilkins, Philadelphia, PA. 6. Delhon, G., E. R. Tulman, C. L. Afonso, Z. Lu, A. de la Concha-Bermejillo, H. D. Lehmkuhl, M. E. Piccone, G. F. Kutish, and D. L. Rock. 2004. Genomes of the parapoxviruses ORF virus and bovine papular stomatitis virus. J Virol 78:168-77. 7. Deng, L., and S. Shuman. 1998. Vaccinia NPH-I, a DExH-box ATPase, is the energy coupling factor for mRNA transcription termination. Genes Dev 12:538-46. 8. Gumbrell, R. C., and D. A. McGregor. 1997. Outbreak of severe fatal orf in lambs. Vet Rec 141:150-1. 9. Haig, D. M., and A. A. Mercer. 1998. Ovine diseases. Orf. Vet Res 29:311-26. 10. Iyer, L. M., L. Aravind, and E. V. Koonin. 2001. Common origin of four diverse families of large eukaryotic DNA viruses. J Virol 75:11720-34. 11. Koonin, E. V., T. G. Senkevich, and V. I. Chernos. 1993. Gene A32 product of vaccinia virus may be an ATPase involved in viral DNA packaging as indicated by sequence comparisons with other putative viral ATPases. Virus Genes 7:89-94. 12. Kuo, M. D., C. Chin, S. L. Hsu, J. Y. Shiao, T. M. Wang, and J. H. Lin. 1996. Characterization of the NTPase activity of Japanese encephalitis virus NS3 protein. J Gen Virol 77 ( Pt 9):2077-84. 13. Mazur, C., and R. D. Machado. 1989. Detection of contagious pustular dermatitis virus of goats in a severe outbreak. Vet Rec 125:419-20. 14. Mercer, A. A., N. Ueda, S. M. Friederichs, K. Hofmann, K. M. Fraser, T. Bateman, and S. B. Fleming. 2006. Comparative analysis of genome sequences of three isolates of Orf virus reveals unexpected sequence variation. Virus Res 116:146-58. 15. Mondal, B., A. K. Bera, M. Hosamani, P. A. Tembhurne, and S. K. Bandyopadhyay. 2006. Detection of Orf virus from an outbreak in goats and its genetic relation with other parapoxviruses. Vet Res Commun 30:531-9. 16. Moss, B. 2007. Poxviridae: the viruses and their replication, p. 2905-2945. In D. M. Knipe, D. E. Griffin, M. A. Martin, R. A. Lamb, B. Roizman, and S. E. Straus (ed.), Fields Virology, 5 ed. Lippincott, Williams and Wilkins, Philadelphia, PA. 17. Ramadevi, N., and P. Roy. 1998. Bluetongue virus core protein VP4 has nucleoside triphosphate phosphohydrolase activity. J Gen Virol 79 ( Pt 10):2475-80. 18. Reid, H. W. 1991. Disease of Sheep, 2 ed. Oxford, Blackwell scientific publication, London. 19. Simpson, D. A., and R. C. Condit. 1995. Vaccinia virus gene A18R encodes an essential DNA helicase. J Virol 69:6131-9. 20. Su, Y. P., J. H. Shien, H. J. Liu, H. S. Yin, and L. H. Lee. 2007. Avian reovirus core protein muA expressed in Escherichia coli possesses both NTPase and RTPase activities. J Gen Virol 88:1797-805. chapter 3 1. Bell, C. E. 2005. Structure and mechanism of Escherichia coli RecA ATPase. Molecular Microbiology 58:358-66. 2. Buttner, M., and H. J. Rziha. 2002. Parapoxviruses: From the lesion to the viral genome. Journal of Veterinary Medicine Series B-Infectious Diseases and Veterinary Public Health 49:7-16. 3. Cassetti, M. C., M. Merchlinsky, E. J. Wolffe, A. S. Weisberg, and B. Moss. 1998. DNA packaging mutant: Repression of the vaccinia virus A32 gene results in noninfectious, DNA-deficient, spherical, enveloped particles. Journal of Virology 72:5769-5780. 4. Chan, K. W., C. H. Yang, J. W. Lin, H. C. Wang, F. Y. Lin, S. T. Kuo, M. L. Wong, and W. L. Hsu. 2009. Phylogenetic analysis of parapoxviruses and the C-terminal heterogeneity of viral ATPase proteins. Gene 432:44-53. 5. Delhon, G., E. R. Tulman, C. L. Afonso, Z. Lu, A. de la Concha-Bermejillo, H. D. Lehmkuhl, M. E. Piccone, G. F. Kutish, and D. L. Rock. 2004. Genomes of the parapoxviruses orf virus and bovine Papular stomatitis virus. Journal of Virology 78:168-177. 6. Gumbrell, R. C., and D. A. McGregor. 1997. Outbreak of severe fatal orf in lambs. Veterinary Record 141:150-151. 7. Guo, P. X., and T. J. Lee. 2007. Viral nanomotors for packaging of dsDNA and dsRNA. Molecular Microbiology 64:886-903. 8. Haig, D. M., and A. A. Mercer. 1998. Orf. Veterinary Research 29:311-326. 9. Heckman, K. L., and L. R. Pease. 2007. Gene splicing and mutagenesis by PCR-driven overlap extension. Nature Protocols 2:924-932. 10. Iyer, L. M., L. Aravind, and E. V. Koonin. 2001. Common origin of four diverse families of large eukaryotic DNA viruses. Journal of Virology 75:11720-34. 11. Iyer, L. M., K. S. Makarova, E. V. Koonin, and L. Aravind. 2004. Comparative genomics of the FtsK-HerA superfamily of pumping ATPases: implications for the origins of chromosome segregation, cell division and viral capsid packaging. Nucleic Acids Research 32:5260-5279. 12. Jakovljevic, V., S. Leonardy, M. Hoppert, and L. Sogaard-Andersen. 2008. PilB and PilT are ATPases acting antagonistically in type IV pilus function in Myxococcus xanthus. Journal of Bacteriology 190:2411-2421. 13. Kim, D. W., J. Kim, Y. Gwack, J. H. Han, and J. Choe. 1997. Mutational analysis of the hepatitis C virus RNA helicase. Journal of Virology 71:9400-9409. 14. Kondabagil, K. R., Z. H. Zhang, and V. B. Rao. 2006. The DNA translocating ATPase of bacteriophage T4 packaging motor. Journal of Molecular Biology 363:486-499. 15. Koonin, E. V. 1997. Evidence for a family of archaeal ATPases. Science 275:1489-1490. 16. Koonin, E. V., T. G. Senkevich, and V. I. Chernos. 1993. Gene-A32 Product of Vaccinia Virus May Be an Atpase Involved in Viral-DNA Packaging as Indicated by Sequence Comparisons with Other Putative Viral ATPases. Virus Genes 7:89-94. 17. Kuo, M. D., C. Chin, S. L. Hsu, J. Y. Shiao, T. M. Wang, and J. H. Lin. 1996. Characterization of the NTPase activity of Japanese encephalitis virus NS3 protein. J Gen Virol 77 ( Pt 9):2077-84. 18. Leipe, D. D., E. V. Koonin, and L. Aravind. 2003. Evolution and classification of P-loop kinases and related proteins. J Mol Biol 333:781-815. 19. Leipe, D. D., Y. I. Wolf, E. V. Koonin, and L. Aravind. 2002. Classification and evolution of P-loop GTPases and related ATPases. J Mol Biol 317:41-72. 20. Lin, F. Y., K. W. Chan, H. C. Wang, W. L. Hsu, and M. L. Wong. 2010. Functional expression of the recombinant ATPase of orf virus. Archives of Virology 155:1701-1705. 21. Lowy, D. R., and B. M. Willumsen. 1993. Function and Regulation of Ras. Annual Review of Biochemistry 62:851-891. 22. Martins, A., C. H. Gross, and S. Shuman. 1999. Mutational analysis of vaccinia virus nucleoside triphosphate phosphohydrolase I, a DNA-dependent ATPase of the DExH box family. Journal of Virology 73:1302-1308. 23. Mercer, A. A., U. A. Norihito, F. B. Sonja-Maria, K. Hofmann, K. M. Fraser, T. Bateman, and S. B. Fleming. 2006. Comparative analysis of genome sequences of three isolates of Orf virus reveals unexpected sequence variation. Virus Research 116:146-158. 24. Murzin, A. G., S. E. Brenner, T. Hubbard, and C. Chothia. 1995. SCOP: a structural classification of proteins database for the investigation of sequences and structures. J Mol Biol 247:536-40. 25. Ostapchuk, P., and P. Hearing. 2008. Adenovirus IVa2 Protein Binds ATP. Journal of Virology 82:10290-10294. 26. Ramadevi, N., and P. Roy. 1998. Bluetongue virus core protein VP4 has nucleoside triphosphate phosphohydrolase activity. J Gen Virol 79 ( Pt 10):2475-80. 27. Russel, M. 1991. Filamentous Phage Assembly. Molecular Microbiology 5:1607-1613. 28. Story, R. M., I. T. Weber, and T. A. Steitz. 1992. The Structure of the Escherichia-Coli Reca Protein Monomer and Polymer. Nature 355:318-325. 29. Su, Y. P., J. H. Shien, H. J. Liu, H. S. Yin, and L. H. Lee. 2007. Avian reovirus core protein muA expressed in Escherichia coli possesses both NTPase and RTPase activities. J Gen Virol 88:1797-805. 30. Teplyakov, A., G. Obmolova, M. Tordova, N. Thanki, N. Bonander, E. Eisenstein, A. J. Howard, and G. L. Gilliland. 2002. Crystal structure of the YjeE protein from Haemophilus influenzae: a putative Atpase involved in cell wall synthesis. Proteins 48:220-6. 31. Valencia, A., P. Chardin, A. Wittinghofer, and C. Sander. 1991. The Ras Protein Family - Evolutionary Tree and Role of Conserved Amino-Acids. Biochemistry 30:4637-4648. 32. Vanderwolk, J. P. W., M. Klose, J. G. Dewit, T. Denblaauwen, R. Freudl, and A. J. M. Driessen. 1995. Identification of the Magnesium-Binding Domain of the High-Affinity Atp Binding-Site of the Bacillus-Subtilis and Escherichia-Coli Seca Protein. Journal of Biological Chemistry 270:18975-18982. 33. Walker, J. E., M. Saraste, M. J. Runswick, and N. J. Gay. 1982. Distantly Related Sequences in the Alpha-Subunits and Beta-Subunits of Atp Synthase, Myosin, Kinases and Other Atp-Requiring Enzymes and a Common Nucleotide Binding Fold. Embo Journal 1:945-951. 34. Wiese, C., J. M. Hinz, R. S. Tebbs, P. B. Nham, S. S. Urbin, D. W. Collins, L. H. Thompson, and D. Schild. 2006. Disparate requirements for the Walker A and B ATPase motifs of human RAD51D in homologous recombination. Nucleic Acids Research 34:2833-2843. 35. Wu, X. Y., A. Kodama, and E. Fuchs. 2008. ACF7 regulates cytoskeletal-focal adhesion dynamics and migration and has ATPase activity. Cell 135:137-148. chapter 4 Cann, A. J. 1999. Virus isolation, p. 33-60. In A. J. cann (ed.), Virus Culture: A Practical Approach, 1 ed. Oxford University Press Inc., New York. 2. Guo, J., J. Rasmussen, A. Wunschmann, and A. de La Concha-Bermejillo. 2004. Genetic characterization of orf viruses isolated from various ruminant species of a zoo. Vet Microbiol 99:81-92. 3. Guo, J., Z. Zhang, J. F. Edwards, R. W. Ermel, C. Taylor, Jr., and A. de la Concha-Bermejillo. 2003. Characterization of a North American orf virus isolated from a goat with persistent, proliferative dermatitis. Virus Res 93:169-79. 4. Kruse, N., and O. Weber. 2001. Selective induction of apoptosis in antigen-presenting cells in mice by Parapoxvirus ovis. J Virol 75:4699-704. 5. Musser, J. M., C. A. Taylor, J. Guo, I. R. Tizard, and J. W. Walker. 2008. Development of a contagious ecthyma vaccine for goats. Am J Vet Res 69:1366-70. 6. Sentsui, H., K. Murakami, Y. Inoshima, T. Shibahara, and Y. Yokomizo. 1999. Isolation of parapoxvirus from a cow treated with interferon-gamma. Vet Microbiol 70:143-52. 7. Suzuki, T., N. Minamoto, M. Sugiyama, T. Kinjo, Y. Suzuki, M. Sugimura, and Y. Atoji. 1993. Isolation and antibody prevalence of a parapoxvirus in wild Japanese serows (Capricornis crispus). J Wildl Dis 29:384-9.
摘要: 羊傳染性化膿性病毒 (orf virus) 主要感染山羊和綿羊,基因體為140 kbp左右的線性雙股去氧核醣核酸。根據氨基酸序列比對,羊傳染性化膿性病毒之A32L基因所轉錄出的蛋白極有可能存有ATP水解的活性。為證明此假說,我們轉接A32L基因到原核表現載體,經轉型到表現宿主後,表現及純化此重組蛋白,並以質譜儀驗證此蛋白。純化後的orf重組蛋白明確顯示出具有ATP水解之特性,且分別在不同的二價離子存在環境下仍具有活性,在不同的pH環境(5.5 - 8.5)下亦仍存有相似的蛋白活性。基於前人研究指出,羊傳染性化膿性病毒的ATP水解蛋白氨基酸序列中,存有四個保留功能區塊 (motif I, II, III, and IV) 及一個AYDG 區塊,此五個功能區塊為蛋白活性所必須。因此,於進一步的實驗中,分別建立可表現五個保留區刪除之A32L蛋白表現載體,同時進行誘導表現、純化與功能分析。實驗結果發現,個別刪除掉I、II、III及IV的保留區塊重組蛋白顯示出具較低的ATP水解活性。其中刪除掉AYDG區塊的重組蛋白具有顯著性的ATP水解活性消退。在同時,亦針對重組蛋白的GTP水解能力進行測試,結果發現orf病毒的ATP水解蛋白除可以水解ATP外亦存有較低的GTP水解能力。為了探討A32L蛋白在病毒複製中所扮演的腳色,先期實驗將進行羊傳染性化膿性病毒的分離,以山羊的初代細胞來分離羊傳染性化膿性病毒,經由不斷的盲目繼代,實驗室成功的分離出太平分離株的羊傳染性化膿性病毒。
Orf virus infects goat and sheep; it has a double-stranded DNA genome of about 140 kbp. According to the similarity of amino acid sequences, we suspected that the A32L gene of orf virus might encode protein with ATPase activity. To address this, the A32L gene was cloned into a prokaryotic expression vector, and the recombinant protein was expressed, purified and identified. The purified recombinant protein did show the ATP hydrolysis function. The ATPase of orf virus was active in the presence of different divalent ions and had similar enzymatic activities in different pH. The viral ATPase contains four functional motifs (motifs I, II, III and IV) and an AYDG motif; they are necessary for ATP hydrolysis reaction. Therefore, recombinant ATPases with deletion of individual motif of the Taiping strain were expressed and purified. It was found that deletions at motifs I, II, III or IV showed lower activity than that of the wild type. Deletion of the AYDG motif significantly decreased the ATPase activity. Moreover, ATPase of orf virus also harbored weaker GTPase activity. For the future study on the role of A32L gene in orf virus replication, goat primary cells were prepared and the orf virus (Taiping strain) was successfully isolated from field orf-infected goats using primary goat testis cells.
URI: http://hdl.handle.net/11455/12951
其他識別: U0005-1901201216125300
文章連結: http://www.airitilibrary.com/Publication/alDetailedMesh1?DocID=U0005-1901201216125300
Appears in Collections:獸醫學系所

文件中的檔案:

取得全文請前往華藝線上圖書館



Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.