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完整後設資料紀錄
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.advisor | 吳漢忠(Han-Chung Wu) | |
dc.contributor.author | Ping-Chang Cheng | en |
dc.contributor.author | 鄭秉昌 | zh_TW |
dc.date.accessioned | 2021-06-08T07:20:53Z | - |
dc.date.copyright | 2008-08-08 | |
dc.date.issued | 2008 | |
dc.date.submitted | 2008-07-24 | |
dc.identifier.citation | Aaskov, J.G., Geysen, H.M., and Mason, T.J. (1989). Serologically defined linear epitopes in the envelope protein of dengue 2 (Jamaica strain 1409). Arch Virol 105, 209-221.
Allison, S.L., Schalich, J., Stiasny, K., Mandl, C.W., and Heinz, F.X. (2001). Mutational evidence for an internal fusion peptide in flavivirus envelope protein E. J Virol 75, 4268-4275. Anderson, R., Wang, S., Osiowy, C., and Issekutz, A.C. (1997). Activation of endothelial cells via antibody-enhanced dengue virus infection of peripheral blood monocytes. J Virol 71, 4226-4232. Avirutnan, P., Malasit, P., Seliger, B., Bhakdi, S., and Husmann, M. (1998). Dengue virus infection of human endothelial cells leads to chemokine production, complement activation, and apoptosis. J Immunol 161, 6338-6346. Azeredo, E.L., De Oliveira-Pinto, L.M., Zagne, S.M., Cerqueira, D.I., Nogueira, R.M., and Kubelka, C.F. (2006). NK cells, displaying early activation, cytotoxicity and adhesion molecules, are associated with mild dengue disease. Clin Exp Immunol 143, 345-356. Balmaseda, A., Hammond, S.N., Perez, L., Tellez, Y., Saborio, S.I., Mercado, J.C., Cuadra, R., Rocha, J., Perez, M.A., Silva, S., et al. (2006). Serotype-specific differences in clinical manifestations of dengue. Am J Trop Med Hyg 74, 449-456. Beasley, D.W., and Barrett, A.D. (2002). Identification of neutralizing epitopes within structural domain III of the West Nile virus envelope protein. J Virol 76, 13097-13100. Braga, E.L., Moura, P., Pinto, L.M., Ignacio, S.R., Oliveira, M.J., Cordeiro, M.T., and Kubelka, C.F. (2001). Detection of circulant tumor necrosis factor-alpha, soluble tumor necrosis factor p75 and interferon-gamma in Brazilian patients with dengue fever and dengue hemorrhagic fever. Mem Inst Oswaldo Cruz 96, 229-232. Chakravarti, A., and Kumaria, R. (2006). Circulating levels of tumour necrosis factor-alpha & interferon-gamma in patients with dengue & dengue haemorrhagic fever during an outbreak. Indian J Med Res 123, 25-30. Chambers, T.J., Hahn, C.S., Galler, R., and Rice, C.M. (1990). Flavivirus genome organization, expression, and replication. Annu Rev Microbiol 44, 649-688. Chambers, T.J., Halevy, M., Nestorowicz, A., Rice, C.M., and Lustig, S. (1998). West Nile virus envelope proteins: nucleotide sequence analysis of strains differing in mouse neuroinvasiveness. J Gen Virol 79 ( Pt 10), 2375-2380. Chareonsirisuthigul, T., Kalayanarooj, S., and Ubol, S. (2007). Dengue virus (DENV) antibody-dependent enhancement of infection upregulates the production of anti-inflammatory cytokines, but suppresses anti-DENV free radical and pro-inflammatory cytokine production, in THP-1 cells. J Gen Virol 88, 365-375. Chen, L.C., Lei, H.Y., Liu, C.C., Shiesh, S.C., Chen, S.H., Liu, H.S., Lin, Y.S., Wang, S.T., Shyu, H.W., and Yeh, T.M. (2006). Correlation of serum levels of macrophage migration inhibitory factor with disease severity and clinical outcome in dengue patients. Am J Trop Med Hyg 74, 142-147. Chen, Y., Maguire, T., Hileman, R.E., Fromm, J.R., Esko, J.D., Linhardt, R.J., and Marks, R.M. (1997). Dengue virus infectivity depends on envelope protein binding to target cell heparan sulfate. Nat Med 3, 866-871. Chen, Y.C., Wang, S.Y., and King, C.C. (1999). Bacterial lipopolysaccharide inhibits dengue virus infection of primary human monocytes/macrophages by blockade of virus entry via a CD14-dependent mechanism. J Virol 73, 2650-2657. Chiu, M.W., and Yang, Y.L. (2003). Blocking the dengue virus 2 infections on BHK-21 cells with purified recombinant dengue virus 2 E protein expressed in Escherichia coli. Biochem Biophys Res Commun 309, 672-678. Clyde, K., Kyle, J.L., and Harris, E. (2006). Recent advances in deciphering viral and host determinants of dengue virus replication and pathogenesis. J Virol 80, 11418-11431. Crabtree, M.B., Kinney, R.M., and Miller, B.R. (2005). Deglycosylation of the NS1 protein of dengue 2 virus, strain 16681: construction and characterization of mutant viruses. Arch Virol 150, 771-786. Crill, W.D., and Roehrig, J.T. (2001). Monoclonal antibodies that bind to domain III of dengue virus E glycoprotein are the most efficient blockers of virus adsorption to Vero cells. J Virol 75, 7769-7773. Cummings, D.A., Schwartz, I.B., Billings, L., Shaw, L.B., and Burke, D.S. (2005). Dynamic effects of antibody-dependent enhancement on the fitness of viruses. Proc Natl Acad Sci U S A 102, 15259-15264. Diamond, M.S., Roberts, T.G., Edgil, D., Lu, B., Ernst, J., and Harris, E. (2000). Modulation of Dengue virus infection in human cells by alpha, beta, and gamma interferons. J Virol 74, 4957-4966. Falconar, A.K. (1999). Identification of an epitope on the dengue virus membrane (M) protein defined by cross-protective monoclonal antibodies: design of an improved epitope sequence based on common determinants present in both envelope (E and M) proteins. Arch Virol 144, 2313-2330. Falconar, A.K. (2007). Antibody responses are generated to immunodominant ELK/KLE-type motifs on the nonstructural-1 glycoprotein during live dengue virus infections in mice and humans: implications for diagnosis, pathogenesis, and vaccine design. Clin Vaccine Immunol 14, 493-504. Falconar, A.K. (2008). Monoclonal antibodies that bind to common epitopes on the dengue virus type 2 nonstructural-1 and envelope glycoproteins display weak neutralizing activity and differentiated responses to virulent strains: implications for pathogenesis and vaccines. Clin Vaccine Immunol 15, 549-561. Falconar, A.K., and Young, P.R. (1991). Production of dimer-specific and dengue virus group cross-reactive mouse monoclonal antibodies to the dengue 2 virus non-structural glycoprotein NS1. J Gen Virol 72 ( Pt 4), 961-965. Goncalvez, A.P., Purcell, R.H., and Lai, C.J. (2004). Epitope determinants of a chimpanzee Fab antibody that efficiently cross-neutralizes dengue type 1 and type 2 viruses map to inside and in close proximity to fusion loop of the dengue type 2 virus envelope glycoprotein. J Virol 78, 12919-12928. Gromowski, G.D., Barrett, N.D., and Barrett, A.D. (2008). Characterization of Dengue Complex-specific Neutralizing Epitopes on the Envelope Protein Domain III of Dengue 2 Virus. J Virol. Gubler, D.J. (1998). Dengue and dengue hemorrhagic fever. Clin Microbiol Rev 11, 480-496. Gubler, D.J. (2002). Epidemic dengue/dengue hemorrhagic fever as a public health, social and economic problem in the 21st century. Trends Microbiol 10, 100-103. Gubler, D.J. (2006). Dengue/dengue haemorrhagic fever: history and current status. Novartis Found Symp 277, 3-16; discussion 16-22, 71-13, 251-253. Halstead, S.B. (1983). Dengue haemorrhagic fever. Trans R Soc Trop Med Hyg 77, 739-740. Halstead, S.B. (1990). Global epidemiology of dengue hemorrhagic fever. Southeast Asian J Trop Med Public Health 21, 636-641. Halstead, S.B. (2003). Neutralization and antibody-dependent enhancement of dengue viruses. Adv Virus Res 60, 421-467. Halstead, S.B., Rojanasuphot, S., and Sangkawibha, N. (1983). Original antigenic sin in dengue. Am J Trop Med Hyg 32, 154-156. Henchal, E.A., Gentry, M.K., McCown, J.M., and Brandt, W.E. (1982). Dengue virus-specific and flavivirus group determinants identified with monoclonal antibodies by indirect immunofluorescence. Am J Trop Med Hyg 31, 830-836. Hiramatsu, K., Tadano, M., Men, R., and Lai, C.J. (1996). Mutational analysis of a neutralization epitope on the dengue type 2 virus (DEN2) envelope protein: monoclonal antibody resistant DEN2/DEN4 chimeras exhibit reduced mouse neurovirulence. Virology 224, 437-445. Ho, L.J., Hung, L.F., Weng, C.Y., Wu, W.L., Chou, P., Lin, Y.L., Chang, D.M., Tai, T.Y., and Lai, J.H. (2005). Dengue virus type 2 antagonizes IFN-alpha but not IFN-gamma antiviral effect via down-regulating Tyk2-STAT signaling in the human dendritic cell. J Immunol 174, 8163-8172. Hober, D., Delannoy, A.S., Benyoucef, S., De Groote, D., and Wattre, P. (1996). High levels of sTNFR p75 and TNF alpha in dengue-infected patients. Microbiol Immunol 40, 569-573. Hsieh, S.C., Liu, I.J., King, C.C., Chang, G.J., and Wang, W.K. (2008). A strong endoplasmic reticulum retention signal in the stem-anchor region of envelope glycoprotein of dengue virus type 2 affects the production of virus-like particles. Virology. Huang, K.J., Yang, Y.C., Lin, Y.S., Huang, J.H., Liu, H.S., Yeh, T.M., Chen, S.H., Liu, C.C., and Lei, H.Y. (2006). The dual-specific binding of dengue virus and target cells for the antibody-dependent enhancement of dengue virus infection. J Immunol 176, 2825-2832. Huang, L., and Shi, Y. (2001). Tissue-type plasminogen activator and plasminogen activator inhibitor type-1 mRNA and their protein expression levels in human decidua after early pregnancy termination by mifepristone plus misoprostol. Chin Med J (Engl) 114, 628-631. Hung, S.L., Lee, P.L., Chen, H.W., Chen, L.K., Kao, C.L., and King, C.C. (1999). Analysis of the steps involved in Dengue virus entry into host cells. Virology 257, 156-167. Innis, B.L., Thirawuth, V., and Hemachudha, C. (1989). Identification of continuous epitopes of the envelope glycoprotein of dengue type 2 virus. Am J Trop Med Hyg 40, 676-687. Jindadamrongwech, S., Thepparit, C., and Smith, D.R. (2004). Identification of GRP 78 (BiP) as a liver cell expressed receptor element for dengue virus serotype 2. Arch Virol 149, 915-927. Kanai, R., Kar, K., Anthony, K., Gould, L.H., Ledizet, M., Fikrig, E., Marasco, W.A., Koski, R.A., and Modis, Y. (2006). Crystal structure of west nile virus envelope glycoprotein reveals viral surface epitopes. J Virol 80, 11000-11008. Kliks, S.C., Nisalak, A., Brandt, W.E., Wahl, L., and Burke, D.S. (1989). Antibody-dependent enhancement of dengue virus growth in human monocytes as a risk factor for dengue hemorrhagic fever. Am J Trop Med Hyg 40, 444-451. Kuhn, R.J., Zhang, W., Rossmann, M.G., Pletnev, S.V., Corver, J., Lenches, E., Jones, C.T., Mukhopadhyay, S., Chipman, P.R., Strauss, E.G., et al. (2002). Structure of dengue virus: implications for flavivirus organization, maturation, and fusion. Cell 108, 717-725. Kurane, I., and Ennis, F.A. (1987). Induction of interferon alpha from human lymphocytes by autologous, dengue virus-infected monocytes. J Exp Med 166, 999-1010. Kurane, I., Innis, B.L., Nimmannitya, S., Nisalak, A., Meager, A., and Ennis, F.A. (1993). High levels of interferon alpha in the sera of children with dengue virus infection. Am J Trop Med Hyg 48, 222-229. Kurane, I., Innis, B.L., Nimmannitya, S., Nisalak, A., Meager, A., Janus, J., and Ennis, F.A. (1991). Activation of T lymphocytes in dengue virus infections. High levels of soluble interleukin 2 receptor, soluble CD4, soluble CD8, interleukin 2, and interferon-gamma in sera of children with dengue. J Clin Invest 88, 1473-1480. Lai, C.Y., Tsai, W.Y., Lin, S.R., Kao, C.L., Hu, H.P., King, C.C., Wu, H.C., Chang, G.J., and Wang, W.K. (2008). Antibodies to envelope glycoprotein of dengue virus during the natural course of infection are predominantly cross-reactive and recognize epitopes containing highly conserved residues at the fusion loop of domain II. J Virol. Laoprasopwattana, K., Libraty, D.H., Endy, T.P., Nisalak, A., Chunsuttiwat, S., Vaughn, D.W., Reed, G., Ennis, F.A., Rothman, A.L., and Green, S. (2005). Dengue Virus (DV) enhancing antibody activity in preillness plasma does not predict subsequent disease severity or viremia in secondary DV infection. J Infect Dis 192, 510-519. Lee, Y.R., Liu, M.T., Lei, H.Y., Liu, C.C., Wu, J.M., Tung, Y.C., Lin, Y.S., Yeh, T.M., Chen, S.H., and Liu, H.S. (2006). MCP-1, a highly expressed chemokine in dengue haemorrhagic fever/dengue shock syndrome patients, may cause permeability change, possibly through reduced tight junctions of vascular endothelium cells. J Gen Virol 87, 3623-3630. Lin, B., Parrish, C.R., Murray, J.M., and Wright, P.J. (1994). Localization of a neutralizing epitope on the envelope protein of dengue virus type 2. Virology 202, 885-890. Lin, C.F., Lei, H.Y., Shiau, A.L., Liu, H.S., Yeh, T.M., Chen, S.H., Liu, C.C., Chiu, S.C., and Lin, Y.S. (2002). Endothelial cell apoptosis induced by antibodies against dengue virus nonstructural protein 1 via production of nitric oxide. J Immunol 169, 657-664. Lin, C.W., and Wu, S.C. (2003). A functional epitope determinant on domain III of the Japanese encephalitis virus envelope protein interacted with neutralizing-antibody combining sites. J Virol 77, 2600-2606. Lin, Y.S., Lin, C.F., Lei, H.Y., Liu, H.S., Yeh, T.M., Chen, S.H., and Liu, C.C. (2004). Antibody-mediated endothelial cell damage via nitric oxide. Curr Pharm Des 10, 213-221. Littaua, R., Kurane, I., and Ennis, F.A. (1990). Human IgG Fc receptor II mediates antibody-dependent enhancement of dengue virus infection. J Immunol 144, 3183-3186. Lok, S.M., Kostyuchenko, V., Nybakken, G.E., Holdaway, H.A., Battisti, A.J., Sukupolvi-Petty, S., Sedlak, D., Fremont, D.H., Chipman, P.R., Roehrig, J.T., et al. (2008). Binding of a neutralizing antibody to dengue virus alters the arrangement of surface glycoproteins. Nat Struct Mol Biol. Lorenz, I.C., Allison, S.L., Heinz, F.X., and Helenius, A. (2002). Folding and dimerization of tick-borne encephalitis virus envelope proteins prM and E in the endoplasmic reticulum. J Virol 76, 5480-5491. Lozach, P.Y., Burleigh, L., Staropoli, I., Navarro-Sanchez, E., Harriague, J., Virelizier, J.L., Rey, F.A., Despres, P., Arenzana-Seisdedos, F., and Amara, A. (2005). Dendritic cell-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN)-mediated enhancement of dengue virus infection is independent of DC-SIGN internalization signals. J Biol Chem 280, 23698-23708. Mady, B.J., Erbe, D.V., Kurane, I., Fanger, M.W., and Ennis, F.A. (1991). Antibody-dependent enhancement of dengue virus infection mediated by bispecific antibodies against cell surface molecules other than Fc gamma receptors. J Immunol 147, 3139-3144. Mady, B.J., Kurane, I., Erbe, D.V., Fanger, M.W., and Ennis, F.A. (1993). Neuraminidase augments Fc gamma receptor II-mediated antibody-dependent enhancement of dengue virus infection. J Gen Virol 74 ( Pt 5), 839-844. Medin, C.L., Fitzgerald, K.A., and Rothman, A.L. (2005). Dengue virus nonstructural protein NS5 induces interleukin-8 transcription and secretion. J Virol 79, 11053-11061. Megret, F., Hugnot, J.P., Falconar, A., Gentry, M.K., Morens, D.M., Murray, J.M., Schlesinger, J.J., Wright, P.J., Young, P., Van Regenmortel, M.H., et al. (1992). Use of recombinant fusion proteins and monoclonal antibodies to define linear and discontinuous antigenic sites on the dengue virus envelope glycoprotein. Virology 187, 480-491. Messer, W.B., Gubler, D.J., Harris, E., Sivananthan, K., and de Silva, A.M. (2003). Emergence and global spread of a dengue serotype 3, subtype III virus. Emerg Infect Dis 9, 800-809. Modis, Y., Ogata, S., Clements, D., and Harrison, S.C. (2003). A ligand-binding pocket in the dengue virus envelope glycoprotein. Proc Natl Acad Sci U S A 100, 6986-6991. Monath, T.P. (1994). Dengue: the risk to developed and developing countries. Proc Natl Acad Sci U S A 91, 2395-2400. Mongkolsapaya, J., Duangchinda, T., Dejnirattisai, W., Vasanawathana, S., Avirutnan, P., Jairungsri, A., Khemnu, N., Tangthawornchaikul, N., Chotiyarnwong, P., Sae-Jang, K., et al. (2006). T cell responses in dengue hemorrhagic fever: are cross-reactive T cells suboptimal? J Immunol 176, 3821-3829. Mukhopadhyay, S., Kim, B.S., Chipman, P.R., Rossmann, M.G., and Kuhn, R.J. (2003). Structure of West Nile virus. Science 302, 248. Navarro-Sanchez, E., Altmeyer, R., Amara, A., Schwartz, O., Fieschi, F., Virelizier, J.L., Arenzana-Seisdedos, F., and Despres, P. (2003). Dendritic-cell-specific ICAM3-grabbing non-integrin is essential for the productive infection of human dendritic cells by mosquito-cell-derived dengue viruses. EMBO Rep 4, 723-728. Neves-Souza, P.C., Azeredo, E.L., Zagne, S.M., Valls-de-Souza, R., Reis, S.R., Cerqueira, D.I., Nogueira, R.M., and Kubelka, C.F. (2005). Inducible nitric oxide synthase (iNOS) expression in monocytes during acute Dengue Fever in patients and during in vitro infection. BMC Infect Dis 5, 64. Oliphant, T., Engle, M., Nybakken, G.E., Doane, C., Johnson, S., Huang, L., Gorlatov, S., Mehlhop, E., Marri, A., Chung, K.M., et al. (2005). Development of a humanized monoclonal antibody with therapeutic potential against West Nile virus. Nat Med 11, 522-530. Oliphant, T., Nybakken, G.E., Engle, M., Xu, Q., Nelson, C.A., Sukupolvi-Petty, S., Marri, A., Lachmi, B.E., Olshevsky, U., Fremont, D.H., et al. (2006). Antibody recognition and neutralization determinants on domains I and II of West Nile Virus envelope protein. J Virol 80, 12149-12159. Palmer, C.J., King, S.D., Cuadrado, R.R., Perez, E., Baum, M., and Ager, A.L. (1999). Evaluation of the MRL diagnostics dengue fever virus IgM capture ELISA and the PanBio Rapid Immunochromatographic Test for diagnosis of dengue fever in Jamaica. J Clin Microbiol 37, 1600-1601. Pierson, T.C., and Diamond, M.S. (2008). Molecular mechanisms of antibody-mediated neutralisation of flavivirus infection. Expert Rev Mol Med 10, e12. Pincus, S., Mason, P.W., Konishi, E., Fonseca, B.A., Shope, R.E., Rice, C.M., and Paoletti, E. (1992). Recombinant vaccinia virus producing the prM and E proteins of yellow fever virus protects mice from lethal yellow fever encephalitis. Virology 187, 290-297. Pokidysheva, E., Zhang, Y., Battisti, A.J., Bator-Kelly, C.M., Chipman, P.R., Xiao, C., Gregorio, G.G., Hendrickson, W.A., Kuhn, R.J., and Rossmann, M.G. (2006). Cryo-EM reconstruction of dengue virus in complex with the carbohydrate recognition domain of DC-SIGN. Cell 124, 485-493. Restrepo, B.N., Isaza, D.M., Salazar, C.L., Ramirez, R., Ospina, M., and Alvarez, L.G. (2008). Serum levels of interleukin-6, tumor necrosis factor-alpha and interferon-gama in infants with and without dengue. Rev Soc Bras Med Trop 41, 6-10. Rey, F.A., Heinz, F.X., Mandl, C., Kunz, C., and Harrison, S.C. (1995). The envelope glycoprotein from tick-borne encephalitis virus at 2 A resolution. Nature 375, 291-298. Reyes-Del Valle, J., Chavez-Salinas, S., Medina, F., and Del Angel, R.M. (2005). Heat shock protein 90 and heat shock protein 70 are components of dengue virus receptor complex in human cells. J Virol 79, 4557-4567. Rico-Hesse, R., Harrison, L.M., Salas, R.A., Tovar, D., Nisalak, A., Ramos, C., Boshell, J., de Mesa, M.T., Nogueira, R.M., and da Rosa, A.T. (1997). Origins of dengue type 2 viruses associated with increased pathogenicity in the Americas. Virology 230, 244-251. Roehrig, J.T. (2003). Antigenic structure of flavivirus proteins. Adv Virus Res 59, 141-175. Roehrig, J.T., Bolin, R.A., and Kelly, R.G. (1998). Monoclonal antibody mapping of the envelope glycoprotein of the dengue 2 virus, Jamaica. Virology 246, 317-328. Roehrig, J.T., Johnson, A.J., Hunt, A.R., Bolin, R.A., and Chu, M.C. (1990). Antibodies to dengue 2 virus E-glycoprotein synthetic peptides identify antigenic conformation. Virology 177, 668-675. Sanchez, M.D., Pierson, T.C., McAllister, D., Hanna, S.L., Puffer, B.A., Valentine, L.E., Murtadha, M.M., Hoxie, J.A., and Doms, R.W. (2005). Characterization of neutralizing antibodies to West Nile virus. Virology 336, 70-82. Sangkawibha, N., Rojanasuphot, S., Ahandrik, S., Viriyapongse, S., Jatanasen, S., Salitul, V., Phanthumachinda, B., and Halstead, S.B. (1984). Risk factors in dengue shock syndrome: a prospective epidemiologic study in Rayong, Thailand. I. The 1980 outbreak. Am J Epidemiol 120, 653-669. Serafin, I.L., and Aaskov, J.G. (2001). Identification of epitopes on the envelope (E) protein of dengue 2 and dengue 3 viruses using monoclonal antibodies. Arch Virol 146, 2469-2479. Stiasny, K., Kiermayr, S., Holzmann, H., and Heinz, F.X. (2006). Cryptic properties of a cluster of dominant flavivirus cross-reactive antigenic sites. J Virol 80, 9557-9568. Takhampunya, R., Padmanabhan, R., and Ubol, S. (2006). Antiviral action of nitric oxide on dengue virus type 2 replication. J Gen Virol 87, 3003-3011. Talavera, D., Castillo, A.M., Dominguez, M.C., Gutierrez, A.E., and Meza, I. (2004). IL8 release, tight junction and cytoskeleton dynamic reorganization conducive to permeability increase are induced by dengue virus infection of microvascular endothelial monolayers. J Gen Virol 85, 1801-1813. Thein, S., Aung, M.M., Shwe, T.N., Aye, M., Zaw, A., Aye, K., Aye, K.M., and Aaskov, J. (1997). Risk factors in dengue shock syndrome. Am J Trop Med Hyg 56, 566-572. Thepparit, C., and Smith, D.R. (2004). Serotype-specific entry of dengue virus into liver cells: identification of the 37-kilodalton/67-kilodalton high-affinity laminin receptor as a dengue virus serotype 1 receptor. J Virol 78, 12647-12656. Trainor, N.B., Crill, W.D., Roberson, J.A., and Chang, G.J. (2007). Mutation analysis of the fusion domain region of St. Louis encephalitis virus envelope protein. Virology 360, 398-406. Trirawatanapong, T., Chandran, B., Putnak, R., and Padmanabhan, R. (1992). Mapping of a region of dengue virus type-2 glycoprotein required for binding by a neutralizing monoclonal antibody. Gene 116, 139-150. Vazquez, S., Guzman, M.G., Guillen, G., Chinea, G., Perez, A.B., Pupo, M., Rodriguez, R., Reyes, O., Garay, H.E., Delgado, I., et al. (2002). Immune response to synthetic peptides of dengue prM protein. Vaccine 20, 1823-1830. Zhang, W., Chipman, P.R., Corver, J., Johnson, P.R., Zhang, Y., Mukhopadhyay, S., Baker, T.S., Strauss, J.H., Rossmann, M.G., and Kuhn, R.J. (2003). Visualization of membrane protein domains by cryo-electron microscopy of dengue virus. Nat Struct Biol 10, 907-912. Zhang, Y., Zhang, W., Ogata, S., Clements, D., Strauss, J.H., Baker, T.S., Kuhn, R.J., and Rossmann, M.G. (2004). Conformational changes of the flavivirus E glycoprotein. Structure 12, 1607-1618. Zhang, Z.S., Yan, Y.S., Weng, Y.W., Huang, H.L., Li, S.Q., He, S., and Zhang, J.M. (2007). High-level expression of recombinant dengue virus type 2 envelope domain III protein and induction of neutralizing antibodies in BALB/C mice. J Virol Methods 143, 125-131. | |
dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/26687 | - |
dc.description.abstract | 引起登革熱、登革出血熱、登革休克症候群的登革病毒為斑蚊所媒介傳染的人類病原體,此病毒在分類上具有四種血清並且盛行於熱帶和亞熱帶地區。全球每年粗估約有五千萬到一億的感染案例,其中約百分之ㄧ的病人甚至會再進一步惡化成登革出血熱的症狀。登革病毒之套膜蛋白是參與並且誘發宿主免疫反應的重要抗原,而且此蛋白對於病毒自身和宿主進行膜融合以及細胞表面受體的辨認扮演重要角色。套膜蛋白之膜外區域可以再進一步區分為三個功能區塊:區塊一、區塊二、區塊三。根據過往及我們實驗室關於抗原決定位的研究指出,若干能對抗黃病毒家族之專一暨中和性抗體大多數偏好辨認套膜蛋白上的區塊三,而此區塊的胺基酸替換會造成這類單株抗體失去了結合能力;除此之外,對於那些中和能力稍弱並且對於其他種類黃病毒有交叉反應的單株抗體則多會結合到套膜蛋白的區塊二。另一方面,許多過往研究也指出人類宿主血清裡倘若有弱中和性的抗體之存在似乎會惡化二次感染之登革熱病人其病情,此種機制已被稱為「抗體依賴性免疫加強反應」假說。
然而對於登革病毒套膜蛋白上之功能區塊在病理發生機制所扮演的角色仍然未被清楚定位。因此我們篩選了若干株由我們實驗室所生產的抗體並藉此來釐清功能區塊和中和性抗體之間的交互作用以冀望最終能改善未來對於此疾病之預防及治療方法。在本篇研究中,我們利用了酵素聯結免疫吸附測試、西方墨點法、套膜蛋白質表現、定量式反轉錄聚合酶連鎖反應等方法來分析弱中和性、叉反應性和專一暨中和性單株抗體與其所辨認的功能區塊之關聯性。此外,我們發現偏好辨認區塊三的抗體常對於登革病毒會具備強中和能力,而偏好辨認區塊一和區塊二的抗體則具弱中和能力或是不具有中和能力,更甚者還提高了病毒對於宿主的感染率。 | zh_TW |
dc.description.abstract | Dengue virus (DEN), the human pathogen leading to dengue fever (DF), is epidemic in tropical and subtropical areas around the world. The DEN envelope protein (E), the primary viral protein inducing protective immunity, is critical for membrane fusion and mediates binding to cellular receptors. The ectodomain of the E monomer could further be divided into three domains assigned to domain I, domain II and domain III (EDI, EDII, and EDIII) (Modis et al., 2003). According to previous and our laboratory’s epitope mapping studies, many type-specific neutralizing antibodies against individual flaviviruses were localized to EDIII and alteration of specific residues in EDIII contributed to the loss of binding of neutralizing monoclonal antibodies (MAbs). Furthermore, subneutralizing MAbs that cross-react with other flaviviruses mainly bound to EDI-II. On the other hand, the presence of subneutralizing DEN cross-reactive serum antibodies in human hosts seems to cause an increase in the severity of secondary DEN infections via antibody-dependent enhancement (ADE).
The roles of B-cell epitopes on the EDs in DEN pathogenesis, however, are still blurred. Accordingly, we screened a panel of MAbs from our laboratory to define the interaction between EDs and cross-reactive and neutralizing MAbs. Identification of neutralizing and pathologic epitopes will be useful for improving therapeutics to these diseases. In this study, we identified a number of cross-reactive and type-specific MAbs with their recognized EDs through ELISA, western blot analysis and quantitative real-time PCR (QRT-PCR). Additionally, we found that MAbs which recognized EDIII usually displayed strong neutralizing activity while MAbs which bound to EDI-II were likely to cause sub-/non-neutralizing or enhancing effects on DEN infections frequently. | en |
dc.description.provenance | Made available in DSpace on 2021-06-08T07:20:53Z (GMT). No. of bitstreams: 1 ntu-97-R95444002-1.pdf: 2900123 bytes, checksum: b709f9f43020926a6bd40042be09d1a7 (MD5) Previous issue date: 2008 | en |
dc.description.tableofcontents | Ackowledgements……………………………………………1
中文摘要 ……………………………………………………3 Abstract ……………………………………………………4 Introduction……………………………………………………6 Materials and Methods…………………………………………18 Results ……………………………………………………24 Discussion……………………………………………………29 Figures ……………………………………………………35 Tables ……………………………………………………48 References……………………………………………………53 Appendixes……………………………………………………64 | |
dc.language.iso | en | |
dc.title | 登革病毒單株抗體其B細胞抗原決定位之研究 | zh_TW |
dc.title | Identification of B-cell Epitopes for Monoclonal
Antibodies against Dengue Virus | en |
dc.type | Thesis | |
dc.date.schoolyear | 96-2 | |
dc.description.degree | 碩士 | |
dc.contributor.oralexamcommittee | 林欽塘(Chin-Tarng Lin),林中梧(Chung-Wu Lin) | |
dc.subject.keyword | 登革病毒,套膜蛋白,單株抗體,B細胞抗原決定位, | zh_TW |
dc.subject.keyword | dengue virus,envelope protein,monoclonal antibody (MAb),B-cell epitope, | en |
dc.relation.page | 66 | |
dc.rights.note | 未授權 | |
dc.date.accepted | 2008-07-25 | |
dc.contributor.author-college | 醫學院 | zh_TW |
dc.contributor.author-dept | 病理學研究所 | zh_TW |
顯示於系所單位: | 病理學科所 |
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