메뉴 건너뛰기




Volumn 84, Issue 14, 2010, Pages 6923-6934

Redirecting lentiviral vectors pseudotyped with Sindbis virus-derived envelope proteins to DC-SIGN by modification of N-linked glycans of envelope proteins

Author keywords

[No Author keywords available]

Indexed keywords

1 DEOXYMANNONOJIRIMYCIN; ENVELOPE PROTEIN; GLYCAN; LENTIVIRUS VECTOR; MANNOSE;

EID: 77953781716     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00435-10     Document Type: Article
Times cited : (41)

References (94)
  • 1
    • 0036278649 scopus 로고    scopus 로고
    • C-type lectins DC-SIGN and L-SIGN mediate cellular entry by Ebola virus in cis and in
    • Alvarez, C. P., F. Lasala, J. Carrillo, O. Muniz, A. L. Corbi, and R. Delgado. 2002. C-type lectins DC-SIGN and L-SIGN mediate cellular entry by Ebola virus in cis and in trans. J. Virol. 76:6841-6844.
    • (2002) Trans. J. Virol. , vol.76 , pp. 6841-6844
    • Alvarez, C.P.1    Lasala, F.2    Carrillo, J.3    Muniz, O.4    Corbi, A.L.5    Delgado, R.6
  • 2
    • 0034919136 scopus 로고    scopus 로고
    • Lentivirus vectors encoding both central polypurine tract and posttranscriptional regulatory element provide enhanced transduction and transgene expression
    • Barry, S. C., B. Harder, M. Brzezinski, L. Y. Flint, J. Seppen, and W. R. Osborne. 2001. Lentivirus vectors encoding both central polypurine tract and posttranscriptional regulatory element provide enhanced transduction and transgene expression. Hum. Gene Ther. 12:1103-1108.
    • (2001) Hum. Gene Ther. , vol.12 , pp. 1103-1108
    • Barry, S.C.1    Harder, B.2    Brzezinski, M.3    Flint, L.Y.4    Seppen, J.5    Osborne, W.R.6
  • 4
    • 0033779574 scopus 로고    scopus 로고
    • Multiple blocks to human immunodeficiency virus type 1 replication in rodent cells
    • Bieniasz, P. D., and B. R. Cullen. 2000. Multiple blocks to human immunodeficiency virus type 1 replication in rodent cells. J. Virol. 74:9868-9877.
    • (2000) J. Virol. , vol.74 , pp. 9868-9877
    • Bieniasz, P.D.1    Cullen, B.R.2
  • 7
    • 33947583453 scopus 로고    scopus 로고
    • In vivo administration of lentiviral vectors triggers a type I interferon response that restricts hepatocyte gene transfer and promotes vector clearance
    • Brown, B. D., G. Sitia, A. Annoni, E. Hauben, L. S. Sergi, A. Zingale, M. G. Roncarolo, L. G. Guidotti, and L. Naldini. 2007. In vivo administration of lentiviral vectors triggers a type I interferon response that restricts hepatocyte gene transfer and promotes vector clearance. Blood 109:2797-2805.
    • (2007) Blood , vol.109 , pp. 2797-2805
    • Brown, B.D.1    Sitia, G.2    Annoni, A.3    Hauben, E.4    Sergi, L.S.5    Zingale, A.6    Roncarolo, M.G.7    Guidotti, L.G.8    Naldini, L.9
  • 8
    • 33646564701 scopus 로고    scopus 로고
    • Endogenous microRNA regulation suppresses transgene expression in hematopoietic lineages and enables stable gene transfer
    • Brown, B. D., M. A. Venneri, A. Zingale, L. Sergi Sergi, and L. Naldini. 2006. Endogenous microRNA regulation suppresses transgene expression in hematopoietic lineages and enables stable gene transfer. Nat. Med. 12:585-591.
    • (2006) Nat. Med. , vol.12 , pp. 585-591
    • Brown, B.D.1    Venneri, M.A.2    Zingale, A.3    Sergi Sergi, L.4    Naldini, L.5
  • 9
    • 0018411985 scopus 로고
    • Carbohydrate structure of Sindbis virus glycoprotein E2 from virus grown in hamster and chicken cells
    • Burke, D., and K. Keegstra. 1979. Carbohydrate structure of Sindbis virus glycoprotein E2 from virus grown in hamster and chicken cells. J. Virol. 29:546-554. (Pubitemid 9098426)
    • (1979) Journal of Virology , vol.29 , Issue.2 , pp. 546-554
    • Burke, D.1    Keegstra, K.2
  • 10
    • 0031849754 scopus 로고    scopus 로고
    • Binding of Sindbis virus to cell surface heparan sulfate
    • Byrnes, A. P., and D. E. Griffin. 1998. Binding of Sindbis virus to cell surface heparan sulfate. J. Virol. 72:7349-7356. (Pubitemid 28377866)
    • (1998) Journal of Virology , vol.72 , Issue.9 , pp. 7349-7356
    • Byrnes, A.P.1    Griffin, D.E.2
  • 13
    • 0028501228 scopus 로고
    • Cell targeting with retroviral vector particles containing antibody-envelope fusion proteins
    • Chu, T. H., I. Martinez, W. C. Sheay, and R. Dornburg. 1994. Cell targeting with retroviral vector particles containing antibody-envelope fusion proteins. Gene Ther. 1:292-299. (Pubitemid 2133698)
    • (1994) Gene Therapy , vol.1 , Issue.5 , pp. 292-299
    • Chu Te Hua, T.1    Martinez, I.2    Sheay, W.C.3    Dornburg, R.4
  • 14
    • 0037079725 scopus 로고    scopus 로고
    • Targeting transgene expression to antigen-presenting cells derived from lentivirus-transduced engrafting human hematopoietic stem/progenitor cells
    • Cui, Y., J. Golob, E. Kelleher, Z. Ye, D. Pardoll, and L. Cheng. 2002. Targeting transgene expression to antigen-presenting cells derived from lentivirus-transduced engrafting human hematopoietic stem/progenitor cells. Blood 99:399-408.
    • (2002) Blood , vol.99 , pp. 399-408
    • Cui, Y.1    Golob, J.2    Kelleher, E.3    Ye, Z.4    Pardoll, D.5    Cheng, L.6
  • 15
    • 31144445030 scopus 로고    scopus 로고
    • West Nile virus discriminates between DC-SIGN and DC-SIGNR for cellular attachment and infection
    • Davis, C. W., H. Y. Nguyen, S. L. Hanna, M. D. Sanchez, R. W. Doms, and T. C. Pierson. 2006. West Nile virus discriminates between DC-SIGN and DC-SIGNR for cellular attachment and infection. J. Virol. 80:1290-1301.
    • (2006) J. Virol. , vol.80 , pp. 1290-1301
    • Davis, C.W.1    Nguyen, H.Y.2    Hanna, S.L.3    Sanchez, M.D.4    Doms, R.W.5    Pierson, T.C.6
  • 16
    • 54449089926 scopus 로고    scopus 로고
    • Dendritic cells mediate herpes simplex virus infection and transmission through the C-type lectin DC-SIGN
    • de Jong, M. A., L. de Witte, A. Bolmstedt, Y. van Kooyk, and T. B. Geijtenbeek. 2008. Dendritic cells mediate herpes simplex virus infection and transmission through the C-type lectin DC-SIGN. J. Gen. Virol. 89:2398-2409.
    • (2008) J. Gen. Virol. , vol.89 , pp. 2398-2409
    • De Jong, M.A.1    De Witte, L.2    Bolmstedt, A.3    Van Kooyk, Y.4    Geijtenbeek, T.B.5
  • 20
    • 58149311504 scopus 로고    scopus 로고
    • Lentiviral-mediated transcriptional targeting of dendritic cells for induction of T cell tolerance in vivo
    • Dresch, C., S. L. Edelmann, P. Marconi, and T. Brocker. 2008. Lentiviral-mediated transcriptional targeting of dendritic cells for induction of T cell tolerance in vivo. J. Immunol. 181:4495-4506.
    • (2008) J. Immunol. , vol.181 , pp. 4495-4506
    • Dresch, C.1    Edelmann, S.L.2    Marconi, P.3    Brocker, T.4
  • 22
    • 33947493929 scopus 로고    scopus 로고
    • Multiple modes of binding enhance the affinity of DC-SIGN for high mannose N-linked glycans found on viral glycoproteins
    • Feinberg, H., R. Castelli, K. Drickamer, P. H. Seeberger, and W. I. Weis. 2007. Multiple modes of binding enhance the affinity of DC-SIGN for high mannose N-linked glycans found on viral glycoproteins. J. Biol. Chem. 282:4202-4209.
    • (2007) J. Biol. Chem. , vol.282 , pp. 4202-4209
    • Feinberg, H.1    Castelli, R.2    Drickamer, K.3    Seeberger, P.H.4    Weis, W.I.5
  • 23
    • 0035824446 scopus 로고    scopus 로고
    • Structural basis for selective recognition of oligosaccharides by DC-SIGN and DCSIGNR
    • Feinberg, H., D. A. Mitchell, K. Drickamer, and W. I. Weis. 2001. Structural basis for selective recognition of oligosaccharides by DC-SIGN and DCSIGNR. Science 294:2163-2166.
    • (2001) Science , vol.294 , pp. 2163-2166
    • Feinberg, H.1    Mitchell, D.A.2    Drickamer, K.3    Weis, W.I.4
  • 24
    • 0032191166 scopus 로고    scopus 로고
    • The serum mannose-binding protein and the macrophage mannose receptor are pattern recognition molecules that link innate and adaptive immunity
    • Fraser, I. P., H. Koziel, and R. A. Ezekowitz. 1998. The serum mannose-binding protein and the macrophage mannose receptor are pattern recognition molecules that link innate and adaptive immunity. Semin. Immunol. 10:363-372.
    • (1998) Semin. Immunol. , vol.10 , pp. 363-372
    • Fraser, I.P.1    Koziel, H.2    Ezekowitz, R.A.3
  • 25
    • 0021281941 scopus 로고
    • Novel mannosidase inhibitor blocking conversion of high mannose to complex oligosaccharides
    • Fuhrmann, U., E. Bause, G. Legler, and H. Ploegh. 1984. Novel mannosidase inhibitor blocking conversion of high mannose to complex oligosaccharides. Nature 307:755-758.
    • (1984) Nature , vol.307 , pp. 755-758
    • Fuhrmann, U.1    Bause, E.2    Legler, G.3    Ploegh, H.4
  • 30
    • 0034598934 scopus 로고    scopus 로고
    • Identification of DC-SIGN, a novel dendritic cell-specific ICAM-3 receptor that supports primary immune responses
    • Geijtenbeek, T. B., R. Torensma, S. J. van Vliet, G. C. van Duijnhoven, G. J. Adema, Y. van Kooyk, and C. G. Figdor. 2000. Identification of DC-SIGN, a novel dendritic cell-specific ICAM-3 receptor that supports primary immune responses. Cell 100:575-585.
    • (2000) Cell , vol.100 , pp. 575-585
    • Geijtenbeek, T.B.1    Torensma, R.2    Van Vliet, S.J.3    Van Duijnhoven, G.C.4    Adema, G.J.5    Van Kooyk, Y.6    Figdor, C.G.7
  • 31
    • 0032169169 scopus 로고    scopus 로고
    • The role of low pH and disulfide shuffling in the entry and fusion of Semliki Forest virus and Sindbis virus
    • Glomb-Reinmund, S., and M. Kielian. 1998. The role of low pH and disulfide shuffling in the entry and fusion of Semliki Forest virus and Sindbis virus. Virology 248:372-381.
    • (1998) Virology , vol.248 , pp. 372-381
    • Glomb-Reinmund, S.1    Kielian, M.2
  • 32
    • 34248544993 scopus 로고    scopus 로고
    • C-type lectin DC-SIGN modulates Toll-like receptor signaling via Raf-1 kinase-dependent acetylation of transcription factor NF-kappaB
    • Gringhuis, S. I., J. den Dunnen, M. Litjens, B. van Het Hof, Y. van Kooyk, and T. B. Geijtenbeek. 2007. C-type lectin DC-SIGN modulates Toll-like receptor signaling via Raf-1 kinase-dependent acetylation of transcription factor NF-kappaB. Immunity 26:605-616.
    • (2007) Immunity , vol.26 , pp. 605-616
    • Gringhuis, S.I.1    Den Dunnen, J.2    Litjens, M.3    Van Het Hof, B.4    Van Kooyk, Y.5    Geijtenbeek, T.B.6
  • 34
    • 14844359815 scopus 로고    scopus 로고
    • Baculovirus GP64-pseudotyped HIV-based lentivirus vectors are stabilized against complement inactivation by codisplay of decay accelerating factor (DAF) or of a GP64-DAF fusion protein
    • Guibinga, G. H., and T. Friedmann. 2005. Baculovirus GP64-pseudotyped HIV-based lentivirus vectors are stabilized against complement inactivation by codisplay of decay accelerating factor (DAF) or of a GP64-DAF fusion protein. Mol. Ther. 11:645-651.
    • (2005) Mol. Ther. , vol.11 , pp. 645-651
    • Guibinga, G.H.1    Friedmann, T.2
  • 35
    • 70349332794 scopus 로고    scopus 로고
    • N-linked glycans on dengue viruses grown in mammalian and insect cells
    • Hacker, K., L. White, and A. M. de Silva. 2009. N-linked glycans on dengue viruses grown in mammalian and insect cells. J. Gen. Virol. 90:2097-2106.
    • (2009) J. Gen. Virol. , vol.90 , pp. 2097-2106
    • Hacker, K.1    White, L.2    De Silva, A.M.3
  • 37
    • 35348882155 scopus 로고    scopus 로고
    • Lentivirus as a potent and mechanistically distinct vector for genetic immunization
    • He, Y., and L. D. Falo, Jr. 2007. Lentivirus as a potent and mechanistically distinct vector for genetic immunization. Curr. Opin. Mol. Ther. 9:439-446.
    • (2007) Curr. Opin. Mol. Ther. , vol.9 , pp. 439-446
    • He, Y.1    Falo Jr., L.D.2
  • 39
    • 0021770329 scopus 로고
    • Regulation of asparagine-linked oligosaccharide processing. Oligosaccharide processing in Aedes albopictus mosquito cells
    • Hsieh, P., and P. W. Robbins. 1984. Regulation of asparagine-linked oligosaccharide processing. Oligosaccharide processing in Aedes albopictus mosquito cells. J. Biol. Chem. 259:2375-2382.
    • (1984) J. Biol. Chem. , vol.259 , pp. 2375-2382
    • Hsieh, P.1    Robbins, P.W.2
  • 40
    • 0024202766 scopus 로고
    • Regulation of glycosylation. The influence of protein structure on N-linked oligosaccharide processing
    • Hubbard, S. C. 1988. Regulation of glycosylation. The influence of protein structure on N-linked oligosaccharide processing. J. Biol. Chem. 263:19303-19317.
    • (1988) J. Biol. Chem. , vol.263 , pp. 19303-19317
    • Hubbard, S.C.1
  • 41
    • 5444248711 scopus 로고    scopus 로고
    • Mannose binding lectin (MBL) and HIV
    • Ji, X., H. Gewurz, and G. T. Spear. 2005. Mannose binding lectin (MBL) and HIV. Mol. Immunol. 42:145-152.
    • (2005) Mol. Immunol. , vol.42 , pp. 145-152
    • Ji, X.1    Gewurz, H.2    Spear, G.T.3
  • 42
    • 23844550737 scopus 로고    scopus 로고
    • Mannose-binding lectin binds to Ebola and Marburg envelope glycoproteins, resulting in blocking of virus interaction with DC-SIGN and complement-mediated virus neutralization
    • Ji, X., G. G. Olinger, S. Aris, Y. Chen, H. Gewurz, and G. T. Spear. 2005. Mannose-binding lectin binds to Ebola and Marburg envelope glycoproteins, resulting in blocking of virus interaction with DC-SIGN and complement-mediated virus neutralization. J. Gen. Virol. 86:2535-2542.
    • (2005) J. Gen. Virol. , vol.86 , pp. 2535-2542
    • Ji, X.1    Olinger, G.G.2    Aris, S.3    Chen, Y.4    Gewurz, H.5    Spear, G.T.6
  • 43
    • 0028567517 scopus 로고
    • Tissue-specific targeting of retroviral vectors through ligand-receptor interactions
    • Kasahara, N., A. M. Dozy, and Y. W. Kan. 1994. Tissue-specific targeting of retroviral vectors through ligand-receptor interactions. Science 266:1373-1376.
    • (1994) Science , vol.266 , pp. 1373-1376
    • Kasahara, N.1    Dozy, A.M.2    Kan, Y.W.3
  • 44
    • 0029917705 scopus 로고    scopus 로고
    • Human CD14 leukocytes acquire the phenotype and function of antigen-presenting dendritic cells when cultured in GM-CSF and IL-4
    • Kiertscher, S. M., and M. D. Roth. 1996. Human CD14 leukocytes acquire the phenotype and function of antigen-presenting dendritic cells when cultured in GM-CSF and IL-4. J. Leukoc. Biol. 59:208-218.
    • (1996) J. Leukoc. Biol. , vol.59 , pp. 208-218
    • Kiertscher, S.M.1    Roth, M.D.2
  • 46
    • 0032775770 scopus 로고    scopus 로고
    • The furin protease cleavage recognition sequence of Sindbis virus PE2 can mediate virion attachment to cell surface heparan sulfate
    • Klimstra, W. B., H. W. Heidner, and R. E. Johnston. 1999. The furin protease cleavage recognition sequence of Sindbis virus PE2 can mediate virion attachment to cell surface heparan sulfate. J. Virol. 73:6299-6306.
    • (1999) J. Virol. , vol.73 , pp. 6299-6306
    • Klimstra, W.B.1    Heidner, H.W.2    Johnston, R.E.3
  • 47
    • 0242363253 scopus 로고    scopus 로고
    • DC-SIGN and L-SIGN can act as attachment receptors for alphaviruses and distinguish between mosquito cell- And mammalian cell-derived viruses
    • Klimstra, W. B., E. M. Nangle, M. S. Smith, A. D. Yurochko, and K. D. Ryman. 2003. DC-SIGN and L-SIGN can act as attachment receptors for alphaviruses and distinguish between mosquito cell- and mammalian cell-derived viruses. J. Virol. 77:12022-12032.
    • (2003) J. Virol. , vol.77 , pp. 12022-12032
    • Klimstra, W.B.1    Nangle, E.M.2    Smith, M.S.3    Yurochko, A.D.4    Ryman, K.D.5
  • 48
    • 66149114468 scopus 로고    scopus 로고
    • Role of N-linked glycosylation for Sindbis virus infection and replication in vertebrate and invertebrate systems
    • Knight, R. L., K. L. Schultz, R. J. Kent, M. Venkatesan, and D. E. Griffin. 2009. Role of N-linked glycosylation for Sindbis virus infection and replication in vertebrate and invertebrate systems. J. Virol. 83:5640-5647.
    • (2009) J. Virol. , vol.83 , pp. 5640-5647
    • Knight, R.L.1    Schultz, K.L.2    Kent, R.J.3    Venkatesan, M.4    Griffin, D.E.5
  • 49
    • 27644532332 scopus 로고    scopus 로고
    • Specific ICAM-3 grabbing nonintegrin-related 1 (SIGNR1) expressed by marginal zone macrophages is essential for defense against pulmonary Streptococcus pneumoniae infection
    • Koppel, E. A., C. W. Wieland, V. C. van den Berg, M. Litjens, S. Florquin, Y. van Kooyk, T. van der Poll, and T. B. Geijtenbeek. 2005. Specific ICAM-3 grabbing nonintegrin-related 1 (SIGNR1) expressed by marginal zone macrophages is essential for defense against pulmonary Streptococcus pneumoniae infection. Eur. J. Immunol. 35:2962-2969.
    • (2005) Eur. J. Immunol. , vol.35 , pp. 2962-2969
    • Koppel, E.A.1    Wieland, C.W.2    Van Den Berg, V.C.3    Litjens, M.4    Florquin, S.5    Van Kooyk, Y.6    Van Der Poll, T.7    Geijtenbeek, T.B.8
  • 51
    • 21244502470 scopus 로고    scopus 로고
    • Novel innate immune functions for galectin-1: Galectin-1 inhibits cell fusion by Nipah virus envelope glycoproteins and augments dendritic cell secretion of proinflammatory cytokines
    • Levroney, E. L., H. C. Aguilar, J. A. Fulcher, L. Kohatsu, K. E. Pace, M. Pang, K. B. Gurney, L. G. Baum, and B. Lee. 2005. Novel innate immune functions for galectin-1: galectin-1 inhibits cell fusion by Nipah virus envelope glycoproteins and augments dendritic cell secretion of proinflammatory cytokines. J. Immunol. 175:413-420.
    • (2005) J. Immunol. , vol.175 , pp. 413-420
    • Levroney, E.L.1    Aguilar, H.C.2    Fulcher, J.A.3    Kohatsu, L.4    Pace, K.E.5    Pang, M.6    Gurney, K.B.7    Baum, L.G.8    Lee, B.9
  • 52
    • 72849142620 scopus 로고    scopus 로고
    • Targeted transduction via CD4 by a lentiviral vector uses a clathrin-mediated entry pathway
    • Liang, M., K. Morizono, N. Pariente, M. Kamata, B. Lee, and I. S. Chen. 2009. Targeted transduction via CD4 by a lentiviral vector uses a clathrin-mediated entry pathway. J. Virol. 83:13026-13031.
    • (2009) J. Virol. , vol.83 , pp. 13026-13031
    • Liang, M.1    Morizono, K.2    Pariente, N.3    Kamata, M.4    Lee, B.5    Chen, I.S.6
  • 53
    • 65349182389 scopus 로고    scopus 로고
    • Targeted transduction of CD34 hematopoietic progenitor cells in nonpurified human mobilized peripheral blood mononuclear cells
    • Liang, M., N. Pariente, K. Morizono, and I. S. Chen. 2009. Targeted transduction of CD34 hematopoietic progenitor cells in nonpurified human mobilized peripheral blood mononuclear cells. J. Gene Med. 11:185-196.
    • (2009) J. Gene Med. , vol.11 , pp. 185-196
    • Liang, M.1    Pariente, N.2    Morizono, K.3    Chen, I.S.4
  • 54
    • 0028017964 scopus 로고
    • Oligosaccharide profiles of HIV-2 external envelope glycoprotein: Dependence on host cells and virus isolates
    • Liedtke, S., M. Adamski, R. Geyer, A. Pfutzner, H. Rubsamen-Waigmann, and H. Geyer. 1994. Oligosaccharide profiles of HIV-2 external envelope glycoprotein: dependence on host cells and virus isolates. Glycobiology 4:477-484. (Pubitemid 24277771)
    • (1994) Glycobiology , vol.4 , Issue.4 , pp. 477-484
    • Liedtke, S.1    Adamski, M.2    Geyer, R.3    Pfutzner, A.4    Rubsamen-Waigmann, H.5    Geyer, H.6
  • 55
    • 0037227929 scopus 로고    scopus 로고
    • Differential N-linked glycosylation of human immunodeficiency virus and Ebola virus envelope glycoproteins modulates interactions with DC-SIGN and DC-SIGNR
    • Lin, G., G. Simmons, S. Pöhlmann, F. Baribaud, H. Ni, G. J. Leslie, B. S. Haggarty, P. Bates, D. Weissman, J. A. Hoxie, and R. W. Doms. 2003. Differential N-linked glycosylation of human immunodeficiency virus and Ebola virus envelope glycoproteins modulates interactions with DC-SIGN and DC-SIGNR. J. Virol. 77:1337-1346.
    • (2003) J. Virol. , vol.77 , pp. 1337-1346
    • Lin, G.1    Simmons, G.2    Pöhlmann, S.3    Baribaud, F.4    Ni, H.5    Leslie, G.J.6    Haggarty, B.S.7    Bates, P.8    Weissman, D.9    Hoxie, J.A.10    Doms, R.W.11
  • 56
    • 33751177983 scopus 로고    scopus 로고
    • Induction of antigen-specific tolerance by intrathymic injection of lentiviral vectors
    • Marodon, G., S. Fisson, B. Levacher, M. Fabre, B. L. Salomon, and D. Klatzmann. 2006. Induction of antigen-specific tolerance by intrathymic injection of lentiviral vectors. Blood 108:2972-2978.
    • (2006) Blood , vol.108 , pp. 2972-2978
    • Marodon, G.1    Fisson, S.2    Levacher, B.3    Fabre, M.4    Salomon, B.L.5    Klatzmann, D.6
  • 58
    • 0022348178 scopus 로고
    • Pattern of glycosylation of Sindbis virus envelope proteins synthesized in hamster and chicken cells
    • Mayne, J. T., J. R. Bell, E. G. Strauss, and J. H. Strauss. 1985. Pattern of glycosylation of Sindbis virus envelope proteins synthesized in hamster and chicken cells. Virology 142:121-133.
    • (1985) Virology , vol.142 , pp. 121-133
    • Mayne, J.T.1    Bell, J.R.2    Strauss, E.G.3    Strauss, J.H.4
  • 60
    • 1642392156 scopus 로고    scopus 로고
    • DC-SIGN promotes exogenous MHC-I-restricted HIV-1 antigen presentation
    • Moris, A., C. Nobile, F. Buseyne, F. Porrot, J. P. Abastado, and O. Schwartz. 2004. DC-SIGN promotes exogenous MHC-I-restricted HIV-1 antigen presentation. Blood 103:2648-2654.
    • (2004) Blood , vol.103 , pp. 2648-2654
    • Moris, A.1    Nobile, C.2    Buseyne, F.3    Porrot, F.4    Abastado, J.P.5    Schwartz, O.6
  • 61
    • 0034872863 scopus 로고    scopus 로고
    • Antibody-directed targeting of retroviral vectors via cell surface antigens
    • Morizono, K., G. Bristol, Y. M. Xie, S. K. Kung, and I. S. Chen. 2001. Antibody-directed targeting of retroviral vectors via cell surface antigens. J. Virol. 75:8016-8020.
    • (2001) J. Virol. , vol.75 , pp. 8016-8020
    • Morizono, K.1    Bristol, G.2    Xie, Y.M.3    Kung, S.K.4    Chen, I.S.5
  • 62
    • 25444522673 scopus 로고    scopus 로고
    • Targeted gene delivery by intravenous injection of retroviral vectors
    • Morizono, K., and I. S. Chen. 2005. Targeted gene delivery by intravenous injection of retroviral vectors. Cell Cycle 4:854-856. (Pubitemid 41359743)
    • (2005) Cell Cycle , vol.4 , Issue.7 , pp. 854-856
    • Morizono, K.1    Chen, I.S.Y.2
  • 63
    • 68949220821 scopus 로고    scopus 로고
    • Redirecting lentiviral vectors by insertion of integrin-tageting peptides into envelope proteins
    • Morizono, K., N. Pariente, Y. Xie, and I. S. Chen. 2009. Redirecting lentiviral vectors by insertion of integrin-tageting peptides into envelope proteins. J. Gene Med. 11:549-558.
    • (2009) J. Gene Med. , vol.11 , pp. 549-558
    • Morizono, K.1    Pariente, N.2    Xie, Y.3    Chen, I.S.4
  • 64
    • 33750075743 scopus 로고    scopus 로고
    • Transient low pH treatment enhances infection of lentiviral vector pseudotypes with a targeting Sindbis envelope
    • DOI 10.1016/j.virol.2006.07.015, PII S0042682206004727
    • Morizono, K., G. E. Ringpis, N. Pariente, Y. Xie, and I. S. Chen. 2006. Transient low pH treatment enhances infection of lentiviral vector pseudotypes with a targeting Sindbis envelope. Virology 355:71-81. (Pubitemid 44585055)
    • (2006) Virology , vol.355 , Issue.1 , pp. 71-81
    • Morizono, K.1    Ringpis, G.-E.2    Pariente, N.3    Xie, Y.4    Chen, I.S.Y.5
  • 66
    • 16244394824 scopus 로고    scopus 로고
    • Lentiviral vector retargeting to P-glycoprotein on metastatic melanoma through intravenous injection
    • Morizono, K., Y. Xie, G. E. Ringpis, M. Johnson, H. Nassanian, B. Lee, L. Wu, and I. S. Chen. 2005. Lentiviral vector retargeting to P-glycoprotein on metastatic melanoma through intravenous injection. Nat. Med. 11:346-352.
    • (2005) Nat. Med. , vol.11 , pp. 346-352
    • Morizono, K.1    Xie, Y.2    Ringpis, G.E.3    Johnson, M.4    Nassanian, H.5    Lee, B.6    Wu, L.7    Chen, I.S.8
  • 67
    • 0041707795 scopus 로고    scopus 로고
    • Deletions in the putative cell receptor-binding domain of Sindbis virus strain MRE16 E2 glycoprotein reduce midgut infectivity in Aedes aegypti
    • Myles, K. M., D. J. Pierro, and K. E. Olson. 2003. Deletions in the putative cell receptor-binding domain of Sindbis virus strain MRE16 E2 glycoprotein reduce midgut infectivity in Aedes aegypti. J. Virol. 77:8872-8881.
    • (2003) J. Virol. , vol.77 , pp. 8872-8881
    • Myles, K.M.1    Pierro, D.J.2    Olson, K.E.3
  • 69
    • 0029996147 scopus 로고    scopus 로고
    • In vivo gene delivery and stable transduction of nondividing cells by a lentiviral vector
    • Naldini, L., U. Blomer, P. Gallay, D. Ory, R. Mulligan, F. H. Gage, I. M. Verma, and D. Trono. 1996. In vivo gene delivery and stable transduction of nondividing cells by a lentiviral vector. Science 272:263-267.
    • (1996) Science , vol.272 , pp. 263-267
    • Naldini, L.1    Blomer, U.2    Gallay, P.3    Ory, D.4    Mulligan, R.5    Gage, F.H.6    Verma, I.M.7    Trono, D.8
  • 70
    • 0030835821 scopus 로고    scopus 로고
    • Cell-specific targeting of Sindbis virus vectors displaying IgG-binding domains of protein A
    • Ohno, K., K. Sawai, Y. Iijima, B. Levin, and D. Meruelo. 1997. Cell-specific targeting of Sindbis virus vectors displaying IgG-binding domains of protein A. Nat. Biotechnol. 15:763-767.
    • (1997) Nat. Biotechnol. , vol.15 , pp. 763-767
    • Ohno, K.1    Sawai, K.2    Iijima, Y.3    Levin, B.4    Meruelo, D.5
  • 71
    • 40649094826 scopus 로고    scopus 로고
    • Efficient targeted transduction of primary human endothelial cells with dual-targeted lentiviral vectors
    • DOI 10.1002/jgm.1151
    • Pariente, N., S. H. Mao, K. Morizono, and I. S. Chen. 2008. Efficient targeted transduction of primary human endothelial cells with dual-targeted lentiviral vectors. J. Gene Med. 10:242-248. (Pubitemid 351368991)
    • (2008) Journal of Gene Medicine , vol.10 , Issue.3 , pp. 242-248
    • Pariente, N.1    Mao, S.-H.2    Morizono, K.3    Chen, I.S.Y.4
  • 72
    • 35548936912 scopus 로고    scopus 로고
    • A novel dual-targeted lentiviral vector leads to specific transduction of prostate cancer bone metastases in vivo after systemic administration
    • Pariente, N., K. Morizono, M. S. Virk, F. A. Petrigliano, R. E. Reiter, J. R. Lieberman, and I. S. Chen. 2007. A novel dual-targeted lentiviral vector leads to specific transduction of prostate cancer bone metastases in vivo after systemic administration. Mol. Ther. 15:1973-1981.
    • (2007) Mol. Ther. , vol.15 , pp. 1973-1981
    • Pariente, N.1    Morizono, K.2    Virk, M.S.3    Petrigliano, F.A.4    Reiter, R.E.5    Lieberman, J.R.6    Chen, I.S.7
  • 77
    • 56449098432 scopus 로고    scopus 로고
    • Utilization of DC-SIGN for entry of feline coronaviruses into host cells
    • Regan, A. D., and G. R. Whittaker. 2008. Utilization of DC-SIGN for entry of feline coronaviruses into host cells. J. Virol. 82:11992-11996.
    • (2008) J. Virol. , vol.82 , pp. 11992-11996
    • Regan, A.D.1    Whittaker, G.R.2
  • 78
    • 33645978992 scopus 로고    scopus 로고
    • Emerging patterns in complement-mediated pathogen recognition
    • Roozendaal, R., and M. C. Carroll. 2006. Emerging patterns in complement-mediated pathogen recognition. Cell 125:29-32.
    • (2006) Cell , vol.125 , pp. 29-32
    • Roozendaal, R.1    Carroll, M.C.2
  • 80
    • 0037455567 scopus 로고    scopus 로고
    • Individual expression of Sindbis virus glycoproteins. E1 alone promotes cell fusion
    • Sanz, M. A., M. T. Rejas, and L. Carrasco. 2003. Individual expression of Sindbis virus glycoproteins. E1 alone promotes cell fusion. Virology 305:463-472.
    • (2003) Virology , vol.305 , pp. 463-472
    • Sanz, M.A.1    Rejas, M.T.2    Carrasco, L.3
  • 81
    • 13544253713 scopus 로고    scopus 로고
    • Complement regulatory proteins are incorporated into lentiviral vectors and protect particles against complement inactivation
    • DOI 10.1038/sj.gt.3302399
    • Schauber-Plewa, C., A. Simmons, M. J. Tuerk, C. D. Pacheco, and G. Veres. 2005. Complement regulatory proteins are incorporated into lentiviral vectors and protect particles against complement inactivation. Gene Ther. 12:238-245. (Pubitemid 40220625)
    • (2005) Gene Therapy , vol.12 , Issue.3 , pp. 238-245
    • Schauber-Plewa, C.1    Simmons, A.2    Tuerk, M.J.3    Pacheco, C.D.4    Veres, G.5
  • 83
    • 0032499531 scopus 로고    scopus 로고
    • Cell-specific viral targeting mediated by a soluble retroviral receptor-ligand fusion protein
    • Snitkovsky, S., and J. A. Young. 1998. Cell-specific viral targeting mediated by a soluble retroviral receptor-ligand fusion protein. Proc. Natl. Acad. Sci. U. S. A. 95:7063-7068.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 7063-7068
    • Snitkovsky, S.1    Young, J.A.2
  • 84
    • 36248965712 scopus 로고    scopus 로고
    • Dendritic cells: Understanding immunogenicity
    • Steinman, R. M. 2007. Dendritic cells: understanding immunogenicity. Eur. J. Immunol. 37(Suppl. 1):S53-S60.
    • (2007) Eur. J. Immunol. , vol.37 , Issue.SUPPL. 1
    • Steinman, R.M.1
  • 89
    • 34447535345 scopus 로고    scopus 로고
    • Engineering targeted viral vectors for gene therapy
    • Waehler, R., S. J. Russell, and D. T. Curiel. 2007. Engineering targeted viral vectors for gene therapy. Nat. Rev. Genet. 8:573-587.
    • (2007) Nat. Rev. Genet. , vol.8 , pp. 573-587
    • Waehler, R.1    Russell, S.J.2    Curiel, D.T.3
  • 90
    • 0026628752 scopus 로고
    • High-affinity laminin receptor is a receptor for Sindbis virus in mammalian cells
    • Wang, K. S., R. J. Kuhn, E. G. Strauss, S. Ou, and J. H. Strauss. 1992. High-affinity laminin receptor is a receptor for Sindbis virus in mammalian cells. J. Virol. 66:4992-5001.
    • (1992) J. Virol. , vol.66 , pp. 4992-5001
    • Wang, K.S.1    Kuhn, R.J.2    Strauss, E.G.3    Ou, S.4    Strauss, J.H.5
  • 93
    • 2442691605 scopus 로고    scopus 로고
    • PH-dependent entry of severe acute respiratory syndrome coronavirus is mediated by the spike glycoprotein and enhanced by dendritic cell transfer through DC-SIGN
    • Yang, Z. Y., Y. Huang, L. Ganesh, K. Leung, W. P. Kong, O. Schwartz, K. Subbarao, and G. J. Nabel. 2004. pH-dependent entry of severe acute respiratory syndrome coronavirus is mediated by the spike glycoprotein and enhanced by dendritic cell transfer through DC-SIGN. J. Virol. 78:5642-5650.
    • (2004) J. Virol. , vol.78 , pp. 5642-5650
    • Yang, Z.Y.1    Huang, Y.2    Ganesh, L.3    Leung, K.4    Kong, W.P.5    Schwartz, O.6    Subbarao, K.7    Nabel, G.J.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.