메뉴 건너뛰기




Volumn 34, Issue 30, 2013, Pages 7506-7518

Self-biotinylation and site-specific double labeling of baculovirus using quantum dots for single-virus in-situ tracking

Author keywords

Autographa californica multiple nucleopolyhedrovirus; Double labeled virus; Long term tracking; Quantum dot; Self biotinylated; Single virus tracking

Indexed keywords

AUTOGRAPHA CALIFORNICA; BIOCHEMICAL METHODS; DISASSEMBLY PROCESS; FUNCTIONAL STRUCTURE; GREEN FLUORESCENT PROTEIN; LONG-TERM TRACKING; QUANTUM DOT; SELF-BIOTINYLATED;

EID: 84880512565     PISSN: 01429612     EISSN: 18785905     Source Type: Journal    
DOI: 10.1016/j.biomaterials.2013.06.030     Document Type: Article
Times cited : (40)

References (47)
  • 2
    • 2542452779 scopus 로고    scopus 로고
    • Assembly of endocytic machinery around individual influenza viruses during viral entry
    • Rust M.J., Lakadamyali M., Zhang F., Zhuang X. Assembly of endocytic machinery around individual influenza viruses during viral entry. Nat Struct Mol Biol 2004, 11:567-573.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 567-573
    • Rust, M.J.1    Lakadamyali, M.2    Zhang, F.3    Zhuang, X.4
  • 3
    • 84865167629 scopus 로고    scopus 로고
    • High-efficiency dual labeling of influenza virus for single-virus imaging
    • Liu S.L., Tian Z.Q., Zhang Z.L., Wu Q.M., Zhao H.S., Ren B., et al. High-efficiency dual labeling of influenza virus for single-virus imaging. Biomaterials 2012, 33:7828-7833.
    • (2012) Biomaterials , vol.33 , pp. 7828-7833
    • Liu, S.L.1    Tian, Z.Q.2    Zhang, Z.L.3    Wu, Q.M.4    Zhao, H.S.5    Ren, B.6
  • 4
    • 84856190012 scopus 로고    scopus 로고
    • Effectively and efficiently dissecting the infection of influenza virus by quantum-dot-based single-particle tracking
    • Liu S.L., Zhang Z.L., Tian Z.Q., Zhao H.S., Liu H., Sun E.Z., et al. Effectively and efficiently dissecting the infection of influenza virus by quantum-dot-based single-particle tracking. ACS Nano 2012, 6:141-150.
    • (2012) ACS Nano , vol.6 , pp. 141-150
    • Liu, S.L.1    Zhang, Z.L.2    Tian, Z.Q.3    Zhao, H.S.4    Liu, H.5    Sun, E.Z.6
  • 5
    • 63149150029 scopus 로고    scopus 로고
    • Imaging viral behavior in mammalian cells with self-assembled capsid-quantum-dot hybrid particles
    • Li F., Zhang Z.P., Peng J., Cui Z.Q., Pang D.W., Li K., et al. Imaging viral behavior in mammalian cells with self-assembled capsid-quantum-dot hybrid particles. Small 2009, 5:718-726.
    • (2009) Small , vol.5 , pp. 718-726
    • Li, F.1    Zhang, Z.P.2    Peng, J.3    Cui, Z.Q.4    Pang, D.W.5    Li, K.6
  • 9
    • 73349130473 scopus 로고    scopus 로고
    • High-speed nanoscopic tracking of the position and orientation of a single virus
    • Kukura P., Ewers H., Muller C., Renn A., Helenius A., Sandoghdar V. High-speed nanoscopic tracking of the position and orientation of a single virus. Nat Methods 2009, 6:923-927.
    • (2009) Nat Methods , vol.6 , pp. 923-927
    • Kukura, P.1    Ewers, H.2    Muller, C.3    Renn, A.4    Helenius, A.5    Sandoghdar, V.6
  • 10
    • 0035976603 scopus 로고    scopus 로고
    • Real-time single-molecule imaging of the infection pathway of an adeno-associated virus
    • Seisenberger G., Ried M.U., Endress T., Buning H., Hallek M., Brauchle C. Real-time single-molecule imaging of the infection pathway of an adeno-associated virus. Science 2001, 294:1929-1932.
    • (2001) Science , vol.294 , pp. 1929-1932
    • Seisenberger, G.1    Ried, M.U.2    Endress, T.3    Buning, H.4    Hallek, M.5    Brauchle, C.6
  • 11
    • 80052073171 scopus 로고    scopus 로고
    • Clathrin-mediated endocytosis in living host cells visualized through quantum dot labeling of infectious hematopoietic necrosis virus
    • Liu H., Liu Y., Liu S., Pang D.W., Xiao G. Clathrin-mediated endocytosis in living host cells visualized through quantum dot labeling of infectious hematopoietic necrosis virus. JVirol 2011, 85:6252-6262.
    • (2011) JVirol , vol.85 , pp. 6252-6262
    • Liu, H.1    Liu, Y.2    Liu, S.3    Pang, D.W.4    Xiao, G.5
  • 12
    • 33847131016 scopus 로고    scopus 로고
    • Virus trafficking - learning from single-virus tracking
    • Brandenburg B., Zhuang X. Virus trafficking - learning from single-virus tracking. Nat Rev Microbiol 2007, 5:197-208.
    • (2007) Nat Rev Microbiol , vol.5 , pp. 197-208
    • Brandenburg, B.1    Zhuang, X.2
  • 13
    • 51849137912 scopus 로고    scopus 로고
    • Site-specific labeling of enveloped viruses with quantum dots for single virus tracking
    • Joo K.I., Lei Y., Lee C.L., Lo J., Xie J., Hamm-Alvarez S.F., et al. Site-specific labeling of enveloped viruses with quantum dots for single virus tracking. ACS Nano 2008, 2:1553-1562.
    • (2008) ACS Nano , vol.2 , pp. 1553-1562
    • Joo, K.I.1    Lei, Y.2    Lee, C.L.3    Lo, J.4    Xie, J.5    Hamm-Alvarez, S.F.6
  • 15
    • 79954632655 scopus 로고    scopus 로고
    • Generating enveloped virus-like particles with invitro assembled cores
    • Cheng F., Mukhopadhyay S. Generating enveloped virus-like particles with invitro assembled cores. Virology 2011, 413:153-160.
    • (2011) Virology , vol.413 , pp. 153-160
    • Cheng, F.1    Mukhopadhyay, S.2
  • 16
  • 17
    • 0033526508 scopus 로고    scopus 로고
    • Host cell receptor binding by baculovirus GP64 and kinetics of virion entry
    • Hefferon K.L., Oomens A.G., Monsma S.A., Finnerty C.M., Blissard G.W. Host cell receptor binding by baculovirus GP64 and kinetics of virion entry. Virology 1999, 258:455-468.
    • (1999) Virology , vol.258 , pp. 455-468
    • Hefferon, K.L.1    Oomens, A.G.2    Monsma, S.A.3    Finnerty, C.M.4    Blissard, G.W.5
  • 18
    • 77951478767 scopus 로고    scopus 로고
    • Autographa californica multicapsid nucleopolyhedrovirus efficiently infects Sf9 cells and transduces mammalian cells via direct fusion with the plasma membrane at low pH
    • Dong S., Wang M., Qiu Z., Deng F., Vlak J.M., Hu Z., et al. Autographa californica multicapsid nucleopolyhedrovirus efficiently infects Sf9 cells and transduces mammalian cells via direct fusion with the plasma membrane at low pH. JVirol 2010, 84:5351-5359.
    • (2010) JVirol , vol.84 , pp. 5351-5359
    • Dong, S.1    Wang, M.2    Qiu, Z.3    Deng, F.4    Vlak, J.M.5    Hu, Z.6
  • 19
    • 3242786572 scopus 로고    scopus 로고
    • Baculovirus display strategies: emerging tools for eukaryotic libraries and gene delivery
    • Oker-Blom C., Airenne K.J., Grabherr R. Baculovirus display strategies: emerging tools for eukaryotic libraries and gene delivery. Brief Funct Genomic Proteomic 2003, 2:244-253.
    • (2003) Brief Funct Genomic Proteomic , vol.2 , pp. 244-253
    • Oker-Blom, C.1    Airenne, K.J.2    Grabherr, R.3
  • 20
    • 77954980510 scopus 로고    scopus 로고
    • Actin-based motility drives baculovirus transit to the nucleus and cell surface
    • Ohkawa T., Volkman L.E., Welch M.D. Actin-based motility drives baculovirus transit to the nucleus and cell surface. JCell Biol 2010, 190:187-195.
    • (2010) JCell Biol , vol.190 , pp. 187-195
    • Ohkawa, T.1    Volkman, L.E.2    Welch, M.D.3
  • 21
    • 79960939738 scopus 로고    scopus 로고
    • Co-expression of four baculovirus proteins, IE1, LEF3, P143, and PP31, elicits a cellular chromatin-containing reticulate structure in the nuclei of uninfected cells
    • Nagamine T., Abe A., Suzuki T., Dohmae N., Matsumoto S. Co-expression of four baculovirus proteins, IE1, LEF3, P143, and PP31, elicits a cellular chromatin-containing reticulate structure in the nuclei of uninfected cells. Virology 2011, 417:188-195.
    • (2011) Virology , vol.417 , pp. 188-195
    • Nagamine, T.1    Abe, A.2    Suzuki, T.3    Dohmae, N.4    Matsumoto, S.5
  • 22
    • 1842859698 scopus 로고    scopus 로고
    • Interaction of Heliothis armigera nuclear polyhedrosis viral capsid protein with its host actin
    • Lu S.Y., Qi Y.P., Ge G.Q. Interaction of Heliothis armigera nuclear polyhedrosis viral capsid protein with its host actin. JBiochem Mol Biol 2002, 35:562-567.
    • (2002) JBiochem Mol Biol , vol.35 , pp. 562-567
    • Lu, S.Y.1    Qi, Y.P.2    Ge, G.Q.3
  • 23
    • 33748674858 scopus 로고    scopus 로고
    • Functional entry of baculovirus into insect and mammalian cells is dependent on clathrin-mediated endocytosis
    • Long G., Pan X.Y., Kormelink R., Vlak J.M. Functional entry of baculovirus into insect and mammalian cells is dependent on clathrin-mediated endocytosis. JVirol 2006, 80:8830-8833.
    • (2006) JVirol , vol.80 , pp. 8830-8833
    • Long, G.1    Pan, X.Y.2    Kormelink, R.3    Vlak, J.M.4
  • 25
  • 26
    • 64549109320 scopus 로고    scopus 로고
    • Clathrin-independent entry of baculovirus triggers uptake of E.coli in non-phagocytic human cells
    • Laakkonen J.P., Makela A.R., Kakkonen E., Turkki P., Kukkonen S., Peranen J., et al. Clathrin-independent entry of baculovirus triggers uptake of E.coli in non-phagocytic human cells. PLoS One 2009, 4:e5093.
    • (2009) PLoS One , vol.4
    • Laakkonen, J.P.1    Makela, A.R.2    Kakkonen, E.3    Turkki, P.4    Kukkonen, S.5    Peranen, J.6
  • 27
    • 0026757345 scopus 로고
    • Baculovirus gp64 envelope glycoprotein is sufficient to mediate pH-dependent membrane fusion
    • Blissard G.W., Wenz J.R. Baculovirus gp64 envelope glycoprotein is sufficient to mediate pH-dependent membrane fusion. JVirol 1992, 66:6829-6835.
    • (1992) JVirol , vol.66 , pp. 6829-6835
    • Blissard, G.W.1    Wenz, J.R.2
  • 28
    • 0028915080 scopus 로고
    • Identification of a membrane fusion domain and an oligomerization domain in the baculovirus GP64 envelope fusion protein
    • Monsma S.A., Blissard G.W. Identification of a membrane fusion domain and an oligomerization domain in the baculovirus GP64 envelope fusion protein. JVirol 1995, 69:2583-2595.
    • (1995) JVirol , vol.69 , pp. 2583-2595
    • Monsma, S.A.1    Blissard, G.W.2
  • 29
    • 0028822096 scopus 로고
    • Eukaryotic virus display: engineering the major surface glycoprotein of the Autographa californica nuclear polyhedrosis virus (AcNPV) for the presentation of foreign proteins on the virus surface
    • Boublik Y., Di Bonito P., Jones I.M. Eukaryotic virus display: engineering the major surface glycoprotein of the Autographa californica nuclear polyhedrosis virus (AcNPV) for the presentation of foreign proteins on the virus surface. Biotechnology (NY) 1995, 13:1079-1084.
    • (1995) Biotechnology (NY) , vol.13 , pp. 1079-1084
    • Boublik, Y.1    Di Bonito, P.2    Jones, I.M.3
  • 30
    • 0030890576 scopus 로고    scopus 로고
    • Expression of foreign proteins on the surface of Autographa californica nuclear polyhedrosis virus
    • Grabherr R., Ernst W., Doblhoff-Dier O., Sara M., Katinger H. Expression of foreign proteins on the surface of Autographa californica nuclear polyhedrosis virus. Biotechniques 1997, 22:730-735.
    • (1997) Biotechniques , vol.22 , pp. 730-735
    • Grabherr, R.1    Ernst, W.2    Doblhoff-Dier, O.3    Sara, M.4    Katinger, H.5
  • 32
    • 0036925266 scopus 로고    scopus 로고
    • Properties of baculovirus particles displaying GFP analyzed by fluorescence correlation spectroscopy
    • Toivola J., Ojala K., Michel P.O., Vuento M., Oker-Blom C. Properties of baculovirus particles displaying GFP analyzed by fluorescence correlation spectroscopy. Biol Chem 2002, 383:1941-1946.
    • (2002) Biol Chem , vol.383 , pp. 1941-1946
    • Toivola, J.1    Ojala, K.2    Michel, P.O.3    Vuento, M.4    Oker-Blom, C.5
  • 33
    • 0032052263 scopus 로고    scopus 로고
    • Baculovirus surface display: construction and screening of a eukaryotic epitope library
    • Ernst W., Grabherr R., Wegner D., Borth N., Grassauer A., Katinger H. Baculovirus surface display: construction and screening of a eukaryotic epitope library. Nucleic Acids Res 1998, 26:1718-1723.
    • (1998) Nucleic Acids Res , vol.26 , pp. 1718-1723
    • Ernst, W.1    Grabherr, R.2    Wegner, D.3    Borth, N.4    Grassauer, A.5    Katinger, H.6
  • 34
    • 0039310043 scopus 로고
    • Use of peptide libraries to map the substrate specificity of a peptide-modifying enzyme: a 13 residue consensus peptide specifies biotinylation in Escherichia coli
    • Schatz P.J. Use of peptide libraries to map the substrate specificity of a peptide-modifying enzyme: a 13 residue consensus peptide specifies biotinylation in Escherichia coli. Biotechnology (NY) 1993, 11:1138-1143.
    • (1993) Biotechnology (NY) , vol.11 , pp. 1138-1143
    • Schatz, P.J.1
  • 36
    • 84856479181 scopus 로고    scopus 로고
    • Dual-objective STORM reveals three-dimensional filament organization in the actin cytoskeleton
    • Xu K., Babcock H.P., Zhuang X. Dual-objective STORM reveals three-dimensional filament organization in the actin cytoskeleton. Nat Methods 2012, 9:185-188.
    • (2012) Nat Methods , vol.9 , pp. 185-188
    • Xu, K.1    Babcock, H.P.2    Zhuang, X.3
  • 38
    • 45749104724 scopus 로고    scopus 로고
    • Nuclear marginalization of host cell chromatin associated with expansion of two discrete virus-induced subnuclear compartments during baculovirus infection
    • Nagamine T., Kawasaki Y., Abe A., Matsumoto S. Nuclear marginalization of host cell chromatin associated with expansion of two discrete virus-induced subnuclear compartments during baculovirus infection. JVirol 2008, 82:6409-6418.
    • (2008) JVirol , vol.82 , pp. 6409-6418
    • Nagamine, T.1    Kawasaki, Y.2    Abe, A.3    Matsumoto, S.4
  • 39
    • 77953762782 scopus 로고    scopus 로고
    • Proteomics of the Autographa californica nucleopolyhedrovirus budded virions
    • Wang R., Deng F., Hou D., Zhao Y., Guo L., Wang H., et al. Proteomics of the Autographa californica nucleopolyhedrovirus budded virions. JVirol 2010, 84:7233-7242.
    • (2010) JVirol , vol.84 , pp. 7233-7242
    • Wang, R.1    Deng, F.2    Hou, D.3    Zhao, Y.4    Guo, L.5    Wang, H.6
  • 40
    • 77953664125 scopus 로고    scopus 로고
    • Baculovirus for eukaryotic protein display
    • Grabherr R., Ernst W. Baculovirus for eukaryotic protein display. Curr Gene Ther 2010, 10:195-200.
    • (2010) Curr Gene Ther , vol.10 , pp. 195-200
    • Grabherr, R.1    Ernst, W.2
  • 43
    • 13944263526 scopus 로고    scopus 로고
    • Involvement of the Toll-like receptor 9 signaling pathway in the induction of innate immunity by baculovirus
    • Abe T., Hemmi H., Miyamoto H., Moriishi K., Tamura S., Takaku H., et al. Involvement of the Toll-like receptor 9 signaling pathway in the induction of innate immunity by baculovirus. JVirol 2005, 79:2847-2858.
    • (2005) JVirol , vol.79 , pp. 2847-2858
    • Abe, T.1    Hemmi, H.2    Miyamoto, H.3    Moriishi, K.4    Tamura, S.5    Takaku, H.6
  • 44
    • 79959959890 scopus 로고    scopus 로고
    • Single-particle tracking as a quantitative microscopy-based approach to unravel cell entry mechanisms of viruses and pharmaceutical nanoparticles
    • Ruthardt N., Lamb D.C., Brauchle C. Single-particle tracking as a quantitative microscopy-based approach to unravel cell entry mechanisms of viruses and pharmaceutical nanoparticles. Mol Ther 2011, 19:1199-1211.
    • (2011) Mol Ther , vol.19 , pp. 1199-1211
    • Ruthardt, N.1    Lamb, D.C.2    Brauchle, C.3
  • 45
    • 80051491980 scopus 로고    scopus 로고
    • Visualizing the endocytic and exocytic processes of wheat germ agglutinin by quantum dot-based single-particle tracking
    • Liu S.L., Zhang Z.L., Sun E.Z., Peng J., Xie M., Tian Z.Q., et al. Visualizing the endocytic and exocytic processes of wheat germ agglutinin by quantum dot-based single-particle tracking. Biomaterials 2011, 32:7616-7624.
    • (2011) Biomaterials , vol.32 , pp. 7616-7624
    • Liu, S.L.1    Zhang, Z.L.2    Sun, E.Z.3    Peng, J.4    Xie, M.5    Tian, Z.Q.6
  • 46
    • 80051757521 scopus 로고    scopus 로고
    • Intracellular protein target detection by quantum dots optimized for live cell imaging
    • Choi Y., Kim K., Hong S., Kim H., Kwon Y.J., Song R. Intracellular protein target detection by quantum dots optimized for live cell imaging. Bioconjug Chem 2011, 22:1576-1586.
    • (2011) Bioconjug Chem , vol.22 , pp. 1576-1586
    • Choi, Y.1    Kim, K.2    Hong, S.3    Kim, H.4    Kwon, Y.J.5    Song, R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.