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Volumn 134, Issue 1-2, 2008, Pages 181-192

Engineering of SV40-based nano-capsules for delivery of heterologous proteins as fusions with the minor capsid proteins VP2/3

Author keywords

Nano capsule; Protein delivery; SV40; VLP

Indexed keywords

BIOMATERIALS; CELL DEATH; FUSION REACTIONS; MOLECULAR INTERACTIONS; PROTEINS; SELF ASSEMBLY;

EID: 39649120302     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2007.12.006     Document Type: Article
Times cited : (74)

References (27)
  • 2
    • 27944501453 scopus 로고    scopus 로고
    • Polyomavirus EGFP-pseudocapsids: analysis of model particles for introduction of proteins and peptides into mammalian cells
    • Boura E., Liebl D., Spisek R., Fric J., Marek M., Stokrova J., Holan V., and Forstova J. Polyomavirus EGFP-pseudocapsids: analysis of model particles for introduction of proteins and peptides into mammalian cells. FEBS Lett. 579 (2005) 6549-6558
    • (2005) FEBS Lett. , vol.579 , pp. 6549-6558
    • Boura, E.1    Liebl, D.2    Spisek, R.3    Fric, J.4    Marek, M.5    Stokrova, J.6    Holan, V.7    Forstova, J.8
  • 3
    • 0032526711 scopus 로고    scopus 로고
    • Interaction of polyomavirus internal protein VP2 with the major capsid protein VP1 and implications for participation of VP2 in viral entry
    • Chen X.S., Stehle T., and Harrison S.C. Interaction of polyomavirus internal protein VP2 with the major capsid protein VP1 and implications for participation of VP2 in viral entry. EMBO J. 17 (1998) 3233-3240
    • (1998) EMBO J. , vol.17 , pp. 3233-3240
    • Chen, X.S.1    Stehle, T.2    Harrison, S.C.3
  • 4
    • 33845655873 scopus 로고    scopus 로고
    • SV40 VP2 and VP3 insertion into ER membranes is controlled by the capsid protein VP1: implications for DNA translocation out of the ER
    • Daniels R., Rusan N.M., Wadsworth P., and Hebert D.N. SV40 VP2 and VP3 insertion into ER membranes is controlled by the capsid protein VP1: implications for DNA translocation out of the ER. Mol. Cell 24 (2006) 955-966
    • (2006) Mol. Cell , vol.24 , pp. 955-966
    • Daniels, R.1    Rusan, N.M.2    Wadsworth, P.3    Hebert, D.N.4
  • 5
    • 0028885230 scopus 로고
    • Essential role of the Vp2 and Vp3 DNA-binding domain in simian virus 40 morphogenesis
    • Dean D.A., Li P.P., Lee L.M., and Kasamatsu H. Essential role of the Vp2 and Vp3 DNA-binding domain in simian virus 40 morphogenesis. J. Virol. 69 (1995) 1115-1121
    • (1995) J. Virol. , vol.69 , pp. 1115-1121
    • Dean, D.A.1    Li, P.P.2    Lee, L.M.3    Kasamatsu, H.4
  • 6
    • 9244257843 scopus 로고    scopus 로고
    • Virus-like particles as vaccines and vessels for the delivery of small molecules
    • Garcea R.L., and Gissmann L. Virus-like particles as vaccines and vessels for the delivery of small molecules. Curr. Opin. Biotechnol. 15 (2004) 513-517
    • (2004) Curr. Opin. Biotechnol. , vol.15 , pp. 513-517
    • Garcea, R.L.1    Gissmann, L.2
  • 7
    • 0035123128 scopus 로고    scopus 로고
    • Gene directed enzyme/prodrug therapy of cancer: historical appraisal and future prospectives
    • Greco O., and Dachs G.U. Gene directed enzyme/prodrug therapy of cancer: historical appraisal and future prospectives. J. Cell Physiol. 187 (2001) 22-36
    • (2001) J. Cell Physiol. , vol.187 , pp. 22-36
    • Greco, O.1    Dachs, G.U.2
  • 9
    • 0034749345 scopus 로고    scopus 로고
    • Roles of disulfide linkage and calcium ion-mediated interactions in assembly and disassembly of virus-like particles composed of simian virus 40 VP1 capsid protein
    • Ishizu K.I., Watanabe H., Han S.I., Kanesashi S.N., Hoque M., Yajima H., Kataoka K., and Handa H. Roles of disulfide linkage and calcium ion-mediated interactions in assembly and disassembly of virus-like particles composed of simian virus 40 VP1 capsid protein. J. Virol. 75 (2001) 61-72
    • (2001) J. Virol. , vol.75 , pp. 61-72
    • Ishizu, K.I.1    Watanabe, H.2    Han, S.I.3    Kanesashi, S.N.4    Hoque, M.5    Yajima, H.6    Kataoka, K.7    Handa, H.8
  • 11
    • 0024844490 scopus 로고
    • Endocytosis of simian virus 40 into the endoplasmic reticulum
    • Kartenbeck J., Stukenbrok H., and Helenius A. Endocytosis of simian virus 40 into the endoplasmic reticulum. J. Cell Biol. 109 (1989) 2721-2729
    • (1989) J. Cell Biol. , vol.109 , pp. 2721-2729
    • Kartenbeck, J.1    Stukenbrok, H.2    Helenius, A.3
  • 12
    • 33748164439 scopus 로고    scopus 로고
    • A structural rationale for SV40 Vp1 temperature-sensitive mutants and their complementation
    • Kasamatsu H., Woo J., Nakamura A., Muller P., Tevethia M.J., and Liddington R.C. A structural rationale for SV40 Vp1 temperature-sensitive mutants and their complementation. Protein Sci. 15 (2006) 2207-2213
    • (2006) Protein Sci. , vol.15 , pp. 2207-2213
    • Kasamatsu, H.1    Woo, J.2    Nakamura, A.3    Muller, P.4    Tevethia, M.J.5    Liddington, R.C.6
  • 14
    • 18244373419 scopus 로고    scopus 로고
    • Computational thermostabilization of an enzyme
    • Korkegian A., Black M.E., Baker D., and Stoddard B.L. Computational thermostabilization of an enzyme. Science 308 (2005) 857-860
    • (2005) Science , vol.308 , pp. 857-860
    • Korkegian, A.1    Black, M.E.2    Baker, D.3    Stoddard, B.L.4
  • 15
    • 0029984841 scopus 로고    scopus 로고
    • Purification and characterization of virus-like particles and pentamers produced by the expression of SV40 capsid proteins in insect cells
    • Kosukegawa A., Arisaka F., Takayama M., Yajima H., Kaidow A., and Handa H. Purification and characterization of virus-like particles and pentamers produced by the expression of SV40 capsid proteins in insect cells. Biochim. Biophys. Acta 1290 (1996) 37-45
    • (1996) Biochim. Biophys. Acta , vol.1290 , pp. 37-45
    • Kosukegawa, A.1    Arisaka, F.2    Takayama, M.3    Yajima, H.4    Kaidow, A.5    Handa, H.6
  • 18
    • 0025955776 scopus 로고
    • Nuclear assembly of polyomavirus capsids in insect cells expressing the major capsid protein VP1
    • Montross L., Watkins S., Moreland R.B., Mamon H., Caspar D.L., and Garcea R.L. Nuclear assembly of polyomavirus capsids in insect cells expressing the major capsid protein VP1. J. Virol. 65 (1991) 4991-4998
    • (1991) J. Virol. , vol.65 , pp. 4991-4998
    • Montross, L.1    Watkins, S.2    Moreland, R.B.3    Mamon, H.4    Caspar, D.L.5    Garcea, R.L.6
  • 19
    • 33748155200 scopus 로고    scopus 로고
    • Identification of amino acid residues within simian virus 40 capsid proteins Vp1, Vp2, and Vp3 that are required for their interaction and for viral infection
    • Nakanishi A., Nakamura A., Liddington R., and Kasamatsu H. Identification of amino acid residues within simian virus 40 capsid proteins Vp1, Vp2, and Vp3 that are required for their interaction and for viral infection. J. Virol. 80 (2006) 8891-8898
    • (2006) J. Virol. , vol.80 , pp. 8891-8898
    • Nakanishi, A.1    Nakamura, A.2    Liddington, R.3    Kasamatsu, H.4
  • 20
    • 0037134014 scopus 로고    scopus 로고
    • Local actin polymerization and dynamin recruitment in SV40-induced internalization of caveolae
    • Pelkmans L., Puntener D., and Helenius A. Local actin polymerization and dynamin recruitment in SV40-induced internalization of caveolae. Science 296 (2002) 535-539
    • (2002) Science , vol.296 , pp. 535-539
    • Pelkmans, L.1    Puntener, D.2    Helenius, A.3
  • 21
    • 0020031457 scopus 로고
    • Polyoma virus capsid structure at 22.5 A resolution
    • Rayment I., Baker T.S., Caspar D.L., and Murakami W.T. Polyoma virus capsid structure at 22.5 A resolution. Nature 295 (1982) 110-115
    • (1982) Nature , vol.295 , pp. 110-115
    • Rayment, I.1    Baker, T.S.2    Caspar, D.L.3    Murakami, W.T.4
  • 22
    • 0022549499 scopus 로고
    • Self-assembly of purified polyomavirus capsid protein VP1
    • Salunke D.M., Caspar D.L., and Garcea R.L. Self-assembly of purified polyomavirus capsid protein VP1. Cell 46 (1986) 895-904
    • (1986) Cell , vol.46 , pp. 895-904
    • Salunke, D.M.1    Caspar, D.L.2    Garcea, R.L.3
  • 23
    • 0035408759 scopus 로고    scopus 로고
    • Protein and peptide delivery via engineered polyomavirus-like particles
    • Schmidt U., Gunther C., Rudolph R., and Bohm G. Protein and peptide delivery via engineered polyomavirus-like particles. FASEB J. 15 (2001) 1646-1648
    • (2001) FASEB J. , vol.15 , pp. 1646-1648
    • Schmidt, U.1    Gunther, C.2    Rudolph, R.3    Bohm, G.4
  • 25
    • 0030584124 scopus 로고    scopus 로고
    • The structure of simian virus 40 refined at 3.1 A resolution
    • Stehle T., Gamblin S.J., Yan Y., and Harrison S.C. The structure of simian virus 40 refined at 3.1 A resolution. Structure 4 (1996) 165-182
    • (1996) Structure , vol.4 , pp. 165-182
    • Stehle, T.1    Gamblin, S.J.2    Yan, Y.3    Harrison, S.C.4
  • 26
    • 34347387533 scopus 로고    scopus 로고
    • Dendritic cells loaded with polyomavirus VP1/VP2Her2 virus-like particles efficiently prevent outgrowth of a Her2/neu expressing tumor
    • Tegerstedt K., Franzen A., Ramqvist T., and Dalianis T. Dendritic cells loaded with polyomavirus VP1/VP2Her2 virus-like particles efficiently prevent outgrowth of a Her2/neu expressing tumor. Cancer Immunol. Immunother. 56 (2007) 1335-1344
    • (2007) Cancer Immunol. Immunother. , vol.56 , pp. 1335-1344
    • Tegerstedt, K.1    Franzen, A.2    Ramqvist, T.3    Dalianis, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.