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Volumn 151, Issue 2, 2008, Pages 172-180

Recombinant hepatitis B virus core particles: Association, dissociation and encapsidation of green fluorescent protein

Author keywords

Capsid assembly; Denaturing agent; Green fluorescent protein; Hepatitis B core antigen; Hepatitis B virus capsid; Protein encapsidation

Indexed keywords

DENATURING AGENT; GREEN FLUORESCENT PROTEIN; GUANIDINE; HEPATITIS B CORE ANTIGEN; NUCLEIC ACID; REAGENT; RECOMBINANT ANTIGEN; RECOMBINANT HEPATITIS B CORE ANTIGEN; UREA;

EID: 46749101277     PISSN: 01660934     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jviromet.2008.05.025     Document Type: Article
Times cited : (56)

References (34)
  • 1
    • 0343279043 scopus 로고    scopus 로고
    • Packaging of up to 240 subunits of a 17 kDa nuclease into the interior of recombinant hepatitis B virus capsids
    • Beterams G., Böttcher B., and Nassal M. Packaging of up to 240 subunits of a 17 kDa nuclease into the interior of recombinant hepatitis B virus capsids. FEBS Lett. 481 (2000) 169-176
    • (2000) FEBS Lett. , vol.481 , pp. 169-176
    • Beterams, G.1    Böttcher, B.2    Nassal, M.3
  • 2
    • 0343147172 scopus 로고    scopus 로고
    • Peptides that block hepatitis B virus assembly: analysis by cryomicroscopy, mutagenesis and transfection
    • Böttcher B., Tsuji N., Takakashi H., Dyson M.R., Zhao S., Crowther R.A., and Murray K. Peptides that block hepatitis B virus assembly: analysis by cryomicroscopy, mutagenesis and transfection. EMBO J. 17 (1998) 6839-6845
    • (1998) EMBO J. , vol.17 , pp. 6839-6845
    • Böttcher, B.1    Tsuji, N.2    Takakashi, H.3    Dyson, M.R.4    Zhao, S.5    Crowther, R.A.6    Murray, K.7
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 0030949436 scopus 로고    scopus 로고
    • Folding and assembly of hepatitis B virus core protein: a new model proposal
    • Bringas R. Folding and assembly of hepatitis B virus core protein: a new model proposal. J. Struct. Biol. 118 (1997) 189-196
    • (1997) J. Struct. Biol. , vol.118 , pp. 189-196
    • Bringas, R.1
  • 5
    • 0018760172 scopus 로고
    • Expression in Escherichia coli of hepatitis B virus DNA sequences cloned in plasmid pBR322
    • Burrell C.J., MacKay P., Greenaway P.J., Hofschneider P.-H., and Murray K. Expression in Escherichia coli of hepatitis B virus DNA sequences cloned in plasmid pBR322. Nature 279 (1979) 43-47
    • (1979) Nature , vol.279 , pp. 43-47
    • Burrell, C.J.1    MacKay, P.2    Greenaway, P.J.3    Hofschneider, P.-H.4    Murray, K.5
  • 6
    • 0027513977 scopus 로고
    • Opening and refolding of simian virus 40 and in vitro packaging of foreign DNA
    • Colomar M.C., Degoumois-Sahli C., and Beard P. Opening and refolding of simian virus 40 and in vitro packaging of foreign DNA. J. Virol. 67 (1993) 2779-2786
    • (1993) J. Virol. , vol.67 , pp. 2779-2786
    • Colomar, M.C.1    Degoumois-Sahli, C.2    Beard, P.3
  • 7
    • 0028307177 scopus 로고
    • Three-dimensional structure of hepatitis B virus core particles determined by electron cryomicroscopy
    • Crowther R.A., Kiselev N.A., Böttcher B., Berriman J.A., Borisova G.P., Ose V., and Pumpens P. Three-dimensional structure of hepatitis B virus core particles determined by electron cryomicroscopy. Cell 77 (1994) 943-950
    • (1994) Cell , vol.77 , pp. 943-950
    • Crowther, R.A.1    Kiselev, N.A.2    Böttcher, B.3    Berriman, J.A.4    Borisova, G.P.5    Ose, V.6    Pumpens, P.7
  • 8
    • 0014932016 scopus 로고
    • Virus-like particles in serum of patients with Australia antigen-associated hepatitis
    • Dane D.S., Cameron C.H., and Briggs M. Virus-like particles in serum of patients with Australia antigen-associated hepatitis. Lancet 295 (1970) 695-698
    • (1970) Lancet , vol.295 , pp. 695-698
    • Dane, D.S.1    Cameron, C.H.2    Briggs, M.3
  • 9
    • 0025782903 scopus 로고
    • Assembly of hepadnaviral virions and subviral particles
    • Ganem D. Assembly of hepadnaviral virions and subviral particles. Curr. Topics Microbiol. Immunol. 168 (1991) 61-83
    • (1991) Curr. Topics Microbiol. Immunol. , vol.168 , pp. 61-83
    • Ganem, D.1
  • 10
    • 0036461318 scopus 로고    scopus 로고
    • Immunology of hepatitis B infection
    • Jung M.-C., and Pape G.R. Immunology of hepatitis B infection. Lancet Infect. Dis. 2 (2002) 43-50
    • (2002) Lancet Infect. Dis. , vol.2 , pp. 43-50
    • Jung, M.-C.1    Pape, G.R.2
  • 11
    • 0033514992 scopus 로고    scopus 로고
    • Native display of complete foreign protein domains on the surface of hepatitis B virus capsids
    • Kratz P.A., Böttcher B., and Nassal M. Native display of complete foreign protein domains on the surface of hepatitis B virus capsids. Proc. Natl. Acad. Sci. U.S.A. 96 (1999) 1915-1920
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 1915-1920
    • Kratz, P.A.1    Böttcher, B.2    Nassal, M.3
  • 12
    • 0038547689 scopus 로고    scopus 로고
    • Hepatitis B virus assembly is sensitive to changes in the cytosolic S loop of the envelope proteins
    • Löffler-Mary H., Dumortier J., Klentsch-Zimmer C., and Prange R. Hepatitis B virus assembly is sensitive to changes in the cytosolic S loop of the envelope proteins. Virology 270 (2000) 358-367
    • (2000) Virology , vol.270 , pp. 358-367
    • Löffler-Mary, H.1    Dumortier, J.2    Klentsch-Zimmer, C.3    Prange, R.4
  • 14
    • 34047107374 scopus 로고    scopus 로고
    • Human papillomavirus-like particles mediate functional delivery of plasmid DNA to antigen presenting cells in vivo
    • Malboeuf C.M., Simon D.A.L., Lee Y.-E.E., Lankes H.A., Dewhurst S., Frelinger J.G., and Rose R.C. Human papillomavirus-like particles mediate functional delivery of plasmid DNA to antigen presenting cells in vivo. Vaccine 25 (2007) 3270-3276
    • (2007) Vaccine , vol.25 , pp. 3270-3276
    • Malboeuf, C.M.1    Simon, D.A.L.2    Lee, Y.-E.E.3    Lankes, H.A.4    Dewhurst, S.5    Frelinger, J.G.6    Rose, R.C.7
  • 15
    • 0033760886 scopus 로고    scopus 로고
    • Gene transfer using recombinant rabbit hemorrhagic disease virus capsids with genetically modified DNA encapsidation capacity by addition of packaging sequences from the L1 or L2 protein of human papillomavirus type 16
    • Mehdaoui S.E., Touze A., Laurent S., Sizaret P.-Y., Rasschaert D., and Coursaget P. Gene transfer using recombinant rabbit hemorrhagic disease virus capsids with genetically modified DNA encapsidation capacity by addition of packaging sequences from the L1 or L2 protein of human papillomavirus type 16. J. Virol. 74 (2000) 10332-10340
    • (2000) J. Virol. , vol.74 , pp. 10332-10340
    • Mehdaoui, S.E.1    Touze, A.2    Laurent, S.3    Sizaret, P.-Y.4    Rasschaert, D.5    Coursaget, P.6
  • 16
    • 0033042257 scopus 로고    scopus 로고
    • The core antigen of hepatitis B virus as a carrier for immunogenic peptides
    • Murray K., and Shiau A.L. The core antigen of hepatitis B virus as a carrier for immunogenic peptides. Biol. Chem. 380 (1999) 277-283
    • (1999) Biol. Chem. , vol.380 , pp. 277-283
    • Murray, K.1    Shiau, A.L.2
  • 17
    • 0026684254 scopus 로고
    • Topological analysis of the hepatitis B virus core particle by cysteine-cysteine cross-linking
    • Nassal M., Rieger A., and Steinau O. Topological analysis of the hepatitis B virus core particle by cysteine-cysteine cross-linking. J. Mol. Biol. 225 (1992) 1013-1025
    • (1992) J. Mol. Biol. , vol.225 , pp. 1013-1025
    • Nassal, M.1    Rieger, A.2    Steinau, O.3
  • 18
    • 36749022937 scopus 로고    scopus 로고
    • Development of hepatitis B virus capsids into a whole-chain protein antigen display platform: new particulate Lyme disease vaccines
    • Nassal M., Skamel C., Vogel M., Kratz P.A., Stehle T., Wallich R., and Simon M.M. Development of hepatitis B virus capsids into a whole-chain protein antigen display platform: new particulate Lyme disease vaccines. Int. J. Med. Microbiol. 298 (2008) 135-142
    • (2008) Int. J. Med. Microbiol. , vol.298 , pp. 135-142
    • Nassal, M.1    Skamel, C.2    Vogel, M.3    Kratz, P.A.4    Stehle, T.5    Wallich, R.6    Simon, M.M.7
  • 20
    • 0344304690 scopus 로고    scopus 로고
    • Stability and morphology comparisons of self-assembled virus-like particles from wild-type and mutant human hepatitis B virus capsid proteins
    • Newman M., Suk F.-M., Cajimat M., Chua P.K., and Shih C. Stability and morphology comparisons of self-assembled virus-like particles from wild-type and mutant human hepatitis B virus capsid proteins. Virology 77 (2003) 12950-12960
    • (2003) Virology , vol.77 , pp. 12950-12960
    • Newman, M.1    Suk, F.-M.2    Cajimat, M.3    Chua, P.K.4    Shih, C.5
  • 21
    • 0034889864 scopus 로고    scopus 로고
    • HBV core particles as a carrier for B cell/T cell epitopes
    • Pumpens P., and Grens E. HBV core particles as a carrier for B cell/T cell epitopes. Intervirology 44 (2001) 98-114
    • (2001) Intervirology , vol.44 , pp. 98-114
    • Pumpens, P.1    Grens, E.2
  • 23
    • 34648846409 scopus 로고    scopus 로고
    • Cryo-electron microscopy of hepatitis B virions reveals variability in envelope capsid interactions
    • Seitz S., Urban S., Antoni C., and Böttcher B. Cryo-electron microscopy of hepatitis B virions reveals variability in envelope capsid interactions. EMBO J. 26 (2007) 4160-4167
    • (2007) EMBO J. , vol.26 , pp. 4160-4167
    • Seitz, S.1    Urban, S.2    Antoni, C.3    Böttcher, B.4
  • 24
    • 33745223883 scopus 로고    scopus 로고
    • Hepatitis B virus capsid-like particles can display the complete, dimeric outer surface protein C and stimulate production of protective antibody responses against Borrelia burgdorferi infection
    • Skamel C., Ploss M., Böttcher B., Stehle T., Wallich R., Simon M.M., and Nassal M. Hepatitis B virus capsid-like particles can display the complete, dimeric outer surface protein C and stimulate production of protective antibody responses against Borrelia burgdorferi infection. J. Biol. Chem. 281 (2006) 17474-17481
    • (2006) J. Biol. Chem. , vol.281 , pp. 17474-17481
    • Skamel, C.1    Ploss, M.2    Böttcher, B.3    Stehle, T.4    Wallich, R.5    Simon, M.M.6    Nassal, M.7
  • 25
    • 0033605211 scopus 로고    scopus 로고
    • Two distinct segments of the hepatitis B virus surface antigen contribute synergistically to its association with the viral core particles
    • Tan W.S., Dyson M.R., and Murray K. Two distinct segments of the hepatitis B virus surface antigen contribute synergistically to its association with the viral core particles. J. Mol. Biol. 286 (1999) 797-808
    • (1999) J. Mol. Biol. , vol.286 , pp. 797-808
    • Tan, W.S.1    Dyson, M.R.2    Murray, K.3
  • 26
    • 0038405161 scopus 로고    scopus 로고
    • Hepatitis B virus core antigen: enhancement of its production in Escherichia coli, and interaction of the core particles with the viral surface antigen
    • Tan W.S., Dyson M.R., and Murray K. Hepatitis B virus core antigen: enhancement of its production in Escherichia coli, and interaction of the core particles with the viral surface antigen. Biol. Chem. 384 (2003) 363-371
    • (2003) Biol. Chem. , vol.384 , pp. 363-371
    • Tan, W.S.1    Dyson, M.R.2    Murray, K.3
  • 27
    • 34547625178 scopus 로고    scopus 로고
    • Crystallization and X-ray analysis of the T = 4 particle of hepatitis B capsid protein with an N-terminal extension
    • Tan W.S., McNae L.W., Ho K.L., and Walkinshaw M.D. Crystallization and X-ray analysis of the T = 4 particle of hepatitis B capsid protein with an N-terminal extension. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. F63 (2007) 642-647
    • (2007) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. , vol.F63 , pp. 642-647
    • Tan, W.S.1    McNae, L.W.2    Ho, K.L.3    Walkinshaw, M.D.4
  • 28
    • 0032030315 scopus 로고    scopus 로고
    • In vitro gene transfer using human papillomavirus-like particles
    • Touze A., and Coursaget P. In vitro gene transfer using human papillomavirus-like particles. Nucleic Acids Res. 26 (1998) 1317-1323
    • (1998) Nucleic Acids Res. , vol.26 , pp. 1317-1323
    • Touze, A.1    Coursaget, P.2
  • 29
    • 24944542799 scopus 로고    scopus 로고
    • In vitro assembly of mosaic hepatitis B virus capsid-like particles (CLPs): rescue into CLPs of assembly-deficient core protein fusions and FRET-suited CLPs
    • Vogel M., Diez M., Eisfeld J., and Nassal M. In vitro assembly of mosaic hepatitis B virus capsid-like particles (CLPs): rescue into CLPs of assembly-deficient core protein fusions and FRET-suited CLPs. FEBS Lett. 579 (2005) 5211-5216
    • (2005) FEBS Lett. , vol.579 , pp. 5211-5216
    • Vogel, M.1    Diez, M.2    Eisfeld, J.3    Nassal, M.4
  • 30
    • 0028953769 scopus 로고
    • Hepatitis core antigen produced in Escherichia coli: subunit composition, conformational analysis, and in vitro capsid assembly
    • Wingfield P.T., Stahl S.J., Williams R.W., and Steven A.C. Hepatitis core antigen produced in Escherichia coli: subunit composition, conformational analysis, and in vitro capsid assembly. Biochemistry 34 (1995) 4919-4932
    • (1995) Biochemistry , vol.34 , pp. 4919-4932
    • Wingfield, P.T.1    Stahl, S.J.2    Williams, R.W.3    Steven, A.C.4
  • 31
    • 0033152857 scopus 로고    scopus 로고
    • The crystal structure of the human hepatitis B virus capsid
    • Wynne S.A., Crowther R.A., and Leslie A.G. The crystal structure of the human hepatitis B virus capsid. Mol. Cell 3 (1999) 771-780
    • (1999) Mol. Cell , vol.3 , pp. 771-780
    • Wynne, S.A.1    Crowther, R.A.2    Leslie, A.G.3
  • 32
    • 0031918760 scopus 로고    scopus 로고
    • 1 under denaturants guanidine hydrochloride and urea
    • 1 under denaturants guanidine hydrochloride and urea. Int. J. Biol. Macromol. 22 (1998) 81-90
    • (1998) Int. J. Biol. Macromol. , vol.22 , pp. 81-90
    • Yang, Y.-W.1    Teng, C.-C.2
  • 33
    • 0026793044 scopus 로고
    • The structure of Hepadnaviral core antigens: identification of free thiols and determination of the disulfide bonding pattern
    • Zheng J., Schödel F., and Peterson D.L. The structure of Hepadnaviral core antigens: identification of free thiols and determination of the disulfide bonding pattern. J. Biol. Chem. 267 (1992) 9422-9428
    • (1992) J. Biol. Chem. , vol.267 , pp. 9422-9428
    • Zheng, J.1    Schödel, F.2    Peterson, D.L.3
  • 34
    • 0033517792 scopus 로고    scopus 로고
    • A theoretical model successfully identifies features of hepatitis B virus capsid assembly
    • Zlotnick A., Johnson J.M., Wingfield P.W., Stahl S.J., and Endres D. A theoretical model successfully identifies features of hepatitis B virus capsid assembly. Biochemistry 38 (1999) 14644-14652
    • (1999) Biochemistry , vol.38 , pp. 14644-14652
    • Zlotnick, A.1    Johnson, J.M.2    Wingfield, P.W.3    Stahl, S.J.4    Endres, D.5


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