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Volumn 298, Issue 1-2, 2008, Pages 135-142

Development of hepatitis B virus capsids into a whole-chain protein antigen display platform: New particulate Lyme disease vaccines

Author keywords

Adjuvant; Capsid like particles; HBcAG; Lyme borreliosis; Osp vaccine; Particulate carrier

Indexed keywords

BACTERIAL PROTEIN; CAPSID PROTEIN; DIMER; EPITOPE; IMMUNOGLOBULIN CLASS; LYME DISEASE VACCINE; NANOPARTICLE; OUTER SURFACE PROTEIN A; PROTEIN OSPC; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG; VIRUS ANTIGEN; VIRUS PROTEIN;

EID: 36749022937     PISSN: 14384221     EISSN: 16180607     Source Type: Journal    
DOI: 10.1016/j.ijmm.2007.08.002     Document Type: Short Survey
Times cited : (38)

References (70)
  • 3
    • 0036892173 scopus 로고    scopus 로고
    • A modified hepatitis B virus core particle containing multiple epitopes of the Plasmodium falciparum circumsporozoite protein provides a highly immunogenic malaria vaccine in preclinical analyses in rodent and primate hosts
    • Birkett A., Lyons K., Schmidt A., Boyd D., Oliveira G.A., Siddique A., Nussenzweig R., Calvo-Calle J.M., and Nardin E. A modified hepatitis B virus core particle containing multiple epitopes of the Plasmodium falciparum circumsporozoite protein provides a highly immunogenic malaria vaccine in preclinical analyses in rodent and primate hosts. Infect. Immun. 70 (2002) 6860-6870
    • (2002) Infect. Immun. , vol.70 , pp. 6860-6870
    • Birkett, A.1    Lyons, K.2    Schmidt, A.3    Boyd, D.4    Oliveira, G.A.5    Siddique, A.6    Nussenzweig, R.7    Calvo-Calle, J.M.8    Nardin, E.9
  • 4
    • 0025316017 scopus 로고
    • Hepatitis B virus nucleocapsid assembly: primary structure requirements in the core protein
    • Birnbaum F., and Nassal M. Hepatitis B virus nucleocapsid assembly: primary structure requirements in the core protein. J. Virol. 64 (1990) 3319-3330
    • (1990) J. Virol. , vol.64 , pp. 3319-3330
    • Birnbaum, F.1    Nassal, M.2
  • 5
    • 0030740450 scopus 로고    scopus 로고
    • Hepatitis B virus, the vaccine, and the control of primary cancer of the liver
    • Blumberg B.S. Hepatitis B virus, the vaccine, and the control of primary cancer of the liver. Proc. Natl. Acad. Sci. USA 94 (1997) 7121-7125
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 7121-7125
    • Blumberg, B.S.1
  • 6
    • 1842409555 scopus 로고    scopus 로고
    • Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy
    • Böttcher B., Wynne S.A., and Crowther R.A. Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy. Nature 386 (1997) 88-91
    • (1997) Nature , vol.386 , pp. 88-91
    • Böttcher, B.1    Wynne, S.A.2    Crowther, R.A.3
  • 7
    • 31344442517 scopus 로고    scopus 로고
    • High plasticity of the hepatitis B virus capsid revealed by conformational stress
    • Böttcher B., Vogel M., Ploss M., and Nassal M. High plasticity of the hepatitis B virus capsid revealed by conformational stress. J. Mol. Biol. 356 (2006) 812-822
    • (2006) J. Mol. Biol. , vol.356 , pp. 812-822
    • Böttcher, B.1    Vogel, M.2    Ploss, M.3    Nassal, M.4
  • 8
    • 0034984750 scopus 로고    scopus 로고
    • Hepatitis B virus core antigen binds and activates naive human B cells in vivo: studies with a human PBL-NOD/SCID mouse model
    • Cao T., Lazdina U., Desombere I., Vanlandschoot P., Milich D.R., Sällberg M., and Leroux-Roels G. Hepatitis B virus core antigen binds and activates naive human B cells in vivo: studies with a human PBL-NOD/SCID mouse model. J. Virol. 75 (2001) 6359-6366
    • (2001) J. Virol. , vol.75 , pp. 6359-6366
    • Cao, T.1    Lazdina, U.2    Desombere, I.3    Vanlandschoot, P.4    Milich, D.R.5    Sällberg, M.6    Leroux-Roels, G.7
  • 9
    • 0028916425 scopus 로고
    • Hepatitis B virus immunopathogenesis
    • Chisari F.V., and Ferrari C. Hepatitis B virus immunopathogenesis. Annu. Rev. Immunol. 13 (1995) 29-60
    • (1995) Annu. Rev. Immunol. , vol.13 , pp. 29-60
    • Chisari, F.V.1    Ferrari, C.2
  • 11
    • 0030937751 scopus 로고    scopus 로고
    • Visualization of a 4-helix bundle in the hepatitis B virus capsid by cryo-electron microscopy
    • Conway J.F., Cheng N., Zlotnick A., Wingfield P.T., Stahl S.J., and Steven A.C. Visualization of a 4-helix bundle in the hepatitis B virus capsid by cryo-electron microscopy. Nature 386 (1997) 91-94
    • (1997) Nature , vol.386 , pp. 91-94
    • Conway, J.F.1    Cheng, N.2    Zlotnick, A.3    Wingfield, P.T.4    Stahl, S.J.5    Steven, A.C.6
  • 12
    • 0032568864 scopus 로고    scopus 로고
    • Hepatitis B virus capsid: localization of the putative immunodominant loop (residues 78-83) on the capsid surface, and implications for the distinction between c and e-antigens
    • Conway J.F., Cheng N., Zlotnick A., Stahl S.J., Wingfield P.T., Belnap D.M., Kanngiesser U., Noah M., and Steven A.C. Hepatitis B virus capsid: localization of the putative immunodominant loop (residues 78-83) on the capsid surface, and implications for the distinction between c and e-antigens. J. Mol. Biol. 279 (1998) 1111-1121
    • (1998) J. Mol. Biol. , vol.279 , pp. 1111-1121
    • Conway, J.F.1    Cheng, N.2    Zlotnick, A.3    Stahl, S.J.4    Wingfield, P.T.5    Belnap, D.M.6    Kanngiesser, U.7    Noah, M.8    Steven, A.C.9
  • 13
    • 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
  • 14
    • 0030025949 scopus 로고    scopus 로고
    • Borrelia burgdorferi OspA is an arthropod-specific transmission-blocking Lyme disease vaccine
    • de Silva A.M., Telford III S.R., Brunet L.R., Barthold S.W., and Fikrig E. Borrelia burgdorferi OspA is an arthropod-specific transmission-blocking Lyme disease vaccine. J. Exp. Med. 183 (1996) 271-275
    • (1996) J. Exp. Med. , vol.183 , pp. 271-275
    • de Silva, A.M.1    Telford III, S.R.2    Brunet, L.R.3    Barthold, S.W.4    Fikrig, E.5
  • 16
    • 0032482985 scopus 로고    scopus 로고
    • T cell-independent type I antibody response against B cell epitopes expressed repetitively on recombinant virus particles
    • Fehr T., Skrastina D., Pumpens P., and Zinkernagel R.M. T cell-independent type I antibody response against B cell epitopes expressed repetitively on recombinant virus particles. Proc. Natl. Acad. Sci. USA 95 (1998) 9477-9481
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 9477-9481
    • Fehr, T.1    Skrastina, D.2    Pumpens, P.3    Zinkernagel, R.M.4
  • 17
    • 0025202254 scopus 로고
    • Protection of mice against the Lyme disease agent by immunizing with recombinant OspA
    • Fikrig E., Barthold S.W., Kantor F.S., and Flavell R.A. Protection of mice against the Lyme disease agent by immunizing with recombinant OspA. Science 250 (1990) 553-556
    • (1990) Science , vol.250 , pp. 553-556
    • Fikrig, E.1    Barthold, S.W.2    Kantor, F.S.3    Flavell, R.A.4
  • 18
    • 0034657179 scopus 로고    scopus 로고
    • Arthropod- and host-specific Borrelia burgdorferi bbk32 expression and the inhibition of spirochete transmission
    • Fikrig E., Feng W., Barthold S.W., Telford III S.R., and Flavell R.A. Arthropod- and host-specific Borrelia burgdorferi bbk32 expression and the inhibition of spirochete transmission. J. Immunol. 164 (2000) 5344-5351
    • (2000) J. Immunol. , vol.164 , pp. 5344-5351
    • Fikrig, E.1    Feng, W.2    Barthold, S.W.3    Telford III, S.R.4    Flavell, R.A.5
  • 20
    • 0028593448 scopus 로고
    • The outer surface protein A of the spirochete Borrelia burgdorferi is a plasmin(ogen) receptor
    • Fuchs H., Wallich R., Simon M.M., and Kramer M.D. The outer surface protein A of the spirochete Borrelia burgdorferi is a plasmin(ogen) receptor. Proc. Natl. Acad. Sci. USA 91 (1994) 12594-12598
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12594-12598
    • Fuchs, H.1    Wallich, R.2    Simon, M.M.3    Kramer, M.D.4
  • 21
    • 19444386577 scopus 로고    scopus 로고
    • A hantavirus nucleocapsid protein segment exposed on hepatitis B virus core particles is highly immunogenic in mice when applied without adjuvants or in the presence of pre-existing anti-core antibodies
    • Geldmacher A., Skrastina D., Borisova G., Petrovskis I., Krüger D.H., Pumpens P., and Ulrich R. A hantavirus nucleocapsid protein segment exposed on hepatitis B virus core particles is highly immunogenic in mice when applied without adjuvants or in the presence of pre-existing anti-core antibodies. Vaccine 23 (2005) 3973-3983
    • (2005) Vaccine , vol.23 , pp. 3973-3983
    • Geldmacher, A.1    Skrastina, D.2    Borisova, G.3    Petrovskis, I.4    Krüger, D.H.5    Pumpens, P.6    Ulrich, R.7
  • 22
    • 33748794562 scopus 로고    scopus 로고
    • Virus-like particles: passport to immune recognition
    • Grgacic E.V., and Anderson D.A. Virus-like particles: passport to immune recognition. Methods 40 (2006) 60-65
    • (2006) Methods , vol.40 , pp. 60-65
    • Grgacic, E.V.1    Anderson, D.A.2
  • 25
    • 0029645618 scopus 로고
    • Evolutionary conservation in the hepatitis B virus core structure: comparison of human and duck cores
    • Kenney J.M., von Bonsdorff C.H., Nassal M., and Fuller S.D. Evolutionary conservation in the hepatitis B virus core structure: comparison of human and duck cores. Structure 3 (1995) 1009-1019
    • (1995) Structure , vol.3 , pp. 1009-1019
    • Kenney, J.M.1    von Bonsdorff, C.H.2    Nassal, M.3    Fuller, S.D.4
  • 26
    • 0032970891 scopus 로고    scopus 로고
    • HBV core particles allow the insertion and surface exposure of the entire potentially protective region of Puumala hantavirus nucleocapsid protein
    • Koletzki D., Biel S.S., Meisel H., Nugel E., Gelderblom H.R., Krüger D.H., and Ulrich R. HBV core particles allow the insertion and surface exposure of the entire potentially protective region of Puumala hantavirus nucleocapsid protein. Biol. Chem. 380 (1999) 325-333
    • (1999) Biol. Chem. , vol.380 , pp. 325-333
    • Koletzki, D.1    Biel, S.S.2    Meisel, H.3    Nugel, E.4    Gelderblom, H.R.5    Krüger, D.H.6    Ulrich, R.7
  • 27
    • 0034715573 scopus 로고    scopus 로고
    • Puumala (PUU) hantavirus strain differences and insertion positions in the hepatitis B virus core antigen influence B-cell immunogenicity and protective potential of core-derived particles
    • Koletzki D., Lundkvist A., Sjolander K.B., Gelderblom H.R., Niedrig M., Meisel H., Krüger D.H., and Ulrich R. Puumala (PUU) hantavirus strain differences and insertion positions in the hepatitis B virus core antigen influence B-cell immunogenicity and protective potential of core-derived particles. Virology 276 (2000) 364-375
    • (2000) Virology , vol.276 , pp. 364-375
    • Koletzki, D.1    Lundkvist, A.2    Sjolander, K.B.3    Gelderblom, H.R.4    Niedrig, M.5    Meisel, H.6    Krüger, D.H.7    Ulrich, R.8
  • 29
    • 1642535449 scopus 로고    scopus 로고
    • Complement resistance of Borrelia burgdorferi correlates with the expression of BbCRASP-1, a novel linear plasmid-encoded surface protein that interacts with human factor H and FHL-1 and is unrelated to Erp proteins
    • Kraiczy P., Hellwage J., Skerka C., Becker H., Kirschfink M., Simon M.M., Brade V., Zipfel P.F., and Wallich R. Complement resistance of Borrelia burgdorferi correlates with the expression of BbCRASP-1, a novel linear plasmid-encoded surface protein that interacts with human factor H and FHL-1 and is unrelated to Erp proteins. J. Biol. Chem. 279 (2004) 2421-2429
    • (2004) J. Biol. Chem. , vol.279 , pp. 2421-2429
    • Kraiczy, P.1    Hellwage, J.2    Skerka, C.3    Becker, H.4    Kirschfink, M.5    Simon, M.M.6    Brade, V.7    Zipfel, P.F.8    Wallich, R.9
  • 30
    • 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. USA 96 (1999) 1915-1920
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 1915-1920
    • Kratz, P.A.1    Böttcher, B.2    Nassal, M.3
  • 31
    • 0035283085 scopus 로고    scopus 로고
    • Crystal structure of outer surface protein C (OspC) from the Lyme disease spirochete, Borrelia burgdorferi
    • Kumaran D., Eswaramoorthy S., Luft B.J., Koide S., Dunn J.J., Lawson C.L., and Swaminathan S. Crystal structure of outer surface protein C (OspC) from the Lyme disease spirochete, Borrelia burgdorferi. EMBO J. 20 (2001) 971-978
    • (2001) EMBO J. , vol.20 , pp. 971-978
    • Kumaran, D.1    Eswaramoorthy, S.2    Luft, B.J.3    Koide, S.4    Dunn, J.J.5    Lawson, C.L.6    Swaminathan, S.7
  • 32
    • 0034979137 scopus 로고    scopus 로고
    • Molecular basis for the interaction of the hepatitis B virus core antigen with the surface immunoglobulin receptor on naive B cells
    • Lazdina U., Cao T., Steinbergs J., Alheim M., Pumpens P., Peterson D.L., Milich D.R., Leroux-Roels G., and Sällberg M. Molecular basis for the interaction of the hepatitis B virus core antigen with the surface immunoglobulin receptor on naive B cells. J. Virol. 75 (2001) 6367-6374
    • (2001) J. Virol. , vol.75 , pp. 6367-6374
    • Lazdina, U.1    Cao, T.2    Steinbergs, J.3    Alheim, M.4    Pumpens, P.5    Peterson, D.L.6    Milich, D.R.7    Leroux-Roels, G.8    Sällberg, M.9
  • 34
    • 0030932886 scopus 로고    scopus 로고
    • Crystal structure of Lyme disease antigen outer surface protein A complexed with an Fab
    • Li H., Dunn J.J., Luft B.J., and Lawson C.L. Crystal structure of Lyme disease antigen outer surface protein A complexed with an Fab. Proc. Natl. Acad. Sci. USA 94 (1997) 3584-3589
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3584-3589
    • Li, H.1    Dunn, J.J.2    Luft, B.J.3    Lawson, C.L.4
  • 35
    • 0027537039 scopus 로고
    • Transcriptional analyses and mapping of the ospC gene in Lyme disease spirochetes
    • Marconi R.T., Samuels D.S., and Garon C.F. Transcriptional analyses and mapping of the ospC gene in Lyme disease spirochetes. J. Bacteriol. 175 (1993) 926-932
    • (1993) J. Bacteriol. , vol.175 , pp. 926-932
    • Marconi, R.T.1    Samuels, D.S.2    Garon, C.F.3
  • 36
    • 0022996325 scopus 로고
    • The nucleocapsid of hepatitis B virus is both a T-cell-independent and a T-cell-dependent antigen
    • Milich D.R., and McLachlan A. The nucleocapsid of hepatitis B virus is both a T-cell-independent and a T-cell-dependent antigen. Science 234 (1986) 1398-1401
    • (1986) Science , vol.234 , pp. 1398-1401
    • Milich, D.R.1    McLachlan, A.2
  • 38
    • 0023902532 scopus 로고
    • Total chemical synthesis of a gene for hepatitis B virus core protein and its functional characterization
    • Nassal M. Total chemical synthesis of a gene for hepatitis B virus core protein and its functional characterization. Gene 66 (1988) 279-294
    • (1988) Gene , vol.66 , pp. 279-294
    • Nassal, M.1
  • 39
    • 0026695732 scopus 로고
    • The arginine-rich domain of the hepatitis B virus core protein is required for pregenome encapsidation and productive viral positive-strand DNA synthesis but not for virus assembly
    • Nassal M. The arginine-rich domain of the hepatitis B virus core protein is required for pregenome encapsidation and productive viral positive-strand DNA synthesis but not for virus assembly. J. Virol. 66 (1992) 4107-4116
    • (1992) J. Virol. , vol.66 , pp. 4107-4116
    • Nassal, M.1
  • 40
    • 0032845490 scopus 로고    scopus 로고
    • Hepatitis B virus replication: novel roles for virus-host interactions
    • Nassal M. Hepatitis B virus replication: novel roles for virus-host interactions. Intervirology 42 (1999) 100-116
    • (1999) Intervirology , vol.42 , pp. 100-116
    • Nassal, M.1
  • 41
    • 0001903859 scopus 로고    scopus 로고
    • Macromolecular interactions in hepatitis B virus replication and particle assembly
    • Cann A.J. (Ed), Oxford University Press, Oxford, UK
    • Nassal M. Macromolecular interactions in hepatitis B virus replication and particle assembly. In: Cann A.J. (Ed). DNA Virus Replication. Frontiers in Molecular Biology (2000), Oxford University Press, Oxford, UK 1-40
    • (2000) DNA Virus Replication. Frontiers in Molecular Biology , pp. 1-40
    • Nassal, M.1
  • 42
    • 14744292190 scopus 로고    scopus 로고
    • A fusion product of the complete Borrelia burgdorferi outer surface protein A (OspA) and the hepatitis B virus capsid protein is highly immunogenic and induces protective immunity similar to that seen with an effective lipidated OspA vaccine formula
    • Nassal M., Skamel C., Kratz P.A., Wallich R., Stehle T., and Simon M.M. A fusion product of the complete Borrelia burgdorferi outer surface protein A (OspA) and the hepatitis B virus capsid protein is highly immunogenic and induces protective immunity similar to that seen with an effective lipidated OspA vaccine formula. Eur. J. Immunol. 35 (2005) 655-665
    • (2005) Eur. J. Immunol. , vol.35 , pp. 655-665
    • Nassal, M.1    Skamel, C.2    Kratz, P.A.3    Wallich, R.4    Stehle, T.5    Simon, M.M.6
  • 43
    • 0042825878 scopus 로고    scopus 로고
    • Virus-like particles as immunogens
    • Noad R., and Roy P. Virus-like particles as immunogens. Trends Microbiol. 11 (2003) 438-444
    • (2003) Trends Microbiol. , vol.11 , pp. 438-444
    • Noad, R.1    Roy, P.2
  • 44
  • 45
    • 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
  • 47
    • 0024500103 scopus 로고
    • Antigenic determinants and functional domains in core antigen and e antigen from hepatitis B virus
    • Salfeld J., Pfaff E., Noah M., and Schaller H. Antigenic determinants and functional domains in core antigen and e antigen from hepatitis B virus. J. Virol. 63 (1989) 798-808
    • (1989) J. Virol. , vol.63 , pp. 798-808
    • Salfeld, J.1    Pfaff, E.2    Noah, M.3    Schaller, H.4
  • 48
    • 0036986329 scopus 로고    scopus 로고
    • A malaria vaccine candidate based on a hepatitis B virus core platform
    • Sällberg M., Hughes J., Jones J., Phillips T.R., and Milich D.R. A malaria vaccine candidate based on a hepatitis B virus core platform. Intervirology 45 (2002) 350-361
    • (2002) Intervirology , vol.45 , pp. 350-361
    • Sällberg, M.1    Hughes, J.2    Jones, J.3    Phillips, T.R.4    Milich, D.R.5
  • 49
    • 0025333897 scopus 로고
    • Monoclonal antibodies specific for the outer surface protein A (OspA) of Borrelia burgdorferi prevent Lyme borreliosis in severe combined immunodeficiency (scid) mice
    • Schaible U.E., Kramer M.D., Eichmann K., Modolell M., Museteanu C., and Simon M.M. Monoclonal antibodies specific for the outer surface protein A (OspA) of Borrelia burgdorferi prevent Lyme borreliosis in severe combined immunodeficiency (scid) mice. Proc. Natl. Acad. Sci. USA 87 (1990) 3768-3772
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 3768-3772
    • Schaible, U.E.1    Kramer, M.D.2    Eichmann, K.3    Modolell, M.4    Museteanu, C.5    Simon, M.M.6
  • 53
    • 0025949089 scopus 로고
    • Recombinant outer surface protein A from Borrelia burgdorferi induces antibodies protective against spirochetal infection in mice
    • Simon M.M., Schaible U.E., Kramer M.D., Eckerskorn C., Museteanu C., Müller-Hermelink H.K., and Wallich R. Recombinant outer surface protein A from Borrelia burgdorferi induces antibodies protective against spirochetal infection in mice. J. Infect. Dis. 164 (1991) 123-132
    • (1991) J. Infect. Dis. , vol.164 , pp. 123-132
    • Simon, M.M.1    Schaible, U.E.2    Kramer, M.D.3    Eckerskorn, C.4    Museteanu, C.5    Müller-Hermelink, H.K.6    Wallich, R.7
  • 54
    • 0029800616 scopus 로고    scopus 로고
    • Protective immunization with plasmid DNA containing the outer surface lipoprotein A gene of Borrelia burgdorferi is independent of an eukaryotic promoter
    • Simon M.M., Gern L., Hauser P., Zhong W., Nielsen P.J., Kramer M.D., Brenner C., and Wallich R. Protective immunization with plasmid DNA containing the outer surface lipoprotein A gene of Borrelia burgdorferi is independent of an eukaryotic promoter. Eur. J. Immunol. 26 (1996) 2831-2840
    • (1996) Eur. J. Immunol. , vol.26 , pp. 2831-2840
    • Simon, M.M.1    Gern, L.2    Hauser, P.3    Zhong, W.4    Nielsen, P.J.5    Kramer, M.D.6    Brenner, C.7    Wallich, R.8
  • 55
    • 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
  • 61
    • 0031606401 scopus 로고    scopus 로고
    • Core particles of hepatitis B virus as carrier for foreign epitopes
    • Ulrich R., Nassal M., Meisel H., and Krüger D.H. Core particles of hepatitis B virus as carrier for foreign epitopes. Adv. Virus Res. 50 (1998) 141-182
    • (1998) Adv. Virus Res. , vol.50 , pp. 141-182
    • Ulrich, R.1    Nassal, M.2    Meisel, H.3    Krüger, D.H.4
  • 63
    • 0030453699 scopus 로고    scopus 로고
    • Evaluation of the safety, reactogenicity and immunogenicity of three recombinant outer surface protein (OspA) lyme vaccines in healthy adults
    • Van Hoecke C., Comberbach M., De Grave D., Desmons P., Fu D., Hauser P., Lebacq E., Lobet Y., and Voet P. Evaluation of the safety, reactogenicity and immunogenicity of three recombinant outer surface protein (OspA) lyme vaccines in healthy adults. Vaccine 14 (1996) 1620-1626
    • (1996) Vaccine , vol.14 , pp. 1620-1626
    • Van Hoecke, C.1    Comberbach, M.2    De Grave, D.3    Desmons, P.4    Fu, D.5    Hauser, P.6    Lebacq, E.7    Lobet, Y.8    Voet, P.9
  • 64
    • 11344265923 scopus 로고    scopus 로고
    • Quaternary structure is critical for protein display on capsid-like particles (CLPs): efficient generation of hepatitis B virus CLPs presenting monomeric but not dimeric and tetrameric fluorescent proteins
    • Vogel M., Vorreiter J., and Nassal M. Quaternary structure is critical for protein display on capsid-like particles (CLPs): efficient generation of hepatitis B virus CLPs presenting monomeric but not dimeric and tetrameric fluorescent proteins. Proteins 58 (2005) 478-488
    • (2005) Proteins , vol.58 , pp. 478-488
    • Vogel, M.1    Vorreiter, J.2    Nassal, M.3
  • 65
    • 0029122852 scopus 로고
    • Molecular cloning and immunological characterization of a novel linear-plasmid-encoded gene, pG, of Borrelia burgdorferi expressed only in vivo
    • Wallich R., Brenner C., Kramer M.D., and Simon M.M. Molecular cloning and immunological characterization of a novel linear-plasmid-encoded gene, pG, of Borrelia burgdorferi expressed only in vivo. Infect. Immun. 63 (1995) 3327-3335
    • (1995) Infect. Immun. , vol.63 , pp. 3327-3335
    • Wallich, R.1    Brenner, C.2    Kramer, M.D.3    Simon, M.M.4
  • 66
    • 0036500146 scopus 로고    scopus 로고
    • The morphogenic linker peptide of HBV capsid protein forms a mobile array on the interior surface
    • Watts N.R., Conway J.F., Cheng N., Stahl S.J., Belnap D.M., Steven A.C., and Wingfield P.T. The morphogenic linker peptide of HBV capsid protein forms a mobile array on the interior surface. EMBO J. 21 (2002) 876-884
    • (2002) EMBO J. , vol.21 , pp. 876-884
    • Watts, N.R.1    Conway, J.F.2    Cheng, N.3    Stahl, S.J.4    Belnap, D.M.5    Steven, A.C.6    Wingfield, P.T.7
  • 67
    • 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
  • 68
    • 0030904280 scopus 로고    scopus 로고
    • Antigenic variation in Lyme disease borreliae by promiscuous recombination of VMP-like sequence cassettes
    • Zhang J.R., Hardham J.M., Barbour A.G., and Norris S.J. Antigenic variation in Lyme disease borreliae by promiscuous recombination of VMP-like sequence cassettes. Cell 89 (1997) 275-285
    • (1997) Cell , vol.89 , pp. 275-285
    • Zhang, J.R.1    Hardham, J.M.2    Barbour, A.G.3    Norris, S.J.4
  • 70
    • 0033060246 scopus 로고    scopus 로고
    • Resolution of experimental and tick-borne Borrelia burgdorferi infection in mice by passive, but not active immunization using recombinant OspC
    • Zhong W., Gern L., Stehle T., Museteanu C., Kramer M., Wallich R., and Simon M.M. Resolution of experimental and tick-borne Borrelia burgdorferi infection in mice by passive, but not active immunization using recombinant OspC. Eur. J. Immunol. 29 (1999) 946-957
    • (1999) Eur. J. Immunol. , vol.29 , pp. 946-957
    • Zhong, W.1    Gern, L.2    Stehle, T.3    Museteanu, C.4    Kramer, M.5    Wallich, R.6    Simon, M.M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.