메뉴 건너뛰기




Volumn 12, Issue 2, 2013, Pages 183-198

Hepatitis B core-based virus-like particles to present heterologous epitopes

Author keywords

arrayed epitope display; B cell immunity; hepatitis B virus; influenza; malaria; T cell immunity; virus like particles

Indexed keywords

ACAM FLU A; CARRIER PROTEIN; CC 1132; CIRCUMSPOROZOITE PROTEIN; EPITOPE; GLYCOPROTEIN; HEPATITIS B CORE ANTIGEN; HEPATITIS B SURFACE ANTIGEN; HEPATITIS B VACCINE; HYBRID PROTEIN; INFLUENZA VACCINE; INTERFERON; LAMIVUDINE; MALARIA VACCINE; MALARIAVAX; NEUTRALIZING ANTIBODY; RTS,S AS VACCINE; UNCLASSIFIED DRUG;

EID: 84874100999     PISSN: 14760584     EISSN: 17448395     Source Type: Journal    
DOI: 10.1586/erv.12.150     Document Type: Review
Times cited : (64)

References (170)
  • 2
    • 0002433747 scopus 로고
    • Viruses and Koch's Postulates
    • Rivers TM. Viruses and Koch's Postulates. J. Bacteriol. 33(1), 1-12 (1937).
    • (1937) J. Bacteriol. , vol.33 , Issue.1 , pp. 1-12
    • Rivers, T.M.1
  • 3
    • 76549181000 scopus 로고
    • A 'new' antigen in leukemia sera
    • Blumberg BS, Alter HJ, Visnich S. A 'new' antigen in leukemia sera. JAMA 191, 541-546 (1965).
    • (1965) JAMA , vol.191 , pp. 541-546
    • Blumberg, B.S.1    Alter, H.J.2    Visnich, S.3
  • 4
    • 0014376546 scopus 로고
    • Hepatitis and leukemia: Their relation to Australia antigen
    • Blumberg BS, Sutnick AI, London WT. Hepatitis and leukemia: their relation to Australia antigen. Bull. N. Y. Acad. Med. 44(12), 1566-1586 (1968).
    • (1968) Bull. N. Y. Acad. Med. , vol.44 , Issue.12 , pp. 1566-1586
    • Blumberg, B.S.1    Sutnick, A.I.2    London, W.T.3
  • 5
    • 0014307579 scopus 로고
    • An antigen detected in the blood during the incubation period of serum hepatitis
    • Prince AM. An antigen detected in the blood during the incubation period of serum hepatitis. Proc. Natl Acad. Sci. USA 60(3), 814-821 (1968).
    • (1968) Proc. Natl Acad. Sci. USA , vol.60 , Issue.3 , pp. 814-821
    • Prince, A.M.1
  • 6
    • 0026493753 scopus 로고
    • The reverse transcriptase of hepatitis B virus acts as a protein primer for viral DNA synthesis
    • Wang GH, Seeger C. The reverse transcriptase of hepatitis B virus acts as a protein primer for viral DNA synthesis. Cell 71(4), 663-670 (1992).
    • (1992) Cell , vol.71 , Issue.4 , pp. 663-670
    • Wang, G.H.1    Seeger, C.2
  • 7
    • 0028300388 scopus 로고
    • Hepadnavirus P protein utilizes a tyrosine residue in the TP domain to prime reverse transcription
    • Weber M, Bronsema V, Bartos H, Bosserhoff A, Bartenschlager R, Schaller H. Hepadnavirus P protein utilizes a tyrosine residue in the TP domain to prime reverse transcription. J. Virol. 68(5), 2994-2999 (1994).
    • (1994) J. Virol. , vol.68 , Issue.5 , pp. 2994-2999
    • Weber, M.1    Bronsema, V.2    Bartos, H.3    Bosserhoff, A.4    Bartenschlager, R.5    Schaller, H.6
  • 8
    • 0018956669 scopus 로고
    • Hepatitis B vaccine: Demonstration of efficacy in a controlled clinical trial in a high-risk population in the United States
    • Szmuness W, Stevens CE, Harley EJ et al. Hepatitis B vaccine: demonstration of efficacy in a controlled clinical trial in a high-risk population in the United States. N. Engl. J. Med. 303(15), 833-841 (1980).
    • (1980) N. Engl. J. Med. , vol.303 , Issue.15 , pp. 833-841
    • Szmuness, W.1    Stevens, C.E.2    Harley, E.J.3
  • 11
    • 0027293511 scopus 로고
    • Mutational analysis of the cysteine residues in the hepatitis B virus small envelope protein
    • Mangold CM, Streeck RE. Mutational analysis of the cysteine residues in the hepatitis B virus small envelope protein. J. Virol. 67(8), 4588-4597 (1993).
    • (1993) J. Virol. , vol.67 , Issue.8 , pp. 4588-4597
    • Mangold, C.M.1    Streeck, R.E.2
  • 12
    • 0023499809 scopus 로고
    • Immunogenicity of the gene S and Pre-S domains in hepatitis B virions and HBsAg filaments
    • Heermann KH, Kruse F, Seifer M, Gerlich WH. Immunogenicity of the gene S and Pre-S domains in hepatitis B virions and HBsAg filaments. Intervirology 28(1), 14-25 (1987).
    • (1987) Intervirology , vol.28 , Issue.1 , pp. 14-25
    • Heermann, K.H.1    Kruse, F.2    Seifer, M.3    Gerlich, W.H.4
  • 13
    • 0022538381 scopus 로고
    • Identification and chemical synthesis of a host cell receptor binding site on hepatitis B virus
    • Neurath AR, Kent SB, Strick N, Parker K. Identification and chemical synthesis of a host cell receptor binding site on hepatitis B virus. Cell 46(3), 429-436 (1986).
    • (1986) Cell , vol.46 , Issue.3 , pp. 429-436
    • Neurath, A.R.1    Kent, S.B.2    Strick, N.3    Parker, K.4
  • 14
    • 75449106643 scopus 로고    scopus 로고
    • Fine mapping of pre-S sequence requirements for hepatitis B virus large envelope protein-mediated receptor interaction
    • Schulze A, Schieck A, Ni Y, Mier W, Urban S. Fine mapping of pre-S sequence requirements for hepatitis B virus large envelope protein-mediated receptor interaction. J. Virol. 84(4), 1989-2000 (2010).
    • (2010) J. Virol. , vol.84 , Issue.4 , pp. 1989-2000
    • Schulze, A.1    Schieck, A.2    Ni, Y.3    Mier, W.4    Urban, S.5
  • 15
    • 0024429037 scopus 로고
    • The preS1 antigen of hepatitis B virus is highly immunogenic at the T cell level in man
    • Ferrari C, Penna A, Bertoletti A et al. The preS1 antigen of hepatitis B virus is highly immunogenic at the T cell level in man. J. Clin. Invest. 84(4), 1314-1319 (1989).
    • (1989) J. Clin. Invest. , vol.84 , Issue.4 , pp. 1314-1319
    • Ferrari, C.1    Penna, A.2    Bertoletti, A.3
  • 16
    • 0023771340 scopus 로고
    • T-and B-cell recognition of hepatitis B viral antigens
    • Milich DR. T-and B-cell recognition of hepatitis B viral antigens. Immunol. Today 9(12), 380-386 (1988).
    • (1988) Immunol. Today , vol.9 , Issue.12 , pp. 380-386
    • Milich, D.R.1
  • 17
    • 0028914040 scopus 로고
    • Weak immunogenicity of the pre-S2 sequence and lack of circumventing effect on the unresponsiveness to the hepatitis B virus vaccine
    • Pillot J, Poynard T, Elias A et al. Weak immunogenicity of the pre-S2 sequence and lack of circumventing effect on the unresponsiveness to the hepatitis B virus vaccine. Vaccine 13(3), 289-294 (1995).
    • (1995) Vaccine , vol.13 , Issue.3 , pp. 289-294
    • Pillot, J.1    Poynard, T.2    Elias, A.3
  • 18
    • 0035133043 scopus 로고    scopus 로고
    • Rapid seroprotection against hepatitis B following the first dose of a Pre-S1/ Pre-S2/S vaccine
    • Shapira MY, Zeira E, Adler R, Shouval D. Rapid seroprotection against hepatitis B following the first dose of a Pre-S1/ Pre-S2/S vaccine. J. Hepatol. 34(1), 123-127 (2001).
    • (2001) J. Hepatol. , vol.34 , Issue.1 , pp. 123-127
    • Shapira, M.Y.1    Zeira, E.2    Adler, R.3    Shouval, D.4
  • 19
    • 0034802568 scopus 로고    scopus 로고
    • Evaluation of a new hepatitis B triple-antigen vaccine in inadequate responders to current vaccines
    • Zuckerman JN, Zuckerman AJ, Symington I et al.; UK Hepacare Study Group. Evaluation of a new hepatitis B triple-antigen vaccine in inadequate responders to current vaccines. Hepatology 34(4 Pt 1), 798-802 (2001).
    • (2001) Hepatology , vol.34 , Issue.4 PART 1 , pp. 798-802
    • Zuckerman, J.N.1    Zuckerman, A.J.2    Symington, I.3
  • 20
    • 33644892768 scopus 로고    scopus 로고
    • Comparative immunogenicity of a PreS/S hepatitis B vaccine in non-and low responders to conventional vaccine
    • Rendi-Wagner P, Shouval D, Genton B et al. Comparative immunogenicity of a PreS/S hepatitis B vaccine in non-and low responders to conventional vaccine. Vaccine 24(15), 2781-2789 (2006).
    • (2006) Vaccine , vol.24 , Issue.15 , pp. 2781-2789
    • Rendi-Wagner, P.1    Shouval, D.2    Genton, B.3
  • 21
    • 70649114408 scopus 로고    scopus 로고
    • Anti-preS responses influence the anti-HBs response in newborns after vaccination with the third generation Sci-B-Vac vaccine
    • Sylvan SP, Madalinski K, Hellström UB. Anti-preS responses influence the anti-HBs response in newborns after vaccination with the third generation Sci-B-Vac vaccine. Vaccine 28(2), 446-451 (2009).
    • (2009) Vaccine , vol.28 , Issue.2 , pp. 446-451
    • Sylvan, S.P.1    Madalinski, K.2    Hellström, U.B.3
  • 22
    • 0028874697 scopus 로고
    • Functions of the internal pre-S domain of the large surface protein in hepatitis B virus particle morphogenesis
    • Bruss V, Vieluf K. Functions of the internal pre-S domain of the large surface protein in hepatitis B virus particle morphogenesis. J. Virol. 69(11), 6652-6657 (1995).
    • (1995) J. Virol. , vol.69 , Issue.11 , pp. 6652-6657
    • Bruss, V.1    Vieluf, K.2
  • 23
    • 0026483273 scopus 로고
    • Hepatitis B virus capsid particles are assembled from core-protein dimer precursors
    • Zhou S, Standring DN. Hepatitis B virus capsid particles are assembled from core-protein dimer precursors. Proc. Natl Acad. Sci. USA 89(21), 10046-10050 (1992).
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , Issue.21 , pp. 10046-10050
    • Zhou, S.1    Standring, D.N.2
  • 24
    • 0028307177 scopus 로고
    • Three-dimensional structure of hepatitis B virus core particles determined by electron cryomicroscopy
    • Crowther RA, Kiselev NA, Böttcher B et al. Three-dimensional structure of hepatitis B virus core particles determined by electron cryomicroscopy. Cell 77(6), 943-950 (1994).
    • (1994) Cell , vol.77 , Issue.6 , pp. 943-950
    • Crowther, R.A.1    Kiselev, N.A.2    Böttcher, B.3
  • 26
    • 0037428471 scopus 로고    scopus 로고
    • Proteolytic processing of the hepatitis B virus e antigen precursor
    • Messageot F, Salhi S, Eon P, Rossignol JM. Proteolytic processing of the hepatitis B virus e antigen precursor. J. Biol. Chem. 278(2), 891 (2003).
    • (2003) J. Biol. Chem. , vol.278 , Issue.2 , pp. 891
    • Messageot, F.1    Salhi, S.2    Eon, P.3    Rossignol, J.M.4
  • 27
    • 0027463464 scopus 로고
    • Structure of hepatitis B virus core and e-antigen. A single precore amino acid prevents nucleocapsid assembly
    • Schödel F, Peterson D, Zheng J, Jones JE, Hughes JL, Milich DR. Structure of hepatitis B virus core and e-antigen. A single precore amino acid prevents nucleocapsid assembly. J. Biol. Chem. 268(2), 1332-1337 (1993).
    • (1993) J. Biol. Chem. , vol.268 , Issue.2 , pp. 1332-1337
    • Schödel, F.1    Peterson, D.2    Zheng, J.3    Jones, J.E.4    Hughes, J.L.5    Milich, D.R.6
  • 28
    • 0025147370 scopus 로고
    • Is a function of the secreted hepatitis B e antigen to induce immunologic tolerance in utero? Proc
    • Milich DR, Jones JE, Hughes JL, Price J, Raney AK, McLachlan A. Is a function of the secreted hepatitis B e antigen to induce immunologic tolerance in utero? Proc. Natl Acad. Sci. USA 87(17), 6599-6603 (1990).
    • (1990) Natl Acad. Sci. USA , vol.87 , Issue.17 , pp. 6599-6603
    • Milich, D.R.1    Jones, J.E.2    Hughes, J.L.3    Price, J.4    Raney, A.K.5    McLachlan, A.6
  • 29
    • 84864583849 scopus 로고    scopus 로고
    • Hepatitis B precore protein: Pathogenic potential and therapeutic promise
    • Walsh R, Locarnini S. Hepatitis B precore protein: pathogenic potential and therapeutic promise. Yonsei Med. J. 53(5), 875-885 (2012).
    • (2012) Yonsei Med. J. , vol.53 , Issue.5 , pp. 875-885
    • Walsh, R.1    Locarnini, S.2
  • 30
    • 77953747864 scopus 로고    scopus 로고
    • Full-length hepatitis B virus core protein packages viral and heterologous RNA with similarly high levels of cooperativity
    • Porterfield JZ, Dhason MS, Loeb DD, Nassal M, Stray SJ, Zlotnick A. Full-length hepatitis B virus core protein packages viral and heterologous RNA with similarly high levels of cooperativity. J. Virol. 84(14), 7174-7184 (2010).
    • (2010) J. Virol. , vol.84 , Issue.14 , pp. 7174-7184
    • Porterfield, J.Z.1    Dhason, M.S.2    Loeb, D.D.3    Nassal, M.4    Stray, S.J.5    Zlotnick, A.6
  • 31
    • 0036500146 scopus 로고    scopus 로고
    • The morphogenic linker peptide of HBV capsid protein forms a mobile array on the interior surface
    • Watts NR, Conway JF, Cheng N et al. The morphogenic linker peptide of HBV capsid protein forms a mobile array on the interior surface. EMBO J. 21(5), 876-884 (2002).
    • (2002) EMBO J. , vol.21 , Issue.5 , pp. 876-884
    • Watts, N.R.1    Conway, J.F.2    Cheng, N.3
  • 32
    • 0029950758 scopus 로고    scopus 로고
    • Dimorphism of hepatitis B virus capsids is strongly influenced by the C-terminus of the capsid protein
    • Zlotnick A, Cheng N, Conway JF et al. Dimorphism of hepatitis B virus capsids is strongly influenced by the C-terminus of the capsid protein. Biochemistry 35(23), 7412-7421 (1996).
    • (1996) Biochemistry , vol.35 , Issue.23 , pp. 7412-7421
    • Zlotnick, A.1    Cheng, N.2    Conway, J.F.3
  • 33
    • 0033152857 scopus 로고    scopus 로고
    • The crystal structure of the human hepatitis B virus capsid
    • Wynne SA, Crowther RA, Leslie AG. The crystal structure of the human hepatitis B virus capsid. Mol. Cell 3(6), 771-780 (1999).
    • (1999) Mol. Cell , vol.3 , Issue.6 , pp. 771-780
    • Wynne, S.A.1    Crowther, R.A.2    Leslie, A.G.3
  • 34
    • 0015252446 scopus 로고
    • Relationship of virus dose to incubation time of clinical hepatitis and time of appearance of hepatitis-associated antigen
    • Barker LF, Murray R. Relationship of virus dose to incubation time of clinical hepatitis and time of appearance of hepatitis-associated antigen. Am. J. Med. Sci. 263(1), 27-33 (1972).
    • (1972) Am. J. Med. Sci. , vol.263 , Issue.1 , pp. 27-33
    • Barker, L.F.1    Murray, R.2
  • 35
    • 0026706346 scopus 로고
    • Hepadnaviral assembly is initiated by polymerase binding to the encapsidation signal in the viral RNA genome
    • Bartenschlager R, Schaller H. Hepadnaviral assembly is initiated by polymerase binding to the encapsidation signal in the viral RNA genome. EMBO J. 11(9), 3413-3420 (1992).
    • (1992) EMBO J. , vol.11 , Issue.9 , pp. 3413-3420
    • Bartenschlager, R.1    Schaller, H.2
  • 36
    • 0025238448 scopus 로고
    • Polymerase gene products of hepatitis B viruses are required for genomic RNA packaging as wel as for reverse transcription
    • Hirsch RC, Lavine JE, Chang LJ, Varmus HE, Ganem D. Polymerase gene products of hepatitis B viruses are required for genomic RNA packaging as wel as for reverse transcription. Nature 344(6266), 552-555 (1990).
    • (1990) Nature , vol.344 , Issue.6266 , pp. 552-555
    • Hirsch, R.C.1    Lavine, J.E.2    Chang, L.J.3    Varmus, H.E.4    Ganem, D.5
  • 37
    • 0141815723 scopus 로고    scopus 로고
    • Efficient Hsp90-independent in vitro activation by Hsc70 and Hsp40 of duck hepatitis B virus reverse transcriptase, an assumed Hsp90 client protein
    • Beck J, Nassal M. Efficient Hsp90-independent in vitro activation by Hsc70 and Hsp40 of duck hepatitis B virus reverse transcriptase, an assumed Hsp90 client protein. J. Biol. Chem. 278(38), 36128-36138 (2003).
    • (2003) J. Biol. Chem. , vol.278 , Issue.38 , pp. 36128-36138
    • Beck, J.1    Nassal, M.2
  • 38
    • 8644249753 scopus 로고    scopus 로고
    • Requirement of heat shock protein 90 for human hepatitis B virus reverse transcriptase function
    • Hu J, Flores D, Toft D, Wang X, Nguyen D. Requirement of heat shock protein 90 for human hepatitis B virus reverse transcriptase function. J. Virol. 78(23), 13122-13131 (2004).
    • (2004) J. Virol. , vol.78 , Issue.23 , pp. 13122-13131
    • Hu, J.1    Flores, D.2    Toft, D.3    Wang, X.4    Nguyen, D.5
  • 39
    • 0037025366 scopus 로고    scopus 로고
    • Role of p50/CDC37 in hepadnavirus assembly and replication
    • Wang X, Grammatikakis N, Hu J. Role of p50/CDC37 in hepadnavirus assembly and replication. J. Biol. Chem. 277(27), 24361-24367 (2002).
    • (2002) J. Biol. Chem. , vol.277 , Issue.27 , pp. 24361-24367
    • Wang, X.1    Grammatikakis, N.2    Hu, J.3
  • 40
    • 0036318795 scopus 로고    scopus 로고
    • Identification of SRPK1 and SRPK2 as the major cellular protein kinases phosphorylating hepatitis B virus core protein
    • Daub H, Blencke S, Habenberger P et al. Identification of SRPK1 and SRPK2 as the major cellular protein kinases phosphorylating hepatitis B virus core protein. J. Virol. 76(16), 8124-8137 (2002).
    • (2002) J. Virol. , vol.76 , Issue.16 , pp. 8124-8137
    • Daub, H.1    Blencke, S.2    Habenberger, P.3
  • 41
    • 0028073177 scopus 로고
    • Effect of core protein phosphorylation by protein kinase C on encapsidation of RNA within core particles of hepatitis B virus
    • Kann M, Gerlich WH. Effect of core protein phosphorylation by protein kinase C on encapsidation of RNA within core particles of hepatitis B virus. J. Virol. 68(12), 7993-8000 (1994).
    • (1994) J. Virol. , vol.68 , Issue.12 , pp. 7993-8000
    • Kann, M.1    Gerlich, W.H.2
  • 42
    • 0031968423 scopus 로고    scopus 로고
    • Phosphorylation of the core protein of hepatitis B virus by a 46-kilodalton serine kinase
    • Kau JH, Ting LP. Phosphorylation of the core protein of hepatitis B virus by a 46-kilodalton serine kinase. J. Virol. 72(5), 3796-3803 (1998).
    • (1998) J. Virol. , vol.72 , Issue.5 , pp. 3796-3803
    • Kau, J.H.1    Ting, L.P.2
  • 44
    • 1842409555 scopus 로고    scopus 로고
    • Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy
    • Böttcher B, Wynne SA, Crowther RA. Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy. Nature 386(6620), 88-91 (1997).
    • (1997) Nature , vol.386 , Issue.6620 , pp. 88-91
    • Böttcher, B.1    Wynne, S.A.2    Crowther, R.A.3
  • 45
    • 0018760172 scopus 로고
    • Expression in Escherichia coli of hepatitis B virus DNA sequences cloned in plasmid pBR322
    • Burrell CJ, Mackay P, Greenaway PJ, Hofschneider PH, Murray K. Expression in Escherichia coli of hepatitis B virus DNA sequences cloned in plasmid pBR322. Nature 279(5708), 43-47 (1979).
    • (1979) Nature , vol.279 , Issue.5708 , pp. 43-47
    • Burrell, C.J.1    MacKay, P.2    Greenaway, P.J.3    Hofschneider, P.H.4    Murray, K.5
  • 46
    • 0019824173 scopus 로고
    • Production in B subtilis of hepatitis B core antigen and a major antigen of foot and mouth disease virus
    • Hardy K, Stahl S, Küpper H. Production in B. subtilis of hepatitis B core antigen and a major antigen of foot and mouth disease virus. Nature 293(5832), 481-483 (1981).
    • (1981) Nature , vol.293 , Issue.5832 , pp. 481-483
    • Hardy, K.1    Stahl, S.2    Küpper, H.3
  • 47
    • 0025696561 scopus 로고
    • Hepatitis B virus nucleocapsid/pre-S2 fusion proteins expressed in attenuated Salmonella for oral vaccination
    • Schödel F, Milich DR, Will H. Hepatitis B virus nucleocapsid/pre-S2 fusion proteins expressed in attenuated Salmonella for oral vaccination. J. Immunol. 145(12), 4317-4321 (1990).
    • (1990) J. Immunol. , vol.145 , Issue.12 , pp. 4317-4321
    • Schödel, F.1    Milich, D.R.2    Will, H.3
  • 48
    • 0022880810 scopus 로고
    • Unusually high-level expression of a foreign gene (hepatitis B virus core antigen) in Saccharomyces cerevisiae
    • Kniskern PJ, Hagopian A, Montgomery DL et al. Unusually high-level expression of a foreign gene (hepatitis B virus core antigen) in Saccharomyces cerevisiae. Gene 46(1), 135-141 (1986).
    • (1986) Gene , vol.46 , Issue.1 , pp. 135-141
    • Kniskern, P.J.1    Hagopian, A.2    Montgomery, D.L.3
  • 49
    • 0141855304 scopus 로고    scopus 로고
    • Evaluation of Aspergillus niger as host for virus-like particle production, using the hepatitis B surface antigen as a model
    • Plüddemann A, Van Zyl WH. Evaluation of Aspergillus niger as host for virus-like particle production, using the hepatitis B surface antigen as a model. Curr. Genet. 43(6), 439-446 (2003).
    • (2003) Curr. Genet. , vol.43 , Issue.6 , pp. 439-446
    • Plüddemann, A.1    Van Zyl, W.H.2
  • 50
    • 0035946262 scopus 로고    scopus 로고
    • Purification of recombinant HBc antigen expressed in Escherichia coli and Pichia pastoris: Comparison of size-exclusion chromatography and ultracentrifugation
    • Rolland D, Gauthier M, Dugua JM et al. Purification of recombinant HBc antigen expressed in Escherichia coli and Pichia pastoris: comparison of size-exclusion chromatography and ultracentrifugation. J. Chromatogr. B Biomed. Sci. Appl. 753(1), 51-65 (2001).
    • (2001) J. Chromatogr. B Biomed. Sci. Appl. , vol.753 , Issue.1 , pp. 51-65
    • Rolland, D.1    Gauthier, M.2    Dugua, J.M.3
  • 52
    • 0005857894 scopus 로고
    • A signal peptide encoded within the precore region of hepatitis B virus directs the secretion of a heterogeneous population of e antigens in Xenopus oocytes
    • Standring DN, Ou JH, Masiarz FR, Rutter WJ. A signal peptide encoded within the precore region of hepatitis B virus directs the secretion of a heterogeneous population of e antigens in Xenopus oocytes. Proc. Natl Acad. Sci. USA 85(22), 8405-8409 (1988).
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , Issue.22 , pp. 8405-8409
    • Standring, D.N.1    Ou, J.H.2    Masiarz, F.R.3    Rutter, W.J.4
  • 53
    • 0023709406 scopus 로고
    • Co-expression of the hepatitis B surface and core antigens using baculovirus multiple expression vectors
    • Takehara K, Ireland D, Bishop DH. Co-expression of the hepatitis B surface and core antigens using baculovirus multiple expression vectors. J. Gen. Virol. Pt 11), 2763-2777 (1988).
    • (1988) J. Gen. Virol , vol.11 , Issue.PART , pp. 2763-2777
    • Takehara, K.1    Ireland, D.2    Bishop, D.H.3
  • 54
    • 0031980924 scopus 로고    scopus 로고
    • Application of the human hepatitis B virus core antigen from transgenic tobacco plants for serological diagnosis
    • Tsuda S, Yoshioka K, Tanaka T et al. Application of the human hepatitis B virus core antigen from transgenic tobacco plants for serological diagnosis. Vox Sang. 74(3), 148-155 (1998).
    • (1998) Vox Sang. , vol.74 , Issue.3 , pp. 148-155
    • Tsuda, S.1    Yoshioka, K.2    Tanaka, T.3
  • 55
    • 0026034960 scopus 로고
    • The role of envelope proteins in hepatitis B virus assembly
    • Bruss V, Ganem D. The role of envelope proteins in hepatitis B virus assembly. Proc. Natl Acad. Sci. USA 88(3), 1059-1063 (1991).
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , Issue.3 , pp. 1059-1063
    • Bruss, V.1    Ganem, D.2
  • 56
    • 0025879364 scopus 로고
    • Three envelope proteins of hepatitis B virus: Large S, middle S, and major S proteins needed for the formation of Dane particles
    • Ueda K, Tsurimoto T, Matsubara K. Three envelope proteins of hepatitis B virus: large S, middle S, and major S proteins needed for the formation of Dane particles. J. Virol. 65(7), 3521-3529 (1991).
    • (1991) J. Virol. , vol.65 , Issue.7 , pp. 3521-3529
    • Ueda, K.1    Tsurimoto, T.2    Matsubara, K.3
  • 57
    • 0023546339 scopus 로고
    • Improved immunogenicity of a peptide epitope after fusion to hepatitis B core protein
    • Clarke BE, Newton SE, Carroll AR et al. Improved immunogenicity of a peptide epitope after fusion to hepatitis B core protein. Nature 330(6146), 381-384 (1987).
    • (1987) Nature , vol.330 , Issue.6146 , pp. 381-384
    • Clarke, B.E.1    Newton, S.E.2    Carroll, A.R.3
  • 58
    • 0020316090 scopus 로고
    • Electron microscopy of hepatitis B core antigen synthesized in e
    • Escherichia coli
    • Cohen BJ, Richmond JE. Electron microscopy of hepatitis B core antigen synthesized in E. coli. Nature 296(5858), 677-679 (1982). Escherichia coli.
    • (1982) Coli. Nature , vol.296 , Issue.5858 , pp. 677-679
    • Cohen, B.J.1    Richmond, J.E.2
  • 59
    • 0017649516 scopus 로고
    • Application of a screening test for antibody the hepatitis B core antigen
    • Cohen BJ, Cossart YE. Application of a screening test for antibody the hepatitis B core antigen. J. Clin. Pathol. 30(8), 709-713 (1977).
    • (1977) J. Clin. Pathol. , vol.30 , Issue.8 , pp. 709-713
    • Cohen, B.J.1    Cossart, Y.E.2
  • 60
    • 0022596902 scopus 로고
    • Bacterially expressed antigenic peptide from foot-and-mouth disease virus capsid elicits variable immunologic responses in animals
    • Winther MD, Allen G, Bomford RH, Brown F. Bacterially expressed antigenic peptide from foot-and-mouth disease virus capsid elicits variable immunologic responses in animals. J. Immunol. 136(5), 1835-1840 (1986).
    • (1986) J. Immunol. , vol.136 , Issue.5 , pp. 1835-1840
    • Winther, M.D.1    Allen, G.2    Bomford, R.H.3    Brown, F.4
  • 61
    • 0030937751 scopus 로고    scopus 로고
    • Visualization of a 4-helix bundle in the hepatitis B virus capsid by cryo-electron microscopy
    • Conway JF, Cheng N, Zlotnick A, Wingfield PT, Stahl SJ, Steven AC. Visualization of a 4-helix bundle in the hepatitis B virus capsid by cryo-electron microscopy. Nature 386(6620), 91-94 (1997).
    • (1997) Nature , vol.386 , Issue.6620 , 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
  • 62
    • 0024500103 scopus 로고
    • Antigenic determinants and functional domains in core antigen and e antigen from hepatitis B virus
    • Salfeld J, Pfaff E, Noah M, Schaller H. Antigenic determinants and functional domains in core antigen and e antigen from hepatitis B virus. J. Virol. 63(2), 798-808 (1989).
    • (1989) J. Virol. , vol.63 , Issue.2 , pp. 798-808
    • Salfeld, J.1    Pfaff, E.2    Noah, M.3    Schaller, H.4
  • 63
    • 0024474088 scopus 로고
    • A recombinant hepatitis B core antigen polypeptide with the protamine-like domain deleted self-assembles into capsid particles but fails to bind nucleic acids
    • Gallina A, Bonelli F, Zentilin L, Rindi G, Muttini M, Milanesi G. A recombinant hepatitis B core antigen polypeptide with the protamine-like domain deleted self-assembles into capsid particles but fails to bind nucleic acids. J. Virol. 63(11), 4645-4652 (1989).
    • (1989) J. Virol. , vol.63 , Issue.11 , pp. 4645-4652
    • Gallina, A.1    Bonelli, F.2    Zentilin, L.3    Rindi, G.4    Muttini, M.5    Milanesi, G.6
  • 64
    • 19444368726 scopus 로고    scopus 로고
    • Universal influenza A vaccine: Optimization of M2-based constructs
    • De Filette M, Min Jou W, Birkett A et al. Universal influenza A vaccine: optimization of M2-based constructs. Virology 337(1), 149-161 (2005).
    • (2005) Virology , vol.337 , Issue.1 , pp. 149-161
    • De Filette, M.1    Min Jou, W.2    Birkett, A.3
  • 65
    • 0026556670 scopus 로고
    • The position of heterologous epitopes inserted in hepatitis B virus core particles determines their immunogenicity
    • Schödel F, Moriarty AM, Peterson DL et al. The position of heterologous epitopes inserted in hepatitis B virus core particles determines their immunogenicity. J. Virol. 66(1), 106-114 (1992).
    • (1992) J. Virol. , vol.66 , Issue.1 , pp. 106-114
    • Schödel, F.1    Moriarty, A.M.2    Peterson, D.L.3
  • 66
    • 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 et al. Development of hepatitis B virus capsids into a whole-chain protein antigen display platform: new particulate Lyme disease vaccines. Int. J. Med. Microbiol. 298(1-2), 135-142 (2008).
    • (2008) Int. J. Med. Microbiol. , vol.298 , Issue.1-2 , pp. 135-142
    • Nassal, M.1    Skamel, C.2    Vogel, M.3
  • 67
    • 0033514992 scopus 로고    scopus 로고
    • Native display of complete foreign protein domains on the surface of hepatitis B virus capsids
    • Kratz PA, Böttcher B, Nassal M. Native display of complete foreign protein domains on the surface of hepatitis B virus capsids. Proc. Natl Acad. Sci. USA 96(5), 1915-1920 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , Issue.5 , pp. 1915-1920
    • Kratz, P.A.1    Böttcher, B.2    Nassal, M.3
  • 68
    • 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 et al. 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(25), 17474-17481 (2006).
    • (2006) J. Biol. Chem. , vol.281 , Issue.25 , pp. 17474-17481
    • Skamel, C.1    Ploss, M.2    Böttcher, B.3
  • 69
    • 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 PA, Wallich R, Stehle T, Simon MM. 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(2), 655-665 (2005).
    • (2005) Eur. J. Immunol. , vol.35 , Issue.2 , pp. 655-665
    • Nassal, M.1    Skamel, C.2    Kratz, P.A.3    Wallich, R.4    Stehle, T.5    Simon, M.M.6
  • 70
    • 57749116030 scopus 로고    scopus 로고
    • Internal core protein cleavage leaves the hepatitis B virus capsid intact and enhances its capacity for surface display of heterologous whole chain proteins
    • Walker A, Skamel C, Vorreiter J, Nassal M. Internal core protein cleavage leaves the hepatitis B virus capsid intact and enhances its capacity for surface display of heterologous whole chain proteins. J. Biol. Chem. 283(48), 33508-33515 (2008).
    • (2008) J. Biol. Chem. , vol.283 , Issue.48 , pp. 33508-33515
    • Walker, A.1    Skamel, C.2    Vorreiter, J.3    Nassal, M.4
  • 71
    • 0037135661 scopus 로고    scopus 로고
    • A molecular assembly system that renders antigens of choice highly repetitive for induction of protective B cell responses
    • Jegerlehner A, Tissot A, Lechner F et al. A molecular assembly system that renders antigens of choice highly repetitive for induction of protective B cell responses. Vaccine 20(25-26), 3104-3112 (2002).
    • (2002) Vaccine , vol.20 , Issue.25-26 , pp. 3104-3112
    • Jegerlehner, A.1    Tissot, A.2    Lechner, F.3
  • 72
    • 70649105484 scopus 로고    scopus 로고
    • A novel virus-like particle based on hepatitis B core antigen and substrate-binding domain of bacterial molecular chaperone DnaK
    • Wang XJ, Gu K, Xiong QY et al. A novel virus-like particle based on hepatitis B core antigen and substrate-binding domain of bacterial molecular chaperone DnaK. Vaccine 27(52), 7377-7384 (2009).
    • (2009) Vaccine , vol.27 , Issue.52 , pp. 7377-7384
    • Wang, X.J.1    Gu, K.2    Xiong, Q.Y.3
  • 73
    • 15844413835 scopus 로고    scopus 로고
    • Efficient homologous prime-boost strategies for T cell vaccination based on virus-like particles
    • Schwarz K, Meijerink E, Speiser DE et al. Efficient homologous prime-boost strategies for T cell vaccination based on virus-like particles. Eur. J. Immunol. 35(3), 816-821 (2005).
    • (2005) Eur. J. Immunol. , vol.35 , Issue.3 , pp. 816-821
    • Schwarz, K.1    Meijerink, E.2    Speiser, D.E.3
  • 74
    • 0022996325 scopus 로고
    • The nucleocapsid of hepatitis B virus is both a T-cellindependent and a T-cell-dependent antigen
    • Milich DR, McLachlan A. The nucleocapsid of hepatitis B virus is both a T-cellindependent and a T-cell-dependent antigen. Science 234(4782), 1398-1401 (1986).
    • (1986) Science , vol.234 , Issue.4782 , pp. 1398-1401
    • Milich, D.R.1    McLachlan, A.2
  • 75
    • 0023278981 scopus 로고
    • Immune response to hepatitis B virus core antigen (HBcAg): Localization of T cell recognition sites within HBcAg/HBeAg
    • Milich DR, McLachlan A, Moriarty A, Thornton GB. Immune response to hepatitis B virus core antigen (HBcAg): localization of T cell recognition sites within HBcAg/HBeAg. J. Immunol. 139(4), 1223-1231 (1987).
    • (1987) J. Immunol. , vol.139 , Issue.4 , pp. 1223-1231
    • Milich, D.R.1    McLachlan, A.2    Moriarty, A.3    Thornton, G.B.4
  • 76
    • 0027765265 scopus 로고
    • Cell mediated immune response to hepatitis B virus nucleocapsid antigen
    • Ferrari C, Penna A, Bertoletti A, Fiaccadori F. Cell mediated immune response to hepatitis B virus nucleocapsid antigen. Arch. Virol. Suppl. 8, 91-101 (1993).
    • (1993) Arch. Virol. Suppl. , vol.8 , pp. 91-101
    • Ferrari, C.1    Penna, A.2    Bertoletti, A.3    Fiaccadori, F.4
  • 77
    • 0028915129 scopus 로고
    • Preferential recognition of hepatitis B nucleocapsid antigens by Th1 or Th2 cells is epitope and major histocompatibility complex dependent
    • Milich DR, Peterson DL, Schödel F, Jones JE, Hughes JL. Preferential recognition of hepatitis B nucleocapsid antigens by Th1 or Th2 cells is epitope and major histocompatibility complex dependent. J. Virol. 69(5), 2776-2785 (1995).
    • (1995) J. Virol. , vol.69 , Issue.5 , pp. 2776-2785
    • Milich, D.R.1    Peterson, D.L.2    Schödel, F.3    Jones, J.E.4    Hughes, J.L.5
  • 78
    • 0023256269 scopus 로고
    • Antibody production to the nucleocapsid and envelope of the hepatitis B virus primed by a single synthetic T cell site
    • Milich DR, McLachlan A, Thornton GB, Hughes JL. Antibody production to the nucleocapsid and envelope of the hepatitis B virus primed by a single synthetic T cell site. Nature 329(6139), 547-549 (1987).
    • (1987) Nature , vol.329 , Issue.6139 , pp. 547-549
    • Milich, D.R.1    McLachlan, A.2    Thornton, G.B.3    Hughes, J.L.4
  • 80
    • 67449110843 scopus 로고    scopus 로고
    • Interaction of the hepatitis B core antigen and the innate immune system
    • Lee BO, Tucker A, Frelin L et al. Interaction of the hepatitis B core antigen and the innate immune system. J. Immunol. 182(11), 6670-6681 (2009).
    • (2009) J. Immunol. , vol.182 , Issue.11 , pp. 6670-6681
    • Lee, B.O.1    Tucker, A.2    Frelin, L.3
  • 81
    • 34648828469 scopus 로고    scopus 로고
    • Generation of chimeric HBc proteins with epitopes in E. coli: Formation of virus-like particles and a potent inducer of antigen-specific cytotoxic immune response and anti-tumor effect in vivo
    • Zhang Y, Song S, Liu C et al. Generation of chimeric HBc proteins with epitopes in E. coli: formation of virus-like particles and a potent inducer of antigen-specific cytotoxic immune response and anti-tumor effect in vivo. Cell. Immunol. 247(1), 18-27 (2007).
    • (2007) Cell. Immunol. , vol.247 , Issue.1 , pp. 18-27
    • Zhang, Y.1    Song, S.2    Liu, C.3
  • 82
    • 66149094633 scopus 로고    scopus 로고
    • Multiepitope peptide-loaded virus-like particles as a vaccine against hepatitis B virus-related hepatocellular carcinoma
    • Ding FX, Wang F, Lu YM et al. Multiepitope peptide-loaded virus-like particles as a vaccine against hepatitis B virus-related hepatocellular carcinoma. Hepatology 49(5), 1492-1502 (2009).
    • (2009) Hepatology , vol.49 , Issue.5 , pp. 1492-1502
    • Ding, F.X.1    Wang, F.2    Lu, Y.M.3
  • 83
    • 77956500311 scopus 로고    scopus 로고
    • Significant anti-tumour activity of adoptively transferred T cells elicited by intratumoral dendritic cell vaccine injection through enhancing the ratio of CD8+ T cell/ regulatory T cells in tumour
    • Song S, Zhang K, You H et al. Significant anti-tumour activity of adoptively transferred T cells elicited by intratumoral dendritic cell vaccine injection through enhancing the ratio of CD8+ T cell/ regulatory T cells in tumour. Clin. Exp. Immunol. 162(1), 75-83 (2010).
    • (2010) Clin. Exp. Immunol. , vol.162 , Issue.1 , pp. 75-83
    • Song, S.1    Zhang, K.2    You, H.3
  • 84
    • 0023804209 scopus 로고
    • Comparative immunogenicity of hepatitis B virus core and e antigens
    • Milich DR, McLachlan A, Stahl S et al. Comparative immunogenicity of hepatitis B virus core and E antigens. J. Immunol. 141(10), 3617-3624 (1988).
    • (1988) J. Immunol. , vol.141 , Issue.10 , pp. 3617-3624
    • Milich, D.R.1    McLachlan, A.2    Stahl, S.3
  • 85
    • 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, Zinkernagel RM. T cell-independent type I antibody response against B cell epitopes expressed repetitively on recombinant virus particles. Proc. Natl Acad. Sci. USA 95(16), 9477-9481 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , Issue.16 , pp. 9477-9481
    • Fehr, T.1    Skrastina, D.2    Pumpens, P.3    Zinkernagel, R.M.4
  • 86
    • 11444263138 scopus 로고    scopus 로고
    • The arginine-rich carboxy-terminal domain of the hepatitis B virus core protein mediates attachment of nucleocapsids to cell-surface-expressed heparan sulfate
    • Vanlandschoot P, Van Houtte F, Serruys B, Leroux-Roels G. The arginine-rich carboxy-terminal domain of the hepatitis B virus core protein mediates attachment of nucleocapsids to cell-surface-expressed heparan sulfate. J. Gen. Virol. 86(Pt 1), 75-84 (2005).
    • (2005) J. Gen. Virol. , vol.86 , Issue.PART 1 , pp. 75-84
    • Vanlandschoot, P.1    Van Houtte, F.2    Serruys, B.3    Leroux-Roels, G.4
  • 87
    • 13644250283 scopus 로고    scopus 로고
    • Immunostimulatory potential of hepatitis B nucleocapsid preparations: Lipopolysaccharide contamination should not be overlooked
    • Vanlandschoot P, Van Houtte F, Ulrichts P, Tavernier J, Leroux-Roels G. Immunostimulatory potential of hepatitis B nucleocapsid preparations: lipopolysaccharide contamination should not be overlooked. J. Gen. Virol. 86(Pt 2), 323-331 (2005).
    • (2005) J. Gen. Virol. , vol.86 , Issue.PART 2 , pp. 323-331
    • Vanlandschoot, P.1    Van Houtte, F.2    Ulrichts, P.3    Tavernier, J.4    Leroux-Roels, G.5
  • 88
    • 33847221792 scopus 로고    scopus 로고
    • Contamination of a recombinant hepatitis B virus nucleocapsid preparation with a human B-cell activator
    • Vanlandschoot P, Van Houtte F, Serruys B, Leroux-Roels G. Contamination of a recombinant hepatitis B virus nucleocapsid preparation with a human B-cell activator. J. Virol. 81(5), 2535-2536 (2007).
    • (2007) J. Virol. , vol.81 , Issue.5 , pp. 2535-2536
    • Vanlandschoot, P.1    Van Houtte, F.2    Serruys, B.3    Leroux-Roels, G.4
  • 89
    • 78649838978 scopus 로고    scopus 로고
    • Advances and challenges in malaria vaccine development
    • Crompton PD, Pierce SK, Miller LH. Advances and challenges in malaria vaccine development. J. Clin. Invest. 120(12), 4168-4178 (2010).
    • (2010) J. Clin. Invest. , vol.120 , Issue.12 , pp. 4168-4178
    • Crompton, P.D.1    Pierce, S.K.2    Miller, L.H.3
  • 90
    • 0014202885 scopus 로고
    • Protective immunity produced by the injection of x-irradiated sporozoites of Plasmodium berghei
    • Nussenzweig RS, Vanderberg J, Most H, Orton C. Protective immunity produced by the injection of x-irradiated sporozoites of Plasmodium berghei. Nature 216(5111), 160-162 (1967).
    • (1967) Nature , vol.216 , Issue.5111 , pp. 160-162
    • Nussenzweig, R.S.1    Vanderberg, J.2    Most, H.3    Orton, C.4
  • 91
    • 0015736375 scopus 로고
    • Specificity of protection of man immunized against sporozoite-induced falciparum malaria
    • Clyde DF, McCarthy VC, Miller RM, Hornick RB. Specificity of protection of man immunized against sporozoite-induced falciparum malaria. Am. J. Med. Sci. 266(6), 398-403 (1973).
    • (1973) Am. J. Med. Sci. , vol.266 , Issue.6 , pp. 398-403
    • Clyde, D.F.1    McCarthy, V.C.2    Miller, R.M.3    Hornick, R.B.4
  • 92
    • 0018593563 scopus 로고
    • Use of attenuated sporozoites in the immunization of human volunteers against falciparum malaria
    • Rieckmann KH, Beaudoin RL, Cassells JS, Sell KW. Use of attenuated sporozoites in the immunization of human volunteers against falciparum malaria. Bull. World Health Organ. 57(Suppl. 1), 261-265 (1979).
    • (1979) Bull. World Health Organ. , vol.57 , Issue.SUPPL. 1 , pp. 261-265
    • Rieckmann, K.H.1    Beaudoin, R.L.2    Cassells, J.S.3    Sell, K.W.4
  • 93
  • 94
    • 0023254214 scopus 로고
    • Safety and efficacy of a recombinant DNA Plasmodium falciparum sporozoite vaccine
    • Ballou WR, Hoffman SL, Sherwood JA et al. Safety and efficacy of a recombinant DNA Plasmodium falciparum sporozoite vaccine. Lancet 1(8545), 1277-1281 (1987).
    • (1987) Lancet , vol.1 , Issue.8545 , pp. 1277-1281
    • Ballou, W.R.1    Hoffman, S.L.2    Sherwood, J.A.3
  • 95
    • 0023182064 scopus 로고
    • Safety and immunogenicity in man of a synthetic peptide malaria vaccine against Plasmodium falciparum sporozoites
    • Herrington DA, Clyde DF, Losonsky G et al. Safety and immunogenicity in man of a synthetic peptide malaria vaccine against Plasmodium falciparum sporozoites. Nature 328(6127), 257-259 (1987).
    • (1987) Nature , vol.328 , Issue.6127 , pp. 257-259
    • Herrington, D.A.1    Clyde, D.F.2    Losonsky, G.3
  • 96
    • 0027932875 scopus 로고
    • Immunity to malaria elicited by hybrid hepatitis B virus core particles carrying circumsporozoite protein epitopes
    • Schödel F, Wirtz R, Peterson D et al. Immunity to malaria elicited by hybrid hepatitis B virus core particles carrying circumsporozoite protein epitopes. J. Exp. Med. 180(3), 1037-1046 (1994).
    • (1994) J. Exp. Med. , vol.180 , Issue.3 , pp. 1037-1046
    • Schödel, F.1    Wirtz, R.2    Peterson, D.3
  • 97
    • 0036986329 scopus 로고    scopus 로고
    • A malaria vaccine candidate based on a hepatitis B virus core platform
    • Sällberg M, Hughes J, Jones J, Phillips TR, Milich DR. A malaria vaccine candidate based on a hepatitis B virus core platform. Intervirology 45(4-6), 350-361 (2002).
    • (2002) Intervirology , vol.45 , Issue.4-6 , pp. 350-361
    • Sällberg, M.1    Hughes, J.2    Jones, J.3    Phillips, T.R.4    Milich, D.R.5
  • 98
    • 0035852348 scopus 로고    scopus 로고
    • Conversion of poorly immunogenic malaria repeat sequences into a highly immunogenic vaccine candidate
    • Milich DR, Hughes J, Jones J, Sällberg M, Phillips TR. Conversion of poorly immunogenic malaria repeat sequences into a highly immunogenic vaccine candidate. Vaccine 20(5-6), 771-788 (2001).
    • (2001) Vaccine , vol.20 , Issue.5-6 , pp. 771-788
    • Milich, D.R.1    Hughes, J.2    Jones, J.3    Sällberg, M.4    Phillips, T.R.5
  • 99
    • 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 et al. 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(12), 6860-6870 (2002).
    • (2002) Infect. Immun. , vol.70 , Issue.12 , pp. 6860-6870
    • Birkett, A.1    Lyons, K.2    Schmidt, A.3
  • 100
    • 21144480904 scopus 로고    scopus 로고
    • Safety and enhanced immunogenicity of a hepatitis B core particle Plasmodium falciparum malaria vaccine formulated in adjuvant Montanide ISA 720 in a phase i trial
    • Oliveira GA, Wetzel K, Calvo-Calle JM et al. Safety and enhanced immunogenicity of a hepatitis B core particle Plasmodium falciparum malaria vaccine formulated in adjuvant Montanide ISA 720 in a phase I trial. Infect. Immun. 73(6), 3587-3597 (2005).
    • (2005) Infect. Immun. , vol.73 , Issue.6 , pp. 3587-3597
    • Oliveira, G.A.1    Wetzel, K.2    Calvo-Calle, J.M.3
  • 101
    • 7044254906 scopus 로고    scopus 로고
    • Phase i testing of a malaria vaccine composed of hepatitis B virus core particles expressing Plasmodium falciparum circumsporozoite epitopes
    • Nardin EH, Oliveira GA, Calvo-Calle JM et al. Phase I testing of a malaria vaccine composed of hepatitis B virus core particles expressing Plasmodium falciparum circumsporozoite epitopes. Infect. Immun. 72(11), 6519-6527 (2004).
    • (2004) Infect. Immun. , vol.72 , Issue.11 , pp. 6519-6527
    • Nardin, E.H.1    Oliveira, G.A.2    Calvo-Calle, J.M.3
  • 102
    • 10444286628 scopus 로고    scopus 로고
    • Safety, immunogenicity and efficacy of a pre-erythrocytic malaria candidate vaccine, ICC-1132 formulated in Seppic ISA 720
    • Walther M, Dunachie S, Keating S et al. Safety, immunogenicity and efficacy of a pre-erythrocytic malaria candidate vaccine, ICC-1132 formulated in Seppic ISA 720. Vaccine 23(7), 857-864 (2005).
    • (2005) Vaccine , vol.23 , Issue.7 , pp. 857-864
    • Walther, M.1    Dunachie, S.2    Keating, S.3
  • 103
    • 45249093689 scopus 로고    scopus 로고
    • Phase i trial of an alhydrogel adjuvanted hepatitis B core virus-like particle containing epitopes of Plasmodium falciparum circumsporozoite protein
    • Gregson AL, Oliveira G, Othoro C et al. Phase I trial of an alhydrogel adjuvanted hepatitis B core virus-like particle containing epitopes of Plasmodium falciparum circumsporozoite protein. PLoS One 3(2), e1556 (2008).
    • (2008) PLoS One , vol.3 , Issue.2
    • Gregson, A.L.1    Oliveira, G.2    Othoro, C.3
  • 104
    • 0023869487 scopus 로고
    • Human T-cell recognition of the circumsporozoite protein of Plasmodium falciparum: Immunodominant T-cell domains map to the polymorphic regions of the molecule
    • Good MF, Pombo D, Quakyi IA et al. Human T-cell recognition of the circumsporozoite protein of Plasmodium falciparum: immunodominant T-cell domains map to the polymorphic regions of the molecule. Proc. Natl Acad. Sci. USA 85(4), 1199-1203 (1988).
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , Issue.4 , pp. 1199-1203
    • Good, M.F.1    Pombo, D.2    Quakyi, I.A.3
  • 105
    • 0023736218 scopus 로고
    • Hepatitis B surface antigen as carrier matrix for the repetitive epitope of the circumsporozoite protein of Plasmodium falciparum
    • Rutgers T, Gordon D, Gathoye AM et al. Hepatitis B surface antigen as carrier matrix for the repetitive epitope of the circumsporozoite protein of Plasmodium falciparum. Nature Biotechnology 6(9), 1065-1070 (1988).
    • (1988) Nature Biotechnology , vol.6 , Issue.9 , pp. 1065-1070
    • Rutgers, T.1    Gordon, D.2    Gathoye, A.M.3
  • 106
    • 0029057169 scopus 로고
    • Safety, immunogenicity, and efficacy of a recombinantly produced Plasmodium falciparum circumsporozoite protein-hepatitis B surface antigen subunit vaccine
    • Gordon DM, McGovern TW, Krzych U et al. Safety, immunogenicity, and efficacy of a recombinantly produced Plasmodium falciparum circumsporozoite protein-hepatitis B surface antigen subunit vaccine. J. Infect. Dis. 171(6), 1576-1585 (1995).
    • (1995) J. Infect. Dis. , vol.171 , Issue.6 , pp. 1576-1585
    • Gordon, D.M.1    McGovern, T.W.2    Krzych, U.3
  • 107
    • 35349028297 scopus 로고    scopus 로고
    • GlaxoSmithKline Adjuvant Systems in vaccines: Concepts, achievements and perspectives
    • Garçon N, Chomez P, Van Mechelen M. GlaxoSmithKline Adjuvant Systems in vaccines: concepts, achievements and perspectives. Expert Rev. Vaccines 6(5), 723-739 (2007).
    • (2007) Expert Rev. Vaccines , vol.6 , Issue.5 , pp. 723-739
    • Garçon, N.1    Chomez, P.2    Van Mechelen, M.3
  • 108
  • 109
    • 79959368201 scopus 로고    scopus 로고
    • Protective immunity to pre-erythrocytic stage malaria
    • Schwenk RJ, Richie TL. Protective immunity to pre-erythrocytic stage malaria. Trends Parasitol. 27(7), 306-314 (2011).
    • (2011) Trends Parasitol. , vol.27 , Issue.7 , pp. 306-314
    • Schwenk, R.J.1    Richie, T.L.2
  • 110
    • 0019403963 scopus 로고
    • Identification of a second protein (M2) encoded by RNA segment 7 of influenza virus
    • Lamb RA, Choppin PW. Identification of a second protein (M2) encoded by RNA segment 7 of influenza virus. Virology 112(2), 729-737 (1981).
    • (1981) Virology , vol.112 , Issue.2 , pp. 729-737
    • Lamb, R.A.1    Choppin, P.W.2
  • 111
    • 0026612385 scopus 로고
    • Influenza virus M2 protein has ion channel activity
    • Pinto LH, Holsinger LJ, Lamb RA. Influenza virus M2 protein has ion channel activity. Cell 69(3), 517-528 (1992).
    • (1992) Cell , vol.69 , Issue.3 , pp. 517-528
    • Pinto, L.H.1    Holsinger, L.J.2    Lamb, R.A.3
  • 112
    • 0036007087 scopus 로고    scopus 로고
    • Influenza a virus M2 ion channel activity is essential for efficient replication in tissue culture
    • Takeda M, Pekosz A, Shuck K, Pinto LH, Lamb RA. Influenza a virus M2 ion channel activity is essential for efficient replication in tissue culture. J. Virol. 76(3), 1391-1399 (2002).
    • (2002) J. Virol. , vol.76 , Issue.3 , pp. 1391-1399
    • Takeda, M.1    Pekosz, A.2    Shuck, K.3    Pinto, L.H.4    Lamb, R.A.5
  • 113
    • 33646718791 scopus 로고    scopus 로고
    • The cytoplasmic tail of the influenza A virus M2 protein plays a role in viral assembly
    • Iwatsuki-Horimoto K, Horimoto T, Noda T et al. The cytoplasmic tail of the influenza A virus M2 protein plays a role in viral assembly. J. Virol. 80(11), 5233-5240 (2006).
    • (2006) J. Virol. , vol.80 , Issue.11 , pp. 5233-5240
    • Iwatsuki-Horimoto, K.1    Horimoto, T.2    Noda, T.3
  • 114
    • 53749092893 scopus 로고    scopus 로고
    • The influenza virus M2 protein cytoplasmic tail interacts with the M1 protein and influences virus assembly at the site of virus budding
    • Chen BJ, Leser GP, Jackson D, Lamb RA. The influenza virus M2 protein cytoplasmic tail interacts with the M1 protein and influences virus assembly at the site of virus budding. J. Virol. 82(20), 10059-10070 (2008).
    • (2008) J. Virol. , vol.82 , Issue.20 , pp. 10059-10070
    • Chen, B.J.1    Leser, G.P.2    Jackson, D.3    Lamb, R.A.4
  • 115
    • 72649105081 scopus 로고    scopus 로고
    • Matrix protein 2 of influenza A virus blocks autophagosome fusion with lysosomes
    • Gannagé M, Dormann D, Albrecht R et al. Matrix protein 2 of influenza A virus blocks autophagosome fusion with lysosomes. Cell Host Microbe 6(4), 367-380 (2009).
    • (2009) Cell Host Microbe , vol.6 , Issue.4 , pp. 367-380
    • Gannagé, M.1    Dormann, D.2    Albrecht, R.3
  • 116
    • 77951437276 scopus 로고    scopus 로고
    • Influenza virus m2 ion channel protein is necessary for filamentous virion formation
    • Rossman JS, Jing X, Leser GP, Balannik V, Pinto LH, Lamb RA. Influenza virus m2 ion channel protein is necessary for filamentous virion formation. J. Virol. 84(10), 5078-5088 (2010).
    • (2010) J. Virol. , vol.84 , Issue.10 , pp. 5078-5088
    • Rossman, J.S.1    Jing, X.2    Leser, G.P.3    Balannik, V.4    Pinto, L.H.5    Lamb, R.A.6
  • 117
    • 77956637693 scopus 로고    scopus 로고
    • Influenza virus M2 protein mediates ESCRT-independent membrane scission
    • Rossman JS, Jing X, Leser GP, Lamb RA. Influenza virus M2 protein mediates ESCRT-independent membrane scission. Cell 142(6), 902-913 (2010).
    • (2010) Cell , vol.142 , Issue.6 , pp. 902-913
    • Rossman, J.S.1    Jing, X.2    Leser, G.P.3    Lamb, R.A.4
  • 118
    • 79953140465 scopus 로고    scopus 로고
    • Interaction of Hsp40 with influenza virus M2 protein: Implications for PKR signaling pathway
    • Guan Z, Liu D, Mi S et al. Interaction of Hsp40 with influenza virus M2 protein: implications for PKR signaling pathway. Protein Cell 1(10), 944-955 (2010).
    • (2010) Protein Cell , vol.1 , Issue.10 , pp. 944-955
    • Guan, Z.1    Liu, D.2    Mi, S.3
  • 119
    • 65649134734 scopus 로고    scopus 로고
    • Pandemic preparedness: Toward a universal influenza vaccine
    • Roose K, Fiers W, Saelens X. Pandemic preparedness: toward a universal influenza vaccine. Drug News Perspect. 22(2), 80-92 (2009).
    • (2009) Drug News Perspect. , vol.22 , Issue.2 , pp. 80-92
    • Roose, K.1    Fiers, W.2    Saelens, X.3
  • 120
    • 84874076843 scopus 로고    scopus 로고
    • Cutting edge approaches toward novel and cross-protective influenza vaccines
    • von Gabain A, Klade C (Eds). Springer, NY, USA
    • Roose K, Schotsaert M, Bakkouri KE, Schepens B, Fiers W, Saelens X. Cutting edge approaches toward novel and cross-protective influenza vaccines. In: Development of Novel Vaccines. von Gabain A, Klade C (Eds). Springer, NY, USA, 205-232 (2012).
    • (2012) Development of Novel Vaccines , pp. 205-232
    • Roose, K.1    Schotsaert, M.2    Bakkouri, K.E.3    Schepens, B.4    Fiers, W.5    Saelens, X.6
  • 121
    • 40749114009 scopus 로고    scopus 로고
    • The influenza matrix protein 2 as a vaccine target
    • Saelens X. The influenza matrix protein 2 as a vaccine target. Future Virology 3(2), 167-178 (2008).
    • (2008) Future Virology , vol.3 , Issue.2 , pp. 167-178
    • Saelens, X.1
  • 122
    • 65449185906 scopus 로고    scopus 로고
    • Universal M2 ectodomain-based influenza A vaccines: Preclinical and clinical developments
    • Schotsaert M, De Filette M, Fiers W, Saelens X. Universal M2 ectodomain-based influenza A vaccines: preclinical and clinical developments. Expert Rev. Vaccines 8(4), 499-508 (2009).
    • (2009) Expert Rev. Vaccines , vol.8 , Issue.4 , pp. 499-508
    • Schotsaert, M.1    De Filette, M.2    Fiers, W.3    Saelens, X.4
  • 123
    • 0032874490 scopus 로고    scopus 로고
    • A universal influenza A vaccine based on the extracellular domain of the M2 protein
    • Neirynck S, Deroo T, Saelens X, Vanlandschoot P, Jou WM, Fiers W. A universal influenza A vaccine based on the extracellular domain of the M2 protein. Nat. Med. 5(10), 1157-1163 (1999).
    • (1999) Nat. Med. , vol.5 , Issue.10 , pp. 1157-1163
    • Neirynck, S.1    Deroo, T.2    Saelens, X.3    Vanlandschoot, P.4    Jou, W.M.5    Fiers, W.6
  • 124
    • 29544452649 scopus 로고    scopus 로고
    • The universal influenza vaccine M2e-HBc administered intranasally in combination with the adjuvant CTA1-DD provides complete protection
    • De Filette M, Ramne A, Birkett A et al. The universal influenza vaccine M2e-HBc administered intranasally in combination with the adjuvant CTA1-DD provides complete protection. Vaccine 24(5), 544-551 (2006).
    • (2006) Vaccine , vol.24 , Issue.5 , pp. 544-551
    • De Filette, M.1    Ramne, A.2    Birkett, A.3
  • 125
    • 58149116926 scopus 로고    scopus 로고
    • Universal influenza A M2e-HBc vaccine protects against disease even in the presence of pre-existing anti-HBc antibodies
    • De Filette M, Martens W, Smet A et al. Universal influenza A M2e-HBc vaccine protects against disease even in the presence of pre-existing anti-HBc antibodies. Vaccine 26(51), 6503-6507 (2008).
    • (2008) Vaccine , vol.26 , Issue.51 , pp. 6503-6507
    • De Filette, M.1    Martens, W.2    Smet, A.3
  • 126
    • 70349967937 scopus 로고    scopus 로고
    • M2e-based universal influenza A vaccine
    • Fiers W, De Filette M, El Bakkouri K et al. M2e-based universal influenza A vaccine. Vaccine 27(45), 6280-6283 (2009).
    • (2009) Vaccine , vol.27 , Issue.45 , pp. 6280-6283
    • Fiers, W.1    De Filette, M.2    El Bakkouri, K.3
  • 127
    • 70349232585 scopus 로고    scopus 로고
    • Enhancement of mucosal immune response against the M2eHBc+ antigen in mice with the fusion expression products of LTB and M2eHBc+ through mucosal immunization route
    • Zhang GG, Li DX, Zhang HH, Zeng YM, Chen L. Enhancement of mucosal immune response against the M2eHBc+ antigen in mice with the fusion expression products of LTB and M2eHBc+ through mucosal immunization route. Vet. Res. Commun. 33(7), 735-747 (2009).
    • (2009) Vet. Res. Commun. , vol.33 , Issue.7 , pp. 735-747
    • Zhang, G.G.1    Li, D.X.2    Zhang, H.H.3    Zeng, Y.M.4    Chen, L.5
  • 128
    • 77956484700 scopus 로고    scopus 로고
    • Delivery of woodchuck hepatitis virus-like particle presented influenza M2e by recombinant attenuated Salmonella displaying a delayed lysis phenotype
    • Ameiss K, Ashraf S, Kong W et al. Delivery of woodchuck hepatitis virus-like particle presented influenza M2e by recombinant attenuated Salmonella displaying a delayed lysis phenotype. Vaccine 28(41), 6704-6713 (2010).
    • (2010) Vaccine , vol.28 , Issue.41 , pp. 6704-6713
    • Ameiss, K.1    Ashraf, S.2    Kong, W.3
  • 129
    • 35448979958 scopus 로고    scopus 로고
    • Transient expression of the ectodomain of matrix protein 2 (M2e) of avian influenza A virus in plants
    • Nemchinov LG, Natilla A. Transient expression of the ectodomain of matrix protein 2 (M2e) of avian influenza A virus in plants. Protein Expr. Purif. 56(2), 153-159 (2007).
    • (2007) Protein Expr. Purif. , vol.56 , Issue.2 , pp. 153-159
    • Nemchinov, L.G.1    Natilla, A.2
  • 130
    • 44749090233 scopus 로고    scopus 로고
    • Development of a universal influenza A vaccine based on the M2e peptide fused to the papaya mosaic virus (PapMV) vaccine platform
    • Denis J, Acosta-Ramirez E, Zhao Y et al. Development of a universal influenza A vaccine based on the M2e peptide fused to the papaya mosaic virus (PapMV) vaccine platform. Vaccine 26(27-28), 3395-3403 (2008).
    • (2008) Vaccine , vol.26 , Issue.27-28 , pp. 3395-3403
    • Denis, J.1    Acosta-Ramirez, E.2    Zhao, Y.3
  • 131
    • 38349049469 scopus 로고    scopus 로고
    • Efficient induction of mucosal and systemic immune responses by virus-like particles administered intranasally: Implications for vaccine design
    • Bessa J, Schmitz N, Hinton HJ, Schwarz K, Jegerlehner A, Bachmann MF. Efficient induction of mucosal and systemic immune responses by virus-like particles administered intranasally: implications for vaccine design. Eur. J. Immunol. 38(1), 114-126 (2008).
    • (2008) Eur. J. Immunol. , vol.38 , Issue.1 , pp. 114-126
    • Bessa, J.1    Schmitz, N.2    Hinton, H.J.3    Schwarz, K.4    Jegerlehner, A.5    Bachmann, M.F.6
  • 132
    • 77955426962 scopus 로고    scopus 로고
    • Versatile virus-like particle carrier for epitope based vaccines
    • Tissot AC, Renhofa R, Schmitz N et al. Versatile virus-like particle carrier for epitope based vaccines. PLoS One 5(3), e9809 (2010).
    • (2010) PLoS One , vol.5 , Issue.3
    • Tissot, A.C.1    Renhofa, R.2    Schmitz, N.3
  • 133
    • 77955421572 scopus 로고    scopus 로고
    • Hepatitis B vaccines: Protective efficacy and therapeutic potential
    • Michel ML, Tiollais P. Hepatitis B vaccines: protective efficacy and therapeutic potential. Pathol. Biol. 58(4), 288-295 (2010).
    • (2010) Pathol. Biol. , vol.58 , Issue.4 , pp. 288-295
    • Michel, M.L.1    Tiollais, P.2
  • 134
    • 0024347431 scopus 로고
    • Antibodies to synthetic peptides from the preS1 region of the hepatitis B virus (HBV) envelope (env) protein are virus-neutralizing and protective
    • Neurath AR, Seto B, Strick N. Antibodies to synthetic peptides from the preS1 region of the hepatitis B virus (HBV) envelope (env) protein are virus-neutralizing and protective. Vaccine 7(3), 234-236 (1989).
    • (1989) Vaccine , vol.7 , Issue.3 , pp. 234-236
    • Neurath, A.R.1    Seto, B.2    Strick, N.3
  • 135
    • 0022611628 scopus 로고
    • Immune response to the pre-S (1) region of the hepatitis B surface antigen (HBsAg): A pre-S (1)-specific T cell response can bypass nonresponsiveness to the pre-S (2) and S regions of HBsAg
    • Milich DR, McLachlan A, Chisari FV, Kent SB, Thorton GB. Immune response to the pre-S (1) region of the hepatitis B surface antigen (HBsAg): A pre-S (1)-specific T cell response can bypass nonresponsiveness to the pre-S (2) and S regions of HBsAg. J. Immunol. 137(1), 315 (1986).
    • (1986) J. Immunol. , vol.137 , Issue.1 , pp. 315
    • Milich, D.R.1    McLachlan, A.2    Chisari, F.V.3    Kent, S.B.4    Thorton, G.B.5
  • 136
    • 0345528132 scopus 로고    scopus 로고
    • Recombinant hepatitis B core antigen carrying preS1 epitopes induce immune response against chronic HBV infection
    • Chen X, Li M, Le X, Ma W, Zhou B. Recombinant hepatitis B core antigen carrying preS1 epitopes induce immune response against chronic HBV infection. Vaccine 22(3-4), 439-446 (2004).
    • (2004) Vaccine , vol.22 , Issue.3-4 , pp. 439-446
    • Chen, X.1    Li, M.2    Le, X.3    Ma, W.4    Zhou, B.5
  • 137
    • 33847182484 scopus 로고    scopus 로고
    • Immune responses to recombinant Mycobacterium smegmatis expressing fused core protein and preS1 peptide of hepatitis B virus in mice
    • Yue Q, Hu X, Yin W et al. Immune responses to recombinant Mycobacterium smegmatis expressing fused core protein and preS1 peptide of hepatitis B virus in mice. J. Virol. Methods 141(1), 41-48 (2007).
    • (2007) J. Virol. Methods , vol.141 , Issue.1 , pp. 41-48
    • Yue, Q.1    Hu, X.2    Yin, W.3
  • 138
    • 19944432514 scopus 로고    scopus 로고
    • Expression and immunoactivity of chimeric particulate antigens of receptor binding site-core antigen of hepatitis B virus
    • Yang HJ, Chen M, Cheng T et al. Expression and immunoactivity of chimeric particulate antigens of receptor binding site-core antigen of hepatitis B virus. World J. Gastroenterol. 11(4), 492-497 (2005).
    • (2005) World J. Gastroenterol. , vol.11 , Issue.4 , pp. 492-497
    • Yang, H.J.1    Chen, M.2    Cheng, T.3
  • 139
    • 40849139017 scopus 로고    scopus 로고
    • High immunogenicity of a hydrophilic component of the hepatitis B virus preS1 sequence exposed on the surface of three virus-like particle carriers
    • Skrastina D, Bulavaite A, Sominskaya I et al. High immunogenicity of a hydrophilic component of the hepatitis B virus preS1 sequence exposed on the surface of three virus-like particle carriers. Vaccine 26(16), 1972-1981 (2008).
    • (2008) Vaccine , vol.26 , Issue.16 , pp. 1972-1981
    • Skrastina, D.1    Bulavaite, A.2    Sominskaya, I.3
  • 140
    • 79958802112 scopus 로고    scopus 로고
    • N-terminal myristoylation-dependent masking of neutralizing epitopes in the preS1 attachment site of hepatitis B virus
    • Bremer CM, Sominskaya I, Skrastina D et al. N-terminal myristoylation-dependent masking of neutralizing epitopes in the preS1 attachment site of hepatitis B virus. J. Hepatol. 55(1), 29-37 (2011).
    • (2011) J. Hepatol. , vol.55 , Issue.1 , pp. 29-37
    • Bremer, C.M.1    Sominskaya, I.2    Skrastina, D.3
  • 141
    • 33645989987 scopus 로고    scopus 로고
    • Characterization of a hepatitis B and hepatitis delta virus receptor binding site
    • Engelke M, Mills K, Seitz S et al. Characterization of a hepatitis B and hepatitis delta virus receptor binding site. Hepatology 43(4), 750-760 (2006).
    • (2006) Hepatology , vol.43 , Issue.4 , pp. 750-760
    • Engelke, M.1    Mills, K.2    Seitz, S.3
  • 142
    • 0028822367 scopus 로고
    • Myristylation of the hepatitis B virus large surface protein is essential for viral infectivity
    • Gripon P, Le Seyec J, Rumin S, Guguen-Guillouzo C. Myristylation of the hepatitis B virus large surface protein is essential for viral infectivity. Virology 213(2), 292-299 (1995).
    • (1995) Virology , vol.213 , Issue.2 , pp. 292-299
    • Gripon, P.1    Le Seyec, J.2    Rumin, S.3    Guguen-Guillouzo, C.4
  • 143
    • 83155168476 scopus 로고    scopus 로고
    • Hepatitis B virus infection and the risk of hepatocellular carcinoma
    • Tan YJ. Hepatitis B virus infection and the risk of hepatocellular carcinoma. World J. Gastroenterol. 17(44), 4853-4857 (2011).
    • (2011) World J. Gastroenterol. , vol.17 , Issue.44 , pp. 4853-4857
    • Tan, Y.J.1
  • 144
    • 80052947349 scopus 로고    scopus 로고
    • Does antiviral therapy prevent hepatocellular carcinoma? Antivir
    • Kwon H, Lok AS. Does antiviral therapy prevent hepatocellular carcinoma? Antivir. Ther. (Lond.) 16(6), 787-795 (2011).
    • (2011) Ther. (Lond.) , vol.16 , Issue.6 , pp. 787-795
    • Kwon, H.1    Lok, A.S.2
  • 145
    • 84860593438 scopus 로고    scopus 로고
    • A critical evaluation of the preventive effect of antiviral therapy on the development of hepatocellular carcinoma in patients with chronic hepatitis C or B: A novel approach by using meta-regression
    • Shen YC, Hsu C, Cheng CC, Hu FC, Cheng AL. A critical evaluation of the preventive effect of antiviral therapy on the development of hepatocellular carcinoma in patients with chronic hepatitis C or B: A novel approach by using meta-regression. Oncology 82(5), 275-289 (2012).
    • (2012) Oncology , vol.82 , Issue.5 , pp. 275-289
    • Shen, Y.C.1    Hsu, C.2    Cheng, C.C.3    Hu, F.C.4    Cheng, A.L.5
  • 146
    • 80052411388 scopus 로고    scopus 로고
    • Hepatitis B virus X gene and hepatocarcinogenesis
    • Ng SA, Lee C. Hepatitis B virus X gene and hepatocarcinogenesis. J. Gastroenterol. 46(8), 974-990 (2011).
    • (2011) J. Gastroenterol. , vol.46 , Issue.8 , pp. 974-990
    • Ng, S.A.1    Lee, C.2
  • 147
    • 0019950441 scopus 로고
    • Epitope-specific regulation II. A bistable, Igh-restricted regulatory mechanism central to immunologic memory
    • Herzenberg LA, Tokuhisa T, Parks DR, Herzenberg LA. Epitope-specific regulation. II. A bistable, Igh-restricted regulatory mechanism central to immunologic memory. J. Exp. Med. 155(6), 1741-1753 (1982).
    • (1982) J. Exp. Med. , vol.155 , Issue.6 , pp. 1741-1753
    • Herzenberg, L.A.1    Tokuhisa, T.2    Parks, D.R.3    Herzenberg, L.A.4
  • 148
    • 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 et al. 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(30), 3973-3983 (2005).
    • (2005) Vaccine , vol.23 , Issue.30 , pp. 3973-3983
    • Geldmacher, A.1    Skrastina, D.2    Borisova, G.3
  • 149
    • 0141814660 scopus 로고    scopus 로고
    • Diversity of core antigen epitopes of hepatitis B virus
    • Belnap DM, Watts NR, Conway JF et al. Diversity of core antigen epitopes of hepatitis B virus. Proc. Natl Acad. Sci. USA 100(19), 10884-10889 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , Issue.19 , pp. 10884-10889
    • Belnap, D.M.1    Watts, N.R.2    Conway, J.F.3
  • 150
    • 33846336495 scopus 로고    scopus 로고
    • Improved design and intranasal delivery of an M2e-based human influenza A vaccine
    • De Filette M, Fiers W, Martens W et al. Improved design and intranasal delivery of an M2e-based human influenza A vaccine. Vaccine 24(44-46), 6597-6601 (2006).
    • (2006) Vaccine , vol.24 , Issue.44-46 , pp. 6597-6601
    • De Filette, M.1    Fiers, W.2    Martens, W.3
  • 152
    • 0025245580 scopus 로고
    • Cellular immune response to hepatitis B virus-encoded antigens in acute and chronic hepatitis B virus infection
    • Ferrari C, Penna A, Bertoletti A et al. Cellular immune response to hepatitis B virus-encoded antigens in acute and chronic hepatitis B virus infection. J. Immunol. 145(10), 3442-3449 (1990).
    • (1990) J. Immunol. , vol.145 , Issue.10 , pp. 3442-3449
    • Ferrari, C.1    Penna, A.2    Bertoletti, A.3
  • 153
    • 27144545321 scopus 로고    scopus 로고
    • Comparative antigenicity and immunogenicity of hepadnavirus core proteins
    • Billaud JN, Peterson D, Schödel F et al. Comparative antigenicity and immunogenicity of hepadnavirus core proteins. J. Virol. 79(21), 13641-13655 (2005).
    • (2005) J. Virol. , vol.79 , Issue.21 , pp. 13641-13655
    • Billaud, J.N.1    Peterson, D.2    Schödel, F.3
  • 154
    • 33846240816 scopus 로고    scopus 로고
    • Advantages to the use of rodent hepadnavirus core proteins as vaccine platforms
    • Billaud JN, Peterson D, Lee BO et al. Advantages to the use of rodent hepadnavirus core proteins as vaccine platforms. Vaccine 25(9), 1593-1606 (2007).
    • (2007) Vaccine , vol.25 , Issue.9 , pp. 1593-1606
    • Billaud, J.N.1    Peterson, D.2    Lee, B.O.3
  • 155
    • 0037094095 scopus 로고    scopus 로고
    • Priming Th1 immunity to viral core particles is facilitated by trace amounts of RNA bound to its arginine-rich domain
    • Riedl P, Stober D, Oehninger C, Melber K, Reimann J, Schirmbeck R. Priming Th1 immunity to viral core particles is facilitated by trace amounts of RNA bound to its arginine-rich domain. J. Immunol. 168(10), 4951-4959 (2002).
    • (2002) J. Immunol. , vol.168 , Issue.10 , pp. 4951-4959
    • Riedl, P.1    Stober, D.2    Oehninger, C.3    Melber, K.4    Reimann, J.5    Schirmbeck, R.6
  • 156
    • 84864607163 scopus 로고    scopus 로고
    • Chimeric Hepatitis B core antigen virus-like particles displaying the envelope domain III of dengue virus type 2
    • Arora U, Tyagi P, Swaminathan S, Khanna N. Chimeric Hepatitis B core antigen virus-like particles displaying the envelope domain III of dengue virus type 2. J. Nanobiotechnology 10, 30 (2012).
    • (2012) J. Nanobiotechnology , vol.10 , pp. 30
    • Arora, U.1    Tyagi, P.2    Swaminathan, S.3    Khanna, N.4
  • 157
    • 68049088631 scopus 로고    scopus 로고
    • Screen of multifunctional monoclonal antibodies against hepatitis B core virus-like particles
    • Sun C, Ding FX, Wang F et al. Screen of multifunctional monoclonal antibodies against hepatitis B core virus-like particles. Microbiol. Immunol. 53(6), 340-348 (2009).
    • (2009) Microbiol. Immunol. , vol.53 , Issue.6 , pp. 340-348
    • Sun, C.1    Ding, F.X.2    Wang, F.3
  • 158
    • 84555177509 scopus 로고    scopus 로고
    • A bi-functional hepatitis B virus core antigen (HBcAg) chimera activates HBcAg-specific T cells and preS1-specific antibodies
    • Malik IR, Chen A, Brass A et al. A bi-functional hepatitis B virus core antigen (HBcAg) chimera activates HBcAg-specific T cells and preS1-specific antibodies. Scand. J. Infect. Dis. 44(1), 55-59 (2012).
    • (2012) Scand. J. Infect. Dis. , vol.44 , Issue.1 , pp. 55-59
    • Malik, I.R.1    Chen, A.2    Brass, A.3
  • 159
    • 29844439692 scopus 로고    scopus 로고
    • Immunogenicity of the epitope of the foot-andmouth disease virus fused with a hepatitis B core protein as expressed in transgenic tobacco
    • Huang Y, Liang W, Wang Y et al. Immunogenicity of the epitope of the foot-andmouth disease virus fused with a hepatitis B core protein as expressed in transgenic tobacco. Viral Immunol. 18(4), 668-677 (2005).
    • (2005) Viral Immunol. , vol.18 , Issue.4 , pp. 668-677
    • Huang, Y.1    Liang, W.2    Wang, Y.3
  • 160
    • 33947609904 scopus 로고    scopus 로고
    • Enhanced immunogenicity of modified hepatitis B virus core particle fused with multiepitopes of foot-and-mouth disease virus
    • Zhang YL, Guo YJ, Wang KY et al. Enhanced immunogenicity of modified hepatitis B virus core particle fused with multiepitopes of foot-and-mouth disease virus. Scand. J. Immunol. 65(4), 320-328 (2007).
    • (2007) Scand. J. Immunol. , vol.65 , Issue.4 , pp. 320-328
    • Zhang, Y.L.1    Guo, Y.J.2    Wang, K.Y.3
  • 161
    • 0028842722 scopus 로고
    • Theileria annulata sporozoite antigen fused to hepatitis B core antigen used in a vaccination trial
    • Boulter NR, Glass EJ, Knight PA, Bell-Sakyi L, Brown CG, Hall R. Theileria annulata sporozoite antigen fused to hepatitis B core antigen used in a vaccination trial. Vaccine 13(13), 1152-1160 (1995).
    • (1995) Vaccine , vol.13 , Issue.13 , pp. 1152-1160
    • Boulter, N.R.1    Glass, E.J.2    Knight, P.A.3    Bell-Sakyi, L.4    Brown, C.G.5    Hall, R.6
  • 162
    • 0026458897 scopus 로고
    • Immunogenicity of recombinant core particles of hepatitis B virus containing epitopes of human immunodeficiency virus core antigen
    • Ulrich R, Borisova GP, Gren E et al. Immunogenicity of recombinant core particles of hepatitis B virus containing epitopes of human immunodeficiency virus core antigen. Arch. Virol. 126(1-4), 321-328 (1992).
    • (1992) Arch. Virol. , vol.126 , Issue.1-4 , pp. 321-328
    • Ulrich, R.1    Borisova, G.P.2    Gren, E.3
  • 163
    • 0024339070 scopus 로고
    • Immunogenicity of peptide fusions to hepatitis B virus core antigen
    • Stahl SJ, Murray K. Immunogenicity of peptide fusions to hepatitis B virus core antigen. Proc. Natl Acad. Sci. USA 86(16), 6283-6287 (1989).
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , Issue.16 , pp. 6283-6287
    • Stahl, S.J.1    Murray, K.2
  • 164
    • 0027318495 scopus 로고
    • Principal neutralizing domain of HIV-1 is highly immunogenic when expressed on the surface of hepatitis B core particles
    • von Brunn A, Brand M, Reichhuber C, Morys-Wortmann C, Deinhardt F, Schödel F. Principal neutralizing domain of HIV-1 is highly immunogenic when expressed on the surface of hepatitis B core particles. Vaccine 11(8), 817-824 (1993).
    • (1993) Vaccine , vol.11 , Issue.8 , pp. 817-824
    • Von Brunn, A.1    Brand, M.2    Reichhuber, C.3    Morys-Wortmann, C.4    Deinhardt, F.5    Schödel, F.6
  • 165
    • 2942695979 scopus 로고    scopus 로고
    • Hemagglutinating virus of Japan protein is efficient for induction of CD4+ T-cell response by a hepatitis B core particlebased HIV vaccine
    • Takeda S, Shiosaki K, Kaneda Y et al. Hemagglutinating virus of Japan protein is efficient for induction of CD4+ T-cell response by a hepatitis B core particlebased HIV vaccine. Clin. Immunol. 112(1), 92-105 (2004).
    • (2004) Clin. Immunol. , vol.112 , Issue.1 , pp. 92-105
    • Takeda, S.1    Shiosaki, K.2    Kaneda, Y.3
  • 166
    • 84873097698 scopus 로고    scopus 로고
    • The amount and integrity of mtDNA in maize decline with development
    • doi: 10.1007/s00425-012-1802-z Epub ahead of print
    • Oldenburg DJ, Kumar RA, Bendich AJ. The amount and integrity of mtDNA in maize decline with development. Planta doi:10.1007/s00425-012-1802-z (2012) (Epub ahead of print).
    • Planta , Issue.2012
    • Oldenburg, D.J.1    Kumar, R.A.2    Bendich, A.J.3
  • 167
    • 2542463976 scopus 로고    scopus 로고
    • An amino-terminal segment of hantavirus nucleocapsid protein presented on hepatitis B virus core particles induces a strong and highly cross-reactive antibody response in mice
    • Geldmacher A, Skrastina D, Petrovskis I et al. An amino-terminal segment of hantavirus nucleocapsid protein presented on hepatitis B virus core particles induces a strong and highly cross-reactive antibody response in mice. Virology 323(1), 108-119 (2004).
    • (2004) Virology , vol.323 , Issue.1 , pp. 108-119
    • Geldmacher, A.1    Skrastina, D.2    Petrovskis, I.3
  • 168
    • 18344370048 scopus 로고    scopus 로고
    • Evaluation of HBs, HBc, and frCP virus-like particles for expression of human papillomavirus 16 E7 oncoprotein epitopes
    • Pumpens P, Razanskas R, Pushko P et al. Evaluation of HBs, HBc, and frCP virus-like particles for expression of human papillomavirus 16 E7 oncoprotein epitopes. Intervirology 45(1), 24-32 (2002).
    • (2002) Intervirology , vol.45 , Issue.1 , pp. 24-32
    • Pumpens, P.1    Razanskas, R.2    Pushko, P.3
  • 169
    • 33846219835 scopus 로고    scopus 로고
    • Development of hepatitis C virus vaccine using hepatitis B core antigen as immuno-carrier
    • Chen JY, Li F. Development of hepatitis C virus vaccine using hepatitis B core antigen as immuno-carrier. World J. Gastroenterol. 12(48), 7774-7778 (2006).
    • (2006) World J. Gastroenterol. , vol.12 , Issue.48 , pp. 7774-7778
    • Chen, J.Y.1    Li, F.2
  • 170
    • 77953148122 scopus 로고    scopus 로고
    • Construction and immunological evaluation of multivalent hepatitis B virus (HBV) core virus-like particles carrying HBV and HCV epitopes
    • Sominskaya I, Skrastina D, Dislers A et al. Construction and immunological evaluation of multivalent hepatitis B virus (HBV) core virus-like particles carrying HBV and HCV epitopes. Clin. Vaccine Immunol. 17(6), 1027-1033 (2010).
    • (2010) Clin. Vaccine Immunol. , vol.17 , Issue.6 , pp. 1027-1033
    • Sominskaya, I.1    Skrastina, D.2    Dislers, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.