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Volumn 303, Issue 2, 2003, Pages 427-432

The influence of glycosylation on secretion, stability, and immunogenicity of recombinant HBV pre-S antigen synthesized in Saccharomyces cerevisiae

Author keywords

HBV pre S; Immunogenicity; N glycosylation; Proteolysis; Secretion

Indexed keywords

GLYCAN DERIVATIVE; MEMBRANE ANTIGEN; NEUTRALIZING ANTIBODY; PROTEINASE;

EID: 0037418742     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-291X(03)00351-6     Document Type: Article
Times cited : (44)

References (22)
  • 1
    • 0023718069 scopus 로고
    • The pre-S region of hepadnavirus envelope proteins
    • Neurath A.R., Kent S.B.H. The pre-S region of hepadnavirus envelope proteins. Adv. Virus Res. 34:1988;65-142.
    • (1988) Adv. Virus Res. , vol.34 , pp. 65-142
    • Neurath, A.R.1    Kent, S.B.H.2
  • 4
    • 0028172936 scopus 로고
    • Improved immunogenicity in mice of a mammalian cell-derived recombinant hepatitis B vaccine containing pre-S1 and pre-S2 antigens as compared with conventional yeast-derived vaccines
    • Shouval D., Ilan Y., Adler R., Deepen R., Panet A., Even-Chen Z., Gorecki M., Gerlich W.H. Improved immunogenicity in mice of a mammalian cell-derived recombinant hepatitis B vaccine containing pre-S1 and pre-S2 antigens as compared with conventional yeast-derived vaccines. Vaccine. 12:1994;1453-1459.
    • (1994) Vaccine , vol.12 , pp. 1453-1459
    • Shouval, D.1    Ilan, Y.2    Adler, R.3    Deepen, R.4    Panet, A.5    Even-Chen, Z.6    Gorecki, M.7    Gerlich, W.H.8
  • 5
    • 0022538381 scopus 로고
    • Identification and chemical synthesis of a host cell receptor binding site on hepatitis B virus
    • Neurath A.R., Kent S.B.H., Strick N., Parker K. Identification and chemical synthesis of a host cell receptor binding site on hepatitis B virus. Cell. 46:1986;429-436.
    • (1986) Cell , vol.46 , pp. 429-436
    • Neurath, A.R.1    Kent, S.B.H.2    Strick, N.3    Parker, K.4
  • 6
    • 0024347431 scopus 로고
    • Antibodies to synthetic peptides from the preS1 region of the hepatitis B virus envelope protein are virus-neutralizing and protective
    • Neurath A.R., Seto B., Strick N. Antibodies to synthetic peptides from the preS1 region of the hepatitis B virus envelope protein are virus-neutralizing and protective. Vaccine. 7:1989;234-236.
    • (1989) Vaccine , vol.7 , pp. 234-236
    • Neurath, A.R.1    Seto, B.2    Strick, N.3
  • 7
    • 0033522817 scopus 로고    scopus 로고
    • T-cell and antibody response characterization of a new recombinant pre-S1, pre-S2 and SHBs antigen-containing hepatitis B vaccine; Demonstration of superior anti-SHBs antibody induction in responder mice
    • Jones C.D., Page M., Bacon A., Cahill E., Bentley M., Chatfield S.N. T-cell and antibody response characterization of a new recombinant pre-S1, pre-S2 and SHBs antigen-containing hepatitis B vaccine; demonstration of superior anti-SHBs antibody induction in responder mice. Vaccine. 17:1999;2528-2537.
    • (1999) Vaccine , vol.17 , pp. 2528-2537
    • Jones, C.D.1    Page, M.2    Bacon, A.3    Cahill, E.4    Bentley, M.5    Chatfield, S.N.6
  • 8
    • 0034880488 scopus 로고    scopus 로고
    • A novel, recombinant triple antigen hepatitis B vaccine (Hepacare)
    • Page M., Jones C.D., Bailey C. A novel, recombinant triple antigen hepatitis B vaccine (Hepacare). Intervirology. 44:2001;88-97.
    • (2001) Intervirology , vol.44 , pp. 88-97
    • Page, M.1    Jones, C.D.2    Bailey, C.3
  • 9
    • 0026778048 scopus 로고
    • Foreign gene expression in yeast: A review
    • Romanos M.A., Score C.A., Clare J.J. Foreign gene expression in yeast: a review. Yeast. 8:1992;423-488.
    • (1992) Yeast , vol.8 , pp. 423-488
    • Romanos, M.A.1    Score, C.A.2    Clare, J.J.3
  • 10
    • 0344605531 scopus 로고    scopus 로고
    • Enhanced secretion of human granulocyte colony-stimulating factor directed by a novel hybrid fusion peptide from recombinant Saccharomyces cerevisiae at high cell concentration
    • Bae C.S., Yang D.S., Jang K.R., Seong B.L., Lee J. Enhanced secretion of human granulocyte colony-stimulating factor directed by a novel hybrid fusion peptide from recombinant Saccharomyces cerevisiae at high cell concentration. Biotechnol. Bioeng. 57:1998;600-609.
    • (1998) Biotechnol. Bioeng. , vol.57 , pp. 600-609
    • Bae, C.S.1    Yang, D.S.2    Jang, K.R.3    Seong, B.L.4    Lee, J.5
  • 11
    • 0033198602 scopus 로고    scopus 로고
    • Novel secretion system of recombinant Saccharomyces cerevisiae using an N-terminus residue of human IL-1β as secretion enhancer
    • Lee J., Choi S.I., Jang J.S., Jang K.R., Moon J.W., Bae C.S., Yang D.S., Seong B.L. Novel secretion system of recombinant Saccharomyces cerevisiae using an N-terminus residue of human IL-1β as secretion enhancer. Biotechnol. Prog. 15:1999;884-890.
    • (1999) Biotechnol. Prog. , vol.15 , pp. 884-890
    • Lee, J.1    Choi, S.I.2    Jang, J.S.3    Jang, K.R.4    Moon, J.W.5    Bae, C.S.6    Yang, D.S.7    Seong, B.L.8
  • 12
    • 0023061489 scopus 로고
    • A novel leader peptide which allows efficient secretion of a fragment human interleukin 1 β in Saccharomyces cerevisiae
    • Baldari C., Murray J.A., Ghiara P., Cesareni G., Galeotti C.L. A novel leader peptide which allows efficient secretion of a fragment human interleukin 1 β in Saccharomyces cerevisiae. EMBO J. 6:1987;229-234.
    • (1987) EMBO J. , vol.6 , pp. 229-234
    • Baldari, C.1    Murray, J.A.2    Ghiara, P.3    Cesareni, G.4    Galeotti, C.L.5
  • 13
    • 0003903343 scopus 로고
    • Molecular Cloning: A Laboratory Manual
    • New York: Cold Spring Harbor Laboratory Press
    • Sambrook J., Fritsch E.F., Maniatis T. Molecular Cloning: A Laboratory Manual. second ed. 1989;Cold Spring Harbor Laboratory Press, New York.
    • (1989) second ed.
    • Sambrook, J.1    Fritsch, E.F.2    Maniatis, T.3
  • 14
    • 0022459886 scopus 로고
    • Identification and characterization of conserved and variable regions in the envelope gene of HTLV-III/LAV the retrovirus of AIDS
    • Starcich B.R., Hahn B.H., Shaw G.M. Identification and characterization of conserved and variable regions in the envelope gene of HTLV-III/LAV the retrovirus of AIDS. Cell. 45:1986;637-648.
    • (1986) Cell , vol.45 , pp. 637-648
    • Starcich, B.R.1    Hahn, B.H.2    Shaw, G.M.3
  • 15
    • 0035851347 scopus 로고    scopus 로고
    • Enhanced immunogenicity of a human immunodeficiency virus type 1 env DNA vaccine by manipulating N-glycosylation signals effects of elimination of the V3 N306 glycan
    • Bolmstedt A., Hinkula J., Rowcliffe E., Biller M., Wahren B., Olofsson S. Enhanced immunogenicity of a human immunodeficiency virus type 1 env DNA vaccine by manipulating N-glycosylation signals effects of elimination of the V3 N306 glycan. Vaccine. 20:2002;397-405.
    • (2002) Vaccine , vol.20 , pp. 397-405
    • Bolmstedt, A.1    Hinkula, J.2    Rowcliffe, E.3    Biller, M.4    Wahren, B.5    Olofsson, S.6
  • 16
    • 0037084285 scopus 로고    scopus 로고
    • Effect of C-domain N-glycosylation and deletion on rat pancreatic α-amylase secretion and activity
    • Doyon Y., Home W., Daull P., LeBel D. Effect of C-domain N-glycosylation and deletion on rat pancreatic α-amylase secretion and activity. Biochem. J. 362:2002;259-264.
    • (2002) Biochem. J. , vol.362 , pp. 259-264
    • Doyon, Y.1    Home, W.2    Daull, P.3    LeBel, D.4
  • 17
    • 0031815514 scopus 로고    scopus 로고
    • Effect of N-linked glycosylation on secretion activity and stability of α-amylase from Aspergillus oryzae
    • Eriksen S.H., Jensen B., Olsen J. Effect of N-linked glycosylation on secretion activity and stability of α-amylase from Aspergillus oryzae. Curr. Microbiol. 37:1998;117-122.
    • (1998) Curr. Microbiol. , vol.37 , pp. 117-122
    • Eriksen, S.H.1    Jensen, B.2    Olsen, J.3
  • 18
    • 0032052908 scopus 로고    scopus 로고
    • Structural studies of α-N-acetylgalactosaminidase: Effect of glycosylation on the level of expression, secretion efficiency and enzyme activity
    • Zhu A., Wang Z.K., Beavis R. Structural studies of α-N-acetylgalactosaminidase: effect of glycosylation on the level of expression, secretion efficiency and enzyme activity. Arch. Biochem. Biophys. 352:1998;1-8.
    • (1998) Arch. Biochem. Biophys. , vol.352 , pp. 1-8
    • Zhu, A.1    Wang, Z.K.2    Beavis, R.3
  • 19
    • 0027301094 scopus 로고
    • Glycosylation of active human rennin is necessary for secretion: Effect of targeted modifications of Asn-5 and Asn-75
    • Rothwell V., Kosowski S., Hadjilambris O., Baska R., Norman J. Glycosylation of active human rennin is necessary for secretion: effect of targeted modifications of Asn-5 and Asn-75. DNA Cell Biol. 12:1993;291-298.
    • (1993) DNA Cell Biol. , vol.12 , pp. 291-298
    • Rothwell, V.1    Kosowski, S.2    Hadjilambris, O.3    Baska, R.4    Norman, J.5
  • 20
    • 0025883650 scopus 로고
    • Secretion of N-glycosylated interleukin-1β in Saccharomyces cerevisiae using a leader peptide from Candida albicans. Effect of N-linked glycosylation on biological activity
    • Livi G.P., Lillquist J.S., Miles L.M., Ferrara A., Sathe G.M., Simon P.L., Meyers C.A., Gorman J.A., Young P.R. Secretion of N-glycosylated interleukin-1β in Saccharomyces cerevisiae using a leader peptide from Candida albicans. Effect of N-linked glycosylation on biological activity. J. Biol. Chem. 266:1991;15348-15355.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15348-15355
    • Livi, G.P.1    Lillquist, J.S.2    Miles, L.M.3    Ferrara, A.4    Sathe, G.M.5    Simon, P.L.6    Meyers, C.A.7    Gorman, J.A.8    Young, P.R.9
  • 21
    • 0034053424 scopus 로고    scopus 로고
    • Characteristics of glycosylated streptokinase secreted from Pichia pastoris: Enhanced resistance of SK to proteolysis by glycosylation
    • Pratap J., Rajamohan G., Dikshit K.L. Characteristics of glycosylated streptokinase secreted from Pichia pastoris: enhanced resistance of SK to proteolysis by glycosylation. Appl. Microbiol. Biotechnol. 53:2000;469-475.
    • (2000) Appl. Microbiol. Biotechnol. , vol.53 , pp. 469-475
    • Pratap, J.1    Rajamohan, G.2    Dikshit, K.L.3
  • 22
    • 0035253348 scopus 로고    scopus 로고
    • Granzyme B proteolysis of a neuronal glutamate receptor generates an autoantigen and is modulated by glycosylation
    • Gahring L., Carlson N.G., Meyer E.L., Rogers S.W. Granzyme B proteolysis of a neuronal glutamate receptor generates an autoantigen and is modulated by glycosylation. J. Immunol. 166:2001;1433-1438.
    • (2001) J. Immunol. , vol.166 , pp. 1433-1438
    • Gahring, L.1    Carlson, N.G.2    Meyer, E.L.3    Rogers, S.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.