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Volumn 13, Issue 2, 2015, Pages 222-234

Detailed functional characterization of glycosylated and nonglycosylated variants of malaria vaccine candidate PfAMA1 produced in Nicotiana benthamiana and analysis of growth inhibitory responses in rabbits

Author keywords

Glycosylation; Malaria; Plants; Plasmodium falciparum; Transient expression; Vaccine

Indexed keywords

EUKARYOTA; NICOTIANA BENTHAMIANA; ORYCTOLAGUS CUNICULUS; PICHIA PASTORIS; PLASMODIUM FALCIPARUM;

EID: 84922756512     PISSN: 14677644     EISSN: 14677652     Source Type: Journal    
DOI: 10.1111/pbi.12255     Document Type: Article
Times cited : (31)

References (64)
  • 2
    • 0031986201 scopus 로고    scopus 로고
    • Immunisation with recombinant AMA-1 protects mice against infection with Plasmodium chabaudi
    • Anders, R.F., Crewther, P.E., Edwards, S., Margetts, M., Matthew, M.L., Pollock, B. and Pye, D. (1998) Immunisation with recombinant AMA-1 protects mice against infection with Plasmodium chabaudi. Vaccine, 16, 240-247.
    • (1998) Vaccine , vol.16 , pp. 240-247
    • Anders, R.F.1    Crewther, P.E.2    Edwards, S.3    Margetts, M.4    Matthew, M.L.5    Pollock, B.6    Pye, D.7
  • 3
    • 0038581900 scopus 로고    scopus 로고
    • Immunoreactivity in mammals of two typical plant glyco-epitopes, core alpha(1,3)-fucose and core xylose
    • Bardor, M., Faveeuw, C., Fitchette, A.-C., Gilbert, D., Galas, L., Trottein, F., Faye, L. and Lerouge, P. (2003) Immunoreactivity in mammals of two typical plant glyco-epitopes, core alpha(1, 3)-fucose and core xylose. Glycobiology, 13, 427-434.
    • (2003) Glycobiology , vol.13 , pp. 427-434
    • Bardor, M.1    Faveeuw, C.2    Fitchette, A.-C.3    Gilbert, D.4    Galas, L.5    Trottein, F.6    Faye, L.7    Lerouge, P.8
  • 4
    • 0026009173 scopus 로고
    • Recombinant Pfs25 protein of Plasmodium falciparum elicits malaria transmission-blocking immunity in experimental animals
    • Barr, P.J., Green, K.M., Gibson, H.L., Bathurst, I.C., Quakyi, I.A. and Kaslow, D.C. (1991) Recombinant Pfs25 protein of Plasmodium falciparum elicits malaria transmission-blocking immunity in experimental animals. J. Exp. Med. 174, 1203-1208.
    • (1991) J. Exp. Med. , vol.174 , pp. 1203-1208
    • Barr, P.J.1    Green, K.M.2    Gibson, H.L.3    Bathurst, I.C.4    Quakyi, I.A.5    Kaslow, D.C.6
  • 5
    • 80054048785 scopus 로고    scopus 로고
    • Affinity purification of a framework 1 engineered mouse/human chimeric IgA2 antibody from tobacco
    • Boes, A., Spiegel, H., Delbrück, H., Fischer, R., Schillberg, S. and Sack, M. (2011) Affinity purification of a framework 1 engineered mouse/human chimeric IgA2 antibody from tobacco. Biotechnol. Bioeng. 108, 2804-2814.
    • (2011) Biotechnol. Bioeng. , vol.108 , pp. 2804-2814
    • Boes, A.1    Spiegel, H.2    Delbrück, H.3    Fischer, R.4    Schillberg, S.5    Sack, M.6
  • 6
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.1
  • 8
    • 84864948329 scopus 로고    scopus 로고
    • Overview of plant-made vaccine antigens against malaria
    • Clemente, M. and Corigliano, M.G. (2012) Overview of plant-made vaccine antigens against malaria. J. Biomed. Biotechnol. 2012, 206918.
    • (2012) J. Biomed. Biotechnol. , vol.2012 , pp. 206918
    • Clemente, M.1    Corigliano, M.G.2
  • 9
    • 0035183986 scopus 로고    scopus 로고
    • Rapid and precise epitope mapping of monoclonal antibodies against Plasmodium falciparum AMA1 by combined phage display of fragments and random peptides
    • Coley, A.M., Campanale, N.V., Casey, J.L., Hodder, A.N., Crewther, P.E., Anders, R.F., Tilley, L.M. and Foley, M. (2001) Rapid and precise epitope mapping of monoclonal antibodies against Plasmodium falciparum AMA1 by combined phage display of fragments and random peptides. Protein Eng. 14, 691-698.
    • (2001) Protein Eng. , vol.14 , pp. 691-698
    • Coley, A.M.1    Campanale, N.V.2    Casey, J.L.3    Hodder, A.N.4    Crewther, P.E.5    Anders, R.F.6    Tilley, L.M.7    Foley, M.8
  • 11
    • 34147169102 scopus 로고    scopus 로고
    • Fine mapping of an epitope recognized by an invasion-inhibitory monoclonal antibody on the malaria vaccine candidate apical membrane antigen 1
    • Collins, C.R., Withers-Martinez, C., Bentley, G.A., Batchelor, A.H., Thomas, A.W. and Blackman, M.J. (2007) Fine mapping of an epitope recognized by an invasion-inhibitory monoclonal antibody on the malaria vaccine candidate apical membrane antigen 1. J. Biol. Chem. 282, 7431-7441.
    • (2007) J. Biol. Chem. , vol.282 , pp. 7431-7441
    • Collins, C.R.1    Withers-Martinez, C.2    Bentley, G.A.3    Batchelor, A.H.4    Thomas, A.W.5    Blackman, M.J.6
  • 12
    • 11144305228 scopus 로고    scopus 로고
    • Allele specificity of naturally acquired antibody responses against Plasmodium falciparum apical membrane antigen 1
    • Cortes, A., Mellombo, M., Masciantonio, R., Murphy, V.J., Reeder, J.C. and Anders, R.F. (2005) Allele specificity of naturally acquired antibody responses against Plasmodium falciparum apical membrane antigen 1. Infect. Immun. 73, 422-430.
    • (2005) Infect. Immun. , vol.73 , pp. 422-430
    • Cortes, A.1    Mellombo, M.2    Masciantonio, R.3    Murphy, V.J.4    Reeder, J.C.5    Anders, R.F.6
  • 13
    • 0023769849 scopus 로고
    • Vaccination trials in rhesus monkeys with a minor, invariant, Plasmodium knowlesi 66 kD merozoite antigen
    • Deans, J.A., Knight, A.M., Jean, W.C., Waters, A.P., Cohen, S. and Mitchell, G.H. (1988) Vaccination trials in rhesus monkeys with a minor, invariant, Plasmodium knowlesi 66 kD merozoite antigen. Parasite Immunol. 10, 535-552.
    • (1988) Parasite Immunol. , vol.10 , pp. 535-552
    • Deans, J.A.1    Knight, A.M.2    Jean, W.C.3    Waters, A.P.4    Cohen, S.5    Mitchell, G.H.6
  • 15
    • 55049101497 scopus 로고    scopus 로고
    • Production, quality control, stability and pharmacotoxicity of cGMP-produced Plasmodium falciparum AMA1 FVO strain ectodomain expressed in Pichia pastoris
    • Faber, B.W., Remarque, E.J., Kocken, C.H., Cheront, P., Cingolani, D., Xhonneux, F., Jurado, M., Haumont, M., Jepsen, S., Leroy, O. and Thomas, A.W. (2008) Production, quality control, stability and pharmacotoxicity of cGMP-produced Plasmodium falciparum AMA1 FVO strain ectodomain expressed in Pichia pastoris. Vaccine, 26, 6143-6150.
    • (2008) Vaccine , vol.26 , pp. 6143-6150
    • Faber, B.W.1    Remarque, E.J.2    Kocken, C.H.3    Cheront, P.4    Cingolani, D.5    Xhonneux, F.6    Jurado, M.7    Haumont, M.8    Jepsen, S.9    Leroy, O.10    Thomas, A.W.11
  • 19
    • 84881354730 scopus 로고    scopus 로고
    • Commercial aspects of pharmaceutical protein production in plants
    • Fischer, R., Schillberg, S., Buyel, J.F. and Twyman, R.M. (2013) Commercial aspects of pharmaceutical protein production in plants. Curr. Pharm. Des. 19, 5471-5477.
    • (2013) Curr. Pharm. Des. , vol.19 , pp. 5471-5477
    • Fischer, R.1    Schillberg, S.2    Buyel, J.F.3    Twyman, R.M.4
  • 21
    • 21544455223 scopus 로고    scopus 로고
    • Posttranslational modification of recombinant Plasmodium falciparum apical membrane antigen 1: impact on functional immune responses to a malaria vaccine candidate
    • Giersing, B., Miura, K., Shimp, R., Wang, J., Zhou, H., Orcutt, A., Stowers, A., Saul, A., Miller, L.H., Long, C.A. and Singh, S. (2005) Posttranslational modification of recombinant Plasmodium falciparum apical membrane antigen 1: impact on functional immune responses to a malaria vaccine candidate. Infect. Immun. 73, 3963-3970.
    • (2005) Infect. Immun. , vol.73 , pp. 3963-3970
    • Giersing, B.1    Miura, K.2    Shimp, R.3    Wang, J.4    Zhou, H.5    Orcutt, A.6    Stowers, A.7    Saul, A.8    Miller, L.H.9    Long, C.A.10    Singh, S.11
  • 22
    • 84875988564 scopus 로고    scopus 로고
    • Rapid and scalable plant-based production of a cholera toxin B subunit variant to aid in mass vaccination against cholera outbreaks
    • Hamorsky, K.T., Kouokam, J.C., Bennett, L.J., Baldauf, K.J., Kajiura, H., Fujiyama, K. and Matoba, N. (2013) Rapid and scalable plant-based production of a cholera toxin B subunit variant to aid in mass vaccination against cholera outbreaks. PLoS Negl. Trop. Dis. 7, e2046.
    • (2013) PLoS Negl. Trop. Dis. , vol.7 , pp. e2046
    • Hamorsky, K.T.1    Kouokam, J.C.2    Bennett, L.J.3    Baldauf, K.J.4    Kajiura, H.5    Fujiyama, K.6    Matoba, N.7
  • 24
    • 0019837431 scopus 로고
    • Complete in vitro maturation of Plasmodium falciparum gametocytes
    • Ifediba, T. and Vanderberg, J.P. (1981) Complete in vitro maturation of Plasmodium falciparum gametocytes. Nature, 294, 364-366.
    • (1981) Nature , vol.294 , pp. 364-366
    • Ifediba, T.1    Vanderberg, J.P.2
  • 25
    • 33846781441 scopus 로고    scopus 로고
    • Cross-reactivity studies of an anti-Plasmodium vivax apical membrane antigen 1 monoclonal antibody: binding and structural characterisation
    • Igonet, S., Vulliez-Le Normand, B., Faure, G., Riottot, M.M., Kocken, C.H., Thomas, A.W. and Bentley, G.A. (2007) Cross-reactivity studies of an anti-Plasmodium vivax apical membrane antigen 1 monoclonal antibody: binding and structural characterisation. J. Mol. Biol., 366, 1523-1537.
    • (2007) J. Mol. Biol. , vol.366 , pp. 1523-1537
    • Igonet, S.1    Vulliez-Le Normand, B.2    Faure, G.3    Riottot, M.M.4    Kocken, C.H.5    Thomas, A.W.6    Bentley, G.A.7
  • 26
  • 27
    • 0036591274 scopus 로고    scopus 로고
    • Plasmodium falciparum: glycosylation status of Plasmodium falciparum circumsporozoite protein expressed in the baculovirus system
    • Kedees, M.H., Azzouz, N., Gerold, P., Shams-Eldin, H., Iqbal, J., Eckert, V. and Schwarz, R.T. (2002) Plasmodium falciparum: glycosylation status of Plasmodium falciparum circumsporozoite protein expressed in the baculovirus system. Exp. Parasitol. 101, 64-68.
    • (2002) Exp. Parasitol. , vol.101 , pp. 64-68
    • Kedees, M.H.1    Azzouz, N.2    Gerold, P.3    Shams-Eldin, H.4    Iqbal, J.5    Eckert, V.6    Schwarz, R.T.7
  • 28
    • 0036892213 scopus 로고    scopus 로고
    • In vitro studies with recombinant Plasmodium falciparum apical membrane antigen 1 (AMA1): production and activity of an AMA1 vaccine and generation of a multiallelic response
    • Kennedy, M.C., Wang, J., Zhang, Y., Miles, A.P., Chitsaz, F., Saul, A., Long, C.A., Miller, L.H. and Stowers, A.W. (2002) In vitro studies with recombinant Plasmodium falciparum apical membrane antigen 1 (AMA1): production and activity of an AMA1 vaccine and generation of a multiallelic response. Infect. Immun. 70, 6948-6960.
    • (2002) Infect. Immun. , vol.70 , pp. 6948-6960
    • Kennedy, M.C.1    Wang, J.2    Zhang, Y.3    Miles, A.P.4    Chitsaz, F.5    Saul, A.6    Long, C.A.7    Miller, L.H.8    Stowers, A.W.9
  • 30
    • 0036073678 scopus 로고    scopus 로고
    • High-level expression of the malaria blood-stage vaccine candidate Plasmodium falciparum apical membrane antigen 1 and induction of antibodies that inhibit erythrocyte invasion
    • Kocken, C.H., Withers-Martinez, C., Dubbeld, M.A., van der Wel, A., Hackett, F., Blackman, M.J. and Thomas, A.W. (2002) High-level expression of the malaria blood-stage vaccine candidate Plasmodium falciparum apical membrane antigen 1 and induction of antibodies that inhibit erythrocyte invasion. Infect. Immun. 70, 4471-4476.
    • (2002) Infect. Immun. , vol.70 , pp. 4471-4476
    • Kocken, C.H.1    Withers-Martinez, C.2    Dubbeld, M.A.3    van der Wel, A.4    Hackett, F.5    Blackman, M.J.6    Thomas, A.W.7
  • 31
    • 0001200134 scopus 로고
    • The promoter of Tl-DNA gene 5 controls the tissue-specific expression of chimeric genes carried by a novel type of agrobacterium binary vector
    • Koncz, C. and Schell, J. (1986) The promoter of Tl-DNA gene 5 controls the tissue-specific expression of chimeric genes carried by a novel type of agrobacterium binary vector. Mol. Genet. Genomics 204, 383-396.
    • (1986) Mol. Genet. Genomics , vol.204 , pp. 383-396
    • Koncz, C.1    Schell, J.2
  • 32
    • 0018704491 scopus 로고
    • Synchronization of Plasmodium falciparum erythrocytic stages in culture
    • Lambros, C. and Vanderberg, J.P. (1979) Synchronization of Plasmodium falciparum erythrocytic stages in culture. J. Parasitol. 65, 418-420.
    • (1979) J. Parasitol. , vol.65 , pp. 418-420
    • Lambros, C.1    Vanderberg, J.P.2
  • 33
    • 34248172560 scopus 로고    scopus 로고
    • Optimization of human papillomavirus type 16 (HPV-16) L1 expression in plants: comparison of the suitability of different HPV-16 L1 gene variants and different cell-compartment localization
    • Maclean, J., Koekemoer, M., Olivier, A.J., Stewart, D., Hitzeroth, I.I., Rademacher, T., Fischer, R., Williamson, A.L. and Rybicki, E.P. (2007) Optimization of human papillomavirus type 16 (HPV-16) L1 expression in plants: comparison of the suitability of different HPV-16 L1 gene variants and different cell-compartment localization. J. Gen. Virol. 88, 1460-1469.
    • (2007) J. Gen. Virol. , vol.88 , pp. 1460-1469
    • Maclean, J.1    Koekemoer, M.2    Olivier, A.J.3    Stewart, D.4    Hitzeroth, I.I.5    Rademacher, T.6    Fischer, R.7    Williamson, A.L.8    Rybicki, E.P.9
  • 34
    • 0031041235 scopus 로고    scopus 로고
    • The glycosylation of the influenza A virus hemagglutinin by mammalian cells. A site-specific study
    • Mir-Shekari, S.Y., Ashford, D.A., Harvey, D.J., Dwek, R.A. and Schulze, I.T. (1997) The glycosylation of the influenza A virus hemagglutinin by mammalian cells. A site-specific study. J. Biol. Chem. 272, 4027-4036.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4027-4036
    • Mir-Shekari, S.Y.1    Ashford, D.A.2    Harvey, D.J.3    Dwek, R.A.4    Schulze, I.T.5
  • 35
    • 67650370079 scopus 로고    scopus 로고
    • Anti-apical-membrane-antigen-1 antibody is more effective than anti-42-kilodalton-merozoite-surface-protein-1 antibody in inhibiting plasmodium falciparum growth, as determined by the in vitro growth inhibition assay
    • Miura, K., Zhou, H., Diouf, A., Moretz, S.E., Fay, M.P., Miller, L.H., Martin, L.B., Pierce, M.A., Ellis, R.D., Mullen, G.E. and Long, C.A. (2009) Anti-apical-membrane-antigen-1 antibody is more effective than anti-42-kilodalton-merozoite-surface-protein-1 antibody in inhibiting plasmodium falciparum growth, as determined by the in vitro growth inhibition assay. Clin. Vaccine Immunol. 16, 963-968.
    • (2009) Clin. Vaccine Immunol. , vol.16 , pp. 963-968
    • Miura, K.1    Zhou, H.2    Diouf, A.3    Moretz, S.E.4    Fay, M.P.5    Miller, L.H.6    Martin, L.B.7    Pierce, M.A.8    Ellis, R.D.9    Mullen, G.E.10    Long, C.A.11
  • 36
    • 0028145547 scopus 로고
    • Differential localization of full-length and processed forms of PF83/AMA-1 an apical membrane antigen of Plasmodium falciparum merozoites
    • Narum, D.L. and Thomas, A.W. (1994) Differential localization of full-length and processed forms of PF83/AMA-1 an apical membrane antigen of Plasmodium falciparum merozoites. Mol. Biochem. Parasitol. 67, 59-68.
    • (1994) Mol. Biochem. Parasitol. , vol.67 , pp. 59-68
    • Narum, D.L.1    Thomas, A.W.2
  • 37
    • 0034095455 scopus 로고    scopus 로고
    • Immunization with parasite-derived apical membrane antigen 1 or passive immunization with a specific monoclonal antibody protects BALB/c mice against lethal Plasmodium yoelii yoelii YM blood-stage infection
    • Narum, D.L., Ogun, S.A., Thomas, A.W. and Holder, A.A. (2000) Immunization with parasite-derived apical membrane antigen 1 or passive immunization with a specific monoclonal antibody protects BALB/c mice against lethal Plasmodium yoelii yoelii YM blood-stage infection. Infect. Immun. 68, 2899-2906.
    • (2000) Infect. Immun. , vol.68 , pp. 2899-2906
    • Narum, D.L.1    Ogun, S.A.2    Thomas, A.W.3    Holder, A.A.4
  • 38
    • 84867774199 scopus 로고    scopus 로고
    • Glycan profiles of the 27 N-glycosylation sites of the HIV envelope protein CN54gp140
    • Pabst, M., Chang, M., Stadlmann, J. and Altmann, F. (2012) Glycan profiles of the 27 N-glycosylation sites of the HIV envelope protein CN54gp140. Biol. Chem. 393, 719-730.
    • (2012) Biol. Chem. , vol.393 , pp. 719-730
    • Pabst, M.1    Chang, M.2    Stadlmann, J.3    Altmann, F.4
  • 39
    • 0038414622 scopus 로고    scopus 로고
    • Hyperglycosylated mutants of human immunodeficiency virus (HIV) type 1 monomeric gp120 as novel antigens for HIV vaccine design
    • Pantophlet, R., Wilson, I.A. and Burton, D.R. (2003) Hyperglycosylated mutants of human immunodeficiency virus (HIV) type 1 monomeric gp120 as novel antigens for HIV vaccine design. J. Virol. 77, 5889-5901.
    • (2003) J. Virol. , vol.77 , pp. 5889-5901
    • Pantophlet, R.1    Wilson, I.A.2    Burton, D.R.3
  • 40
    • 12444337649 scopus 로고    scopus 로고
    • Improved design of an antigen with enhanced specificity for the broadly HIV-neutralizing antibody b12
    • Pantophlet, R., Wilson, I.A. and Burton, D.R. (2004) Improved design of an antigen with enhanced specificity for the broadly HIV-neutralizing antibody b12. Protein Eng. Des. Sel. 17, 749-758.
    • (2004) Protein Eng. Des. Sel. , vol.17 , pp. 749-758
    • Pantophlet, R.1    Wilson, I.A.2    Burton, D.R.3
  • 41
    • 0023988955 scopus 로고
    • Evidence that luminal ER proteins are sorted from secreted proteins in a post-ER compartment
    • Pelham, H.R. (1988) Evidence that luminal ER proteins are sorted from secreted proteins in a post-ER compartment. EMBO J. 7, 913-918.
    • (1988) EMBO J. , vol.7 , pp. 913-918
    • Pelham, H.R.1
  • 43
    • 33846471713 scopus 로고    scopus 로고
    • Biosensor-based characterization of serum antibodies during development of an anti-IgE immunotherapeutic against allergy and asthma
    • Pol, E., Karlsson, R., Roos, H., Jansson, A., Xu, B., Larsson, A., Jarhede, T., Franklin, G., Fuentes, A. and Persson, S. (2007) Biosensor-based characterization of serum antibodies during development of an anti-IgE immunotherapeutic against allergy and asthma. J. Mol. Recognit. 20, 22-31.
    • (2007) J. Mol. Recognit. , vol.20 , pp. 22-31
    • Pol, E.1    Karlsson, R.2    Roos, H.3    Jansson, A.4    Xu, B.5    Larsson, A.6    Jarhede, T.7    Franklin, G.8    Fuentes, A.9    Persson, S.10
  • 44
    • 0034849136 scopus 로고    scopus 로고
    • Strong diversifying selection on domains of the Plasmodium falciparum apical membrane antigen 1 gene
    • Polley, S.D. and Conway, D.J. (2001) Strong diversifying selection on domains of the Plasmodium falciparum apical membrane antigen 1 gene. Genetics, 158, 1505-1512.
    • (2001) Genetics , vol.158 , pp. 1505-1512
    • Polley, S.D.1    Conway, D.J.2
  • 45
    • 2942672722 scopus 로고    scopus 로고
    • A multidomain adhesion protein family expressed in Plasmodium falciparum is essential for transmission to the mosquito
    • Pradel, G., Hayton, K., Aravind, L., Iyer, L.M., Abrahamsen, M.S., Bonawitz, A., Mejia, C. and Templeton, T.J. (2004) A multidomain adhesion protein family expressed in Plasmodium falciparum is essential for transmission to the mosquito. J. Exp. Med. 199, 1533-1544.
    • (2004) J. Exp. Med. , vol.199 , pp. 1533-1544
    • Pradel, G.1    Hayton, K.2    Aravind, L.3    Iyer, L.M.4    Abrahamsen, M.S.5    Bonawitz, A.6    Mejia, C.7    Templeton, T.J.8
  • 47
    • 38349117119 scopus 로고    scopus 로고
    • Apical membrane antigen 1: a malaria vaccine candidate in review
    • Remarque, E.J., Faber, B.W., Kocken, C.H. and Thomas, A.W. (2008a) Apical membrane antigen 1: a malaria vaccine candidate in review. Trends Parasitol. 24, 74-84.
    • (2008) Trends Parasitol. , vol.24 , pp. 74-84
    • Remarque, E.J.1    Faber, B.W.2    Kocken, C.H.3    Thomas, A.W.4
  • 48
    • 46249103583 scopus 로고    scopus 로고
    • A diversity-covering approach to immunization with Plasmodium falciparum apical membrane antigen 1 induces broader allelic recognition and growth inhibition responses in rabbits
    • Remarque, E.J., Faber, B.W., Kocken, C.H. and Thomas, A.W. (2008b) A diversity-covering approach to immunization with Plasmodium falciparum apical membrane antigen 1 induces broader allelic recognition and growth inhibition responses in rabbits. Infect. Immun. 76, 2660-2670.
    • (2008) Infect. Immun. , vol.76 , pp. 2660-2670
    • Remarque, E.J.1    Faber, B.W.2    Kocken, C.H.3    Thomas, A.W.4
  • 51
    • 77953987341 scopus 로고    scopus 로고
    • Plant-made vaccines for humans and animals
    • Rybicki, E.P. (2010) Plant-made vaccines for humans and animals. Plant Biotechnol. J. 8, 620-637.
    • (2010) Plant Biotechnol. J. , vol.8 , pp. 620-637
    • Rybicki, E.P.1
  • 53
    • 13444281918 scopus 로고    scopus 로고
    • The diversity of dolichol-linked precursors to Asn-linked glycans likely results from secondary loss of sets of glycosyltransferases
    • Samuelson, J., Banerjee, S., Magnelli, P., Cui, J., Kelleher, D.J., Gilmore, R. and Robbins, P.W. (2005) The diversity of dolichol-linked precursors to Asn-linked glycans likely results from secondary loss of sets of glycosyltransferases. Proc. Natl Acad. Sci. USA 102, 1548-1553.
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 1548-1553
    • Samuelson, J.1    Banerjee, S.2    Magnelli, P.3    Cui, J.4    Kelleher, D.J.5    Gilmore, R.6    Robbins, P.W.7
  • 54
    • 0030740376 scopus 로고    scopus 로고
    • Effects of glycosylation on the properties and functions of influenza virus hemagglutinin
    • Schulze, I.T. (1997) Effects of glycosylation on the properties and functions of influenza virus hemagglutinin. J. Infect. Dis. 176(Suppl 1), 24-28.
    • (1997) J. Infect. Dis. , vol.176 , pp. 24-28
    • Schulze, I.T.1
  • 55
    • 5644303930 scopus 로고    scopus 로고
    • Recombinant anti-hCG antibodies retained in the endoplasmic reticulum of transformed plants lack core-xylose and core-alpha (1,3)-fucose residues
    • Sriraman, R., Bardor, M., Sack, M., Vaquero, C., Faye, L., Fischer, R., Finnern, R. and Lerouge, P. (2004) Recombinant anti-hCG antibodies retained in the endoplasmic reticulum of transformed plants lack core-xylose and core-alpha (1, 3)-fucose residues. Plant Biotechnol. J. 2, 279-287.
    • (2004) Plant Biotechnol. J. , vol.2 , pp. 279-287
    • Sriraman, R.1    Bardor, M.2    Sack, M.3    Vaquero, C.4    Faye, L.5    Fischer, R.6    Finnern, R.7    Lerouge, P.8
  • 57
    • 0017311840 scopus 로고
    • Human malaria parasites in continuous culture
    • Trager, W. and Jensen, J.B. (1976) Human malaria parasites in continuous culture. Science, 193, 673-675.
    • (1976) Science , vol.193 , pp. 673-675
    • Trager, W.1    Jensen, J.B.2
  • 58
    • 33646842291 scopus 로고    scopus 로고
    • Plant-derived mouse IgG monoclonal antibody fused to KDEL endoplasmic reticulum-retention signal is N-glycosylated homogeneously throughout the plant with mostly high-mannose-type N-glycans
    • Triguero, A., Cabrera, G., Cremata, J.A., Yuen, C.T., Wheeler, J. and Ramírez, N.I. (2005) Plant-derived mouse IgG monoclonal antibody fused to KDEL endoplasmic reticulum-retention signal is N-glycosylated homogeneously throughout the plant with mostly high-mannose-type N-glycans. Plant Biotechnol. J. 3, 449-457.
    • (2005) Plant Biotechnol. J. , vol.3 , pp. 449-457
    • Triguero, A.1    Cabrera, G.2    Cremata, J.A.3    Yuen, C.T.4    Wheeler, J.5    Ramírez, N.I.6
  • 59
    • 0029108560 scopus 로고
    • Reduced virus infectivity in nicotiana tabacum secreting a TMV-specific full-size antibody
    • Voss, A., Niersbach, M., Hain, R., Hirsch, H.J., Liao, Y.C., Kreuzaler, F. and Fischer, R. (1995) Reduced virus infectivity in nicotiana tabacum secreting a TMV-specific full-size antibody. Mol. Breed. 1, 39-50.
    • (1995) Mol. Breed. , vol.1 , pp. 39-50
    • Voss, A.1    Niersbach, M.2    Hain, R.3    Hirsch, H.J.4    Liao, Y.C.5    Kreuzaler, F.6    Fischer, R.7
  • 61
    • 84874426182 scopus 로고    scopus 로고
    • Plant-derived vaccines: an approach for affordable vaccines against cervical cancer
    • Waheed, M.T., Gottschamel, J., Hassan, S.W. and Lössl, A.G. (2012) Plant-derived vaccines: an approach for affordable vaccines against cervical cancer. Hum. Vaccin. Immunother. 8, 403-406.
    • (2012) Hum. Vaccin. Immunother. , vol.8 , pp. 403-406
    • Waheed, M.T.1    Gottschamel, J.2    Hassan, S.W.3    Lössl, A.G.4
  • 63
    • 84922724570 scopus 로고    scopus 로고
    • Ld Malaria Report 2012 World Health Organization.
    • World Health Organization (2012). Ld Malaria Report 2012 World Health Organization.
    • (2012)
  • 64
    • 79953697416 scopus 로고    scopus 로고
    • Clinical development of plant-produced recombinant pharmaceuticals: vaccines, antibodies and beyond
    • Yusibov, V., Streatfield, S.J. and Kushnir, N. (2011) Clinical development of plant-produced recombinant pharmaceuticals: vaccines, antibodies and beyond. Hum. Vaccin. 7, 313-321.
    • (2011) Hum. Vaccin. , vol.7 , pp. 313-321
    • Yusibov, V.1    Streatfield, S.J.2    Kushnir, N.3


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