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Volumn 16, Issue 9, 2018, Pages 1531-1545

Production of complex viral glycoproteins in plants as vaccine immunogens

Author keywords

biopharming; chaperone; glycoprotein; vaccine

Indexed keywords


EID: 85050455412     PISSN: 14677644     EISSN: 14677652     Source Type: Journal    
DOI: 10.1111/pbi.12963     Document Type: Review
Times cited : (60)

References (181)
  • 1
    • 84947445736 scopus 로고    scopus 로고
    • Identification of common features in prototype broadly neutralizing antibodies to HIV envelope V2 apex to facilitate vaccine design
    • Andrabi, R., Voss, J.E., Liang, C.H., Briney, B., McCoy, L.E., Wu, C.Y., Wong, C.H. et al. (2015) Identification of common features in prototype broadly neutralizing antibodies to HIV envelope V2 apex to facilitate vaccine design. Immunity, 43, 959–973.
    • (2015) Immunity , vol.43 , pp. 959-973
    • Andrabi, R.1    Voss, J.E.2    Liang, C.H.3    Briney, B.4    McCoy, L.E.5    Wu, C.Y.6    Wong, C.H.7
  • 2
    • 85029172601 scopus 로고    scopus 로고
    • Glycans function as anchors for antibodies and help drive HIV broadly neutralizing antibody development
    • e523.
    • Andrabi, R., Su, C.Y., Liang, C.H., Shivatare, S.S., Briney, B., Voss, J.E., Nawazi, S.K. et al. (2017) Glycans function as anchors for antibodies and help drive HIV broadly neutralizing antibody development. Immunity, 47, 524–537. e523.
    • (2017) Immunity , vol.47 , pp. 524-537
    • Andrabi, R.1    Su, C.Y.2    Liang, C.H.3    Shivatare, S.S.4    Briney, B.5    Voss, J.E.6    Nawazi, S.K.7
  • 3
    • 23444448769 scopus 로고    scopus 로고
    • High level expression of surface glycoprotein of rabies virus in tobacco leaves and its immunoprotective activity in mice
    • Ashraf, S., Singh, P.K., Yadav, D.K., Shahnawaz, M., Mishra, S., Sawant, S.V. and Tuli, R. (2005) High level expression of surface glycoprotein of rabies virus in tobacco leaves and its immunoprotective activity in mice. J. Biotechnol. 119, 1–14.
    • (2005) J. Biotechnol. , vol.119 , pp. 1-14
    • Ashraf, S.1    Singh, P.K.2    Yadav, D.K.3    Shahnawaz, M.4    Mishra, S.5    Sawant, S.V.6    Tuli, R.7
  • 4
    • 78049288264 scopus 로고    scopus 로고
    • Vaccine delivery: a matter of size, geometry, kinetics and molecular patterns
    • Bachmann, M.F. and Jennings, G.T. (2010) Vaccine delivery: a matter of size, geometry, kinetics and molecular patterns. Nat. Rev. Immunol. 10, 787–796.
    • (2010) Nat. Rev. Immunol. , vol.10 , pp. 787-796
    • Bachmann, M.F.1    Jennings, G.T.2
  • 5
    • 84880431984 scopus 로고    scopus 로고
    • The N276 glycosylation site is required for HIV-1 neutralization by the CD4 binding site specific HJ16 monoclonal antibody
    • Balla-Jhagjhoorsingh, S.S., Corti, D., Heyndrickx, L., Willems, E., Vereecken, K., Davis, D. and Vanham, G. (2013) The N276 glycosylation site is required for HIV-1 neutralization by the CD4 binding site specific HJ16 monoclonal antibody. PLoS ONE, 8, e68863.
    • (2013) PLoS ONE , vol.8
    • Balla-Jhagjhoorsingh, S.S.1    Corti, D.2    Heyndrickx, L.3    Willems, E.4    Vereecken, K.5    Davis, D.6    Vanham, G.7
  • 6
    • 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. et al. (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
  • 7
    • 0036891872 scopus 로고    scopus 로고
    • Identification of neutralizing epitopes within structural domain III of the West Nile virus envelope protein
    • Beasley, D.W. and Barrett, A.D. (2002) Identification of neutralizing epitopes within structural domain III of the West Nile virus envelope protein. J. Virol. 76, 13097–13100.
    • (2002) J. Virol. , vol.76 , pp. 13097-13100
    • Beasley, D.W.1    Barrett, A.D.2
  • 8
    • 27744449665 scopus 로고    scopus 로고
    • Mucosal and systemic immunization elicited by Newcastle disease virus (NDV) transgenic plants as antigens
    • Berinstein, A., Vazquez-Rovere, C., Asurmendi, S., Gomez, E., Zanetti, F., Zabal, O., Tozzini, A. et al. (2005) Mucosal and systemic immunization elicited by Newcastle disease virus (NDV) transgenic plants as antigens. Vaccine, 23, 5583–5589.
    • (2005) Vaccine , vol.23 , pp. 5583-5589
    • Berinstein, A.1    Vazquez-Rovere, C.2    Asurmendi, S.3    Gomez, E.4    Zanetti, F.5    Zabal, O.6    Tozzini, A.7
  • 9
    • 0033985999 scopus 로고    scopus 로고
    • A recombinant human immunodeficiency virus type 1 envelope glycoprotein complex stabilized by an intermolecular disulfide bond between the gp120 and gp41 subunits is an antigenic mimic of the trimeric virion-associated structure
    • Binley, J.M., Sanders, R.W., Clas, B., Schuelke, N., Master, A., Guo, Y., Kajumo, F. et al. (2000) A recombinant human immunodeficiency virus type 1 envelope glycoprotein complex stabilized by an intermolecular disulfide bond between the gp120 and gp41 subunits is an antigenic mimic of the trimeric virion-associated structure. J. Virol. 74, 627–643.
    • (2000) J. Virol. , vol.74 , pp. 627-643
    • Binley, J.M.1    Sanders, R.W.2    Clas, B.3    Schuelke, N.4    Master, A.5    Guo, Y.6    Kajumo, F.7
  • 10
    • 0036184790 scopus 로고    scopus 로고
    • Enhancing the proteolytic maturation of human immunodeficiency virus type 1 envelope glycoproteins
    • Binley, J.M., Sanders, R.W., Master, A., Cayanan, C.S., Wiley, C.L., Schiffner, L., Travis, B. et al. (2002) Enhancing the proteolytic maturation of human immunodeficiency virus type 1 envelope glycoproteins. J. Virol. 76, 2606–2616.
    • (2002) J. Virol. , vol.76 , pp. 2606-2616
    • Binley, J.M.1    Sanders, R.W.2    Master, A.3    Cayanan, C.S.4    Wiley, C.L.5    Schiffner, L.6    Travis, B.7
  • 11
    • 84900467984 scopus 로고    scopus 로고
    • Structural delineation of a quaternary, cleavage-dependent epitope at the gp41-gp120 interface on intact HIV-1 Env trimers
    • Blattner, C., Lee, J.H., Sliepen, K., Derking, R., Falkowska, E., de la Pena, A.T., Cupo, A. et al. (2014) Structural delineation of a quaternary, cleavage-dependent epitope at the gp41-gp120 interface on intact HIV-1 Env trimers. Immunity, 40, 669–680.
    • (2014) Immunity , vol.40 , pp. 669-680
    • Blattner, C.1    Lee, J.H.2    Sliepen, K.3    Derking, R.4    Falkowska, E.5    de la Pena, A.T.6    Cupo, A.7
  • 12
    • 77249136744 scopus 로고    scopus 로고
    • Rift Valley fever virus subunit vaccines confer complete protection against a lethal virus challenge
    • de Boer, S.M., Kortekaas, J., Antonis, A.F., Kant, J., van Oploo, J.L., Rottier, P.J., Moormann, R.J. et al. (2010) Rift Valley fever virus subunit vaccines confer complete protection against a lethal virus challenge. Vaccine, 28, 2330–2339.
    • (2010) Vaccine , vol.28 , pp. 2330-2339
    • de Boer, S.M.1    Kortekaas, J.2    Antonis, A.F.3    Kant, J.4    van Oploo, J.L.5    Rottier, P.J.6    Moormann, R.J.7
  • 13
    • 80051677678 scopus 로고    scopus 로고
    • The glycan shield of HIV is predominantly oligomannose independently of production system or viral clade
    • Bonomelli, C., Doores, K.J., Dunlop, D.C., Thaney, V., Dwek, R.A., Burton, D.R., Crispin, M. et al. (2011) The glycan shield of HIV is predominantly oligomannose independently of production system or viral clade. PLoS ONE, 6, e23521.
    • (2011) PLoS ONE , vol.6
    • Bonomelli, C.1    Doores, K.J.2    Dunlop, D.C.3    Thaney, V.4    Dwek, R.A.5    Burton, D.R.6    Crispin, M.7
  • 14
    • 77955262351 scopus 로고    scopus 로고
    • Plant glycans: friend or foe in vaccine development?
    • Bosch, D. and Schots, A. (2010) Plant glycans: friend or foe in vaccine development? Expert. Rev. Vaccines, 9, 835–842.
    • (2010) Expert. Rev. Vaccines , vol.9 , pp. 835-842
    • Bosch, D.1    Schots, A.2
  • 16
    • 0028023726 scopus 로고
    • Structure of influenza haemagglutinin at the pH of membrane fusion
    • Bullough, P.A., Hughson, F.M., Skehel, J.J. and Wiley, D.C. (1994) Structure of influenza haemagglutinin at the pH of membrane fusion. Nature, 371, 37–43.
    • (1994) Nature , vol.371 , pp. 37-43
    • Bullough, P.A.1    Hughson, F.M.2    Skehel, J.J.3    Wiley, D.C.4
  • 17
    • 85016232433 scopus 로고    scopus 로고
    • Global site-specific N-glycosylation analysis of HIV envelope glycoprotein
    • Cao, L., Diedrich, J.K., Kulp, D.W., Pauthner, M., He, L., Park, S.R., Sok, D. et al. (2017) Global site-specific N-glycosylation analysis of HIV envelope glycoprotein. Nat. Commun. 8, 14954.
    • (2017) Nat. Commun. , vol.8 , pp. 14954
    • Cao, L.1    Diedrich, J.K.2    Kulp, D.W.3    Pauthner, M.4    He, L.5    Park, S.R.6    Sok, D.7
  • 18
    • 85011277394 scopus 로고    scopus 로고
    • Plant expression systems, a budding way to confront chikungunya and Zika in developing countries?
    • Cardona-Ospina, J.A., Sepulveda-Arias, J.C., Mancilla, L. and Gutierrez-Lopez, L.G. (2016) Plant expression systems, a budding way to confront chikungunya and Zika in developing countries? F1000Res, 5, 2121.
    • (2016) F1000Res , vol.5 , pp. 2121
    • Cardona-Ospina, J.A.1    Sepulveda-Arias, J.C.2    Mancilla, L.3    Gutierrez-Lopez, L.G.4
  • 19
    • 84866037634 scopus 로고    scopus 로고
    • Glyco-engineering in plants to produce human-like N-glycan structures
    • Castilho, A. and Steinkellner, H. (2012) Glyco-engineering in plants to produce human-like N-glycan structures. Biotechnol. J. 7, 1088–1098.
    • (2012) Biotechnol. J. , vol.7 , pp. 1088-1098
    • Castilho, A.1    Steinkellner, H.2
  • 20
    • 77952408200 scopus 로고    scopus 로고
    • In planta protein sialylation through overexpression of the respective mammalian pathway
    • Castilho, A., Strasser, R., Stadlmann, J., Grass, J., Jez, J., Gattinger, P., Kunert, R. et al. (2010) In planta protein sialylation through overexpression of the respective mammalian pathway. J. Biol. Chem. 285, 15923–15930.
    • (2010) J. Biol. Chem. , vol.285 , pp. 15923-15930
    • Castilho, A.1    Strasser, R.2    Stadlmann, J.3    Grass, J.4    Jez, J.5    Gattinger, P.6    Kunert, R.7
  • 22
    • 85044419692 scopus 로고    scopus 로고
    • An oligosacchyaryl transferase from Leishmania major increases the N-glycan occupancy on recombinant glycoproteins produced in Nicotiana benthamiana
    • In press.
    • Castilho, A., Beihammer, G., Pfeiffer, C., Goritzer, K., Montero-Morales, L., Vavra, U., Moresch, D. et al. (2018) An oligosacchyaryl transferase from Leishmania major increases the N-glycan occupancy on recombinant glycoproteins produced in Nicotiana benthamiana. Plant Biotechnol. J. https://doi.org/10.1111/pbi.12906, In press.
    • (2018) Plant Biotechnol. J.
    • Castilho, A.1    Beihammer, G.2    Pfeiffer, C.3    Goritzer, K.4    Montero-Morales, L.5    Vavra, U.6    Moresch, D.7
  • 23
    • 34250792678 scopus 로고    scopus 로고
    • Influenza virus hemagglutinin and neuraminidase, but not the matrix protein, are required for assembly and budding of plasmid-derived virus-like particles
    • Chen, B.J., Leser, G.P., Morita, E. and Lamb, R.A. (2007) Influenza virus hemagglutinin and neuraminidase, but not the matrix protein, are required for assembly and budding of plasmid-derived virus-like particles. J. Virol. 81, 7111–7123.
    • (2007) J. Virol. , vol.81 , pp. 7111-7123
    • Chen, B.J.1    Leser, G.P.2    Morita, E.3    Lamb, R.A.4
  • 24
    • 85019716803 scopus 로고    scopus 로고
    • Production of Japanese encephalitis virus antigens in plants using bamboo mosaic virus-based vector
    • Chen, T.-H., Hu, C.-C., Liao, J.-T., Lee, Y.-L., Huang, Y.-W., Lin, N.-S., Lin, Y.-L. et al. (2017) Production of Japanese encephalitis virus antigens in plants using bamboo mosaic virus-based vector. Front. Microbiol. 8, 788.
    • (2017) Front. Microbiol. , vol.8 , pp. 788
    • Chen, T.-H.1    Hu, C.-C.2    Liao, J.-T.3    Lee, Y.-L.4    Huang, Y.-W.5    Lin, N.-S.6    Lin, Y.-L.7
  • 25
    • 84870622077 scopus 로고    scopus 로고
    • Safety and immunogenicity of a plant-produced recombinant hemagglutinin-based influenza vaccine (HAI-05) derived from A/Indonesia/05/2005 (H5N1) influenza virus: a phase 1 randomized, double-blind, placebo-controlled, dose-escalation study in healthy adults
    • Chichester, J.A., Jones, R.M., Green, B.J., Stow, M., Miao, F., Moonsammy, G., Streatfield, S.J. et al. (2012) Safety and immunogenicity of a plant-produced recombinant hemagglutinin-based influenza vaccine (HAI-05) derived from A/Indonesia/05/2005 (H5N1) influenza virus: a phase 1 randomized, double-blind, placebo-controlled, dose-escalation study in healthy adults. Viruses, 4, 3227–3244.
    • (2012) Viruses , vol.4 , pp. 3227-3244
    • Chichester, J.A.1    Jones, R.M.2    Green, B.J.3    Stow, M.4    Miao, F.5    Moonsammy, G.6    Streatfield, S.J.7
  • 26
    • 0034899311 scopus 로고    scopus 로고
    • Monoclonal antibodies that bind to domain III of dengue virus E glycoprotein are the most efficient blockers of virus adsorption to Vero cells
    • Crill, W.D. and Roehrig, J.T. (2001) Monoclonal antibodies that bind to domain III of dengue virus E glycoprotein are the most efficient blockers of virus adsorption to Vero cells. J. Virol. 75, 7769–7773.
    • (2001) J. Virol. , vol.75 , pp. 7769-7773
    • Crill, W.D.1    Roehrig, J.T.2
  • 27
    • 85047543847 scopus 로고    scopus 로고
    • Structure and immune recognition of the HIV Glycan shield
    • Crispin, M., Ward, A.B. and Wilson, I.A. (2018) Structure and immune recognition of the HIV Glycan shield. Annu. Rev. Biophys. 47, 499–523.
    • (2018) Annu. Rev. Biophys. , vol.47 , pp. 499-523
    • Crispin, M.1    Ward, A.B.2    Wilson, I.A.3
  • 28
    • 79958086672 scopus 로고    scopus 로고
    • Enzyme digests eliminate nonfunctional Env from HIV-1 particle surfaces, leaving native Env trimers intact and viral infectivity unaffected
    • Crooks, E.T., Tong, T., Osawa, K. and Binley, J.M. (2011) Enzyme digests eliminate nonfunctional Env from HIV-1 particle surfaces, leaving native Env trimers intact and viral infectivity unaffected. J. Virol. 85, 5825–5839.
    • (2011) J. Virol. , vol.85 , pp. 5825-5839
    • Crooks, E.T.1    Tong, T.2    Osawa, K.3    Binley, J.M.4
  • 29
    • 84897110525 scopus 로고    scopus 로고
    • Safety and immunogenicity of a plant-produced recombinant monomer hemagglutinin-based influenza vaccine derived from influenza A (H1N1)pdm09 virus: a Phase 1 dose-escalation study in healthy adults
    • Cummings, J.F., Guerrero, M.L., Moon, J.E., Waterman, P., Nielsen, R.K., Jefferson, S., Gross, F.L. et al. (2014) Safety and immunogenicity of a plant-produced recombinant monomer hemagglutinin-based influenza vaccine derived from influenza A (H1N1)pdm09 virus: a Phase 1 dose-escalation study in healthy adults. Vaccine, 32, 2251–2259.
    • (2014) Vaccine , vol.32 , pp. 2251-2259
    • Cummings, J.F.1    Guerrero, M.L.2    Moon, J.E.3    Waterman, P.4    Nielsen, R.K.5    Jefferson, S.6    Gross, F.L.7
  • 30
    • 0037245727 scopus 로고    scopus 로고
    • N-linked glycans direct the cotranslational folding pathway of influenza hemagglutinin
    • Daniels, R., Kurowski, B., Johnson, A.E. and Hebert, D.N. (2003) N-linked glycans direct the cotranslational folding pathway of influenza hemagglutinin. Mol. Cell. 11, 79–90.
    • (2003) Mol. Cell. , vol.11 , pp. 79-90
    • Daniels, R.1    Kurowski, B.2    Johnson, A.E.3    Hebert, D.N.4
  • 31
    • 55949124182 scopus 로고    scopus 로고
    • Influenza virus-like particles produced by transient expression in Nicotiana benthamiana induce a protective immune response against a lethal viral challenge in mice
    • D'Aoust, M.A., Lavoie, P.O., Couture, M.M., Trepanier, S., Guay, J.M., Dargis, M., Mongrand, S. et al. (2008) Influenza virus-like particles produced by transient expression in Nicotiana benthamiana induce a protective immune response against a lethal viral challenge in mice. Plant Biotechnol. J. 6, 930–940.
    • (2008) Plant Biotechnol. J. , vol.6 , pp. 930-940
    • D'Aoust, M.A.1    Lavoie, P.O.2    Couture, M.M.3    Trepanier, S.4    Guay, J.M.5    Dargis, M.6    Mongrand, S.7
  • 32
    • 77953964469 scopus 로고    scopus 로고
    • The production of hemagglutinin-based virus-like particles in plants: a rapid, efficient and safe response to pandemic influenza
    • D'Aoust, M.A., Couture, M.M., Charland, N., Trepanier, S., Landry, N., Ors, F. and Vezina, L.P. (2010) The production of hemagglutinin-based virus-like particles in plants: a rapid, efficient and safe response to pandemic influenza. Plant Biotechnol. J. 8, 607–619.
    • (2010) Plant Biotechnol. J. , vol.8 , pp. 607-619
    • D'Aoust, M.A.1    Couture, M.M.2    Charland, N.3    Trepanier, S.4    Landry, N.5    Ors, F.6    Vezina, L.P.7
  • 33
    • 0028362008 scopus 로고
    • The convertases furin and PC1 can both cleave the human immunodeficiency virus (HIV)-1 envelope glycoprotein gp160 into gp120 (HIV-1 SU) and gp41 (HIV-I TM)
    • Decroly, E., Vandenbranden, M., Ruysschaert, J.M., Cogniaux, J., Jacob, G.S., Howard, S.C., Marshall, G. et al. (1994) The convertases furin and PC1 can both cleave the human immunodeficiency virus (HIV)-1 envelope glycoprotein gp160 into gp120 (HIV-1 SU) and gp41 (HIV-I TM). J. Biol. Chem. 269, 12240–12247.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12240-12247
    • Decroly, E.1    Vandenbranden, M.2    Ruysschaert, J.M.3    Cogniaux, J.4    Jacob, G.S.5    Howard, S.C.6    Marshall, G.7
  • 34
    • 0029836967 scopus 로고    scopus 로고
    • Identification of the paired basic convertases implicated in HIV gp160 processing based on in vitro assays and expression in CD4(+) cell lines
    • Decroly, E., Wouters, S., Di Bello, C., Lazure, C., Ruysschaert, J.M. and Seidah, N.G. (1996) Identification of the paired basic convertases implicated in HIV gp160 processing based on in vitro assays and expression in CD4(+) cell lines. J. Biol. Chem. 271, 30442–30450.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30442-30450
    • Decroly, E.1    Wouters, S.2    Di Bello, C.3    Lazure, C.4    Ruysschaert, J.M.5    Seidah, N.G.6
  • 38
    • 84900517557 scopus 로고    scopus 로고
    • Broadly neutralizing HIV antibodies define a glycan-dependent epitope on the prefusion conformation of gp41 on cleaved envelope trimers
    • Falkowska, E., Le, K.M., Ramos, A., Doores, K.J., Lee, J.H., Blattner, C., Ramirez, A. et al. (2014) Broadly neutralizing HIV antibodies define a glycan-dependent epitope on the prefusion conformation of gp41 on cleaved envelope trimers. Immunity, 40, 657–668.
    • (2014) Immunity , vol.40 , pp. 657-668
    • Falkowska, E.1    Le, K.M.2    Ramos, A.3    Doores, K.J.4    Lee, J.H.5    Blattner, C.6    Ramirez, A.7
  • 39
    • 14744298421 scopus 로고    scopus 로고
    • Protein modifications in the plant secretory pathway: current status and practical implications in molecular pharming
    • Faye, L., Boulaflous, A., Benchabane, M., Gomord, V. and Michaud, D. (2005) Protein modifications in the plant secretory pathway: current status and practical implications in molecular pharming. Vaccine, 23, 1770–1778.
    • (2005) Vaccine , vol.23 , pp. 1770-1778
    • Faye, L.1    Boulaflous, A.2    Benchabane, M.3    Gomord, V.4    Michaud, D.5
  • 40
    • 0033564752 scopus 로고    scopus 로고
    • Expression and characterization of bispecific single-chain Fv fragments produced in transgenic plants
    • Fischer, R., Schumann, D., Zimmermann, S., Drossard, J., Sack, M. and Schillberg, S. (1999) Expression and characterization of bispecific single-chain Fv fragments produced in transgenic plants. Eur. J. Biochem. 262, 810–816.
    • (1999) Eur. J. Biochem. , vol.262 , pp. 810-816
    • Fischer, R.1    Schumann, D.2    Zimmermann, S.3    Drossard, J.4    Sack, M.5    Schillberg, S.6
  • 42
    • 84874761652 scopus 로고    scopus 로고
    • Influenza HA subtypes demonstrate divergent phenotypes for cleavage activation and pH of fusion: implications for host range and adaptation
    • Galloway, S.E., Reed, M.L., Russell, C.J. and Steinhauer, D.A. (2013) Influenza HA subtypes demonstrate divergent phenotypes for cleavage activation and pH of fusion: implications for host range and adaptation. PLoS Pathog. 9, e1003151.
    • (2013) PLoS Pathog. , vol.9
    • Galloway, S.E.1    Reed, M.L.2    Russell, C.J.3    Steinhauer, D.A.4
  • 43
    • 84928523302 scopus 로고    scopus 로고
    • Single-chain soluble BG505.SOSIP gp140 trimers as structural and antigenic mimics of mature closed HIV-1 Env
    • Georgiev, I.S., Joyce, M.G., Yang, Y., Sastry, M., Zhang, B., Baxa, U., Chen, R.E. et al. (2015) Single-chain soluble BG505.SOSIP gp140 trimers as structural and antigenic mimics of mature closed HIV-1 Env. J. Virol. 89, 5318–5329.
    • (2015) J. Virol. , vol.89 , pp. 5318-5329
    • Georgiev, I.S.1    Joyce, M.G.2    Yang, Y.3    Sastry, M.4    Zhang, B.5    Baxa, U.6    Chen, R.E.7
  • 44
    • 83455259591 scopus 로고    scopus 로고
    • Mice orally immunized with a transgenic plant expressing the glycoprotein of Crimean-Congo hemorrhagic fever virus
    • Ghiasi, S.M., Salmanian, A.H., Chinikar, S. and Zakeri, S. (2011) Mice orally immunized with a transgenic plant expressing the glycoprotein of Crimean-Congo hemorrhagic fever virus. Clin. Vaccine Immunol. 18, 2031–2037.
    • (2011) Clin. Vaccine Immunol. , vol.18 , pp. 2031-2037
    • Ghiasi, S.M.1    Salmanian, A.H.2    Chinikar, S.3    Zakeri, S.4
  • 45
    • 84914109422 scopus 로고    scopus 로고
    • Glycosylation and disulfide bond analysis of transiently and stably expressed clade C HIV-1 gp140 trimers in 293T cells identifies disulfide heterogeneity present in both proteins and differences in O-linked glycosylation
    • Go, E.P., Hua, D. and Desaire, H. (2014) Glycosylation and disulfide bond analysis of transiently and stably expressed clade C HIV-1 gp140 trimers in 293T cells identifies disulfide heterogeneity present in both proteins and differences in O-linked glycosylation. J. Proteome Res. 13, 4012–4027.
    • (2014) J. Proteome Res. , vol.13 , pp. 4012-4027
    • Go, E.P.1    Hua, D.2    Desaire, H.3
  • 46
    • 70450248470 scopus 로고    scopus 로고
    • Expression of Hemagglutinin-Neuraminidase glycoprotein of Newcastle Disease Virus in agroinfiltrated Nicotiana benthamiana plants
    • Gomez, E., Zoth, S.C., Asurmendi, S., Rovere, C.V. and Berinstein, A. (2009) Expression of Hemagglutinin-Neuraminidase glycoprotein of Newcastle Disease Virus in agroinfiltrated Nicotiana benthamiana plants. J. Biotechnol. 144, 337–340.
    • (2009) J. Biotechnol. , vol.144 , pp. 337-340
    • Gomez, E.1    Zoth, S.C.2    Asurmendi, S.3    Rovere, C.V.4    Berinstein, A.5
  • 47
    • 84954381077 scopus 로고    scopus 로고
    • Structures of HIV-1 Env V1V2 with broadly neutralizing antibodies reveal commonalities that enable vaccine design
    • Gorman, J., Soto, C., Yang, M.M., Davenport, T.M., Guttman, M., Bailer, R.T., Chambers, M. et al. (2016) Structures of HIV-1 Env V1V2 with broadly neutralizing antibodies reveal commonalities that enable vaccine design. Nat. Struct. Mol. Biol. 23, 81–90.
    • (2016) Nat. Struct. Mol. Biol. , vol.23 , pp. 81-90
    • Gorman, J.1    Soto, C.2    Yang, M.M.3    Davenport, T.M.4    Guttman, M.5    Bailer, R.T.6    Chambers, M.7
  • 48
    • 83055194481 scopus 로고    scopus 로고
    • A protease activity-depleted environment for heterologous proteins migrating towards the leaf cell apoplast
    • Goulet, C., Khalf, M., Sainsbury, F., D'Aoust, M.A. and Michaud, D. (2012) A protease activity-depleted environment for heterologous proteins migrating towards the leaf cell apoplast. Plant Biotechnol. J. 10, 83–94.
    • (2012) Plant Biotechnol. J. , vol.10 , pp. 83-94
    • Goulet, C.1    Khalf, M.2    Sainsbury, F.3    D'Aoust, M.A.4    Michaud, D.5
  • 49
    • 0029062244 scopus 로고
    • Furin is important but not essential for the proteolytic maturation of gp160 of HIV-1
    • Gu, M., Rappaport, J. and Leppla, S.H. (1995) Furin is important but not essential for the proteolytic maturation of gp160 of HIV-1. FEBS Lett. 365, 95–97.
    • (1995) FEBS Lett. , vol.365 , pp. 95-97
    • Gu, M.1    Rappaport, J.2    Leppla, S.H.3
  • 52
    • 0026716831 scopus 로고
    • Inhibition of furin-mediated cleavage activation of HIV-1 glycoprotein gp160
    • Hallenberger, S., Bosch, V., Angliker, H., Shaw, E., Klenk, H.D. and Garten, W. (1992) Inhibition of furin-mediated cleavage activation of HIV-1 glycoprotein gp160. Nature, 360, 358–361.
    • (1992) Nature , vol.360 , pp. 358-361
    • Hallenberger, S.1    Bosch, V.2    Angliker, H.3    Shaw, E.4    Klenk, H.D.5    Garten, W.6
  • 53
    • 84899504050 scopus 로고    scopus 로고
    • A plant-produced antigen elicits potent immune responses against West Nile virus in mice
    • He, J., Peng, L., Lai, H., Hurtado, J., Stahnke, J. and Chen, Q. (2014) A plant-produced antigen elicits potent immune responses against West Nile virus in mice. Biomed. Res. Int. 2014, 952865.
    • (2014) Biomed. Res. Int. , vol.2014 , pp. 952865
    • He, J.1    Peng, L.2    Lai, H.3    Hurtado, J.4    Stahnke, J.5    Chen, Q.6
  • 54
    • 84884989291 scopus 로고    scopus 로고
    • Plant-derived pharmaceuticals for the developing world
    • Hefferon, K. (2013) Plant-derived pharmaceuticals for the developing world. Biotechnol. J. 8, 1193–1202.
    • (2013) Biotechnol. J. , vol.8 , pp. 1193-1202
    • Hefferon, K.1
  • 55
    • 33748937555 scopus 로고    scopus 로고
    • The surprising complexity of signal sequences
    • Hegde, R.S. and Bernstein, H.D. (2006) The surprising complexity of signal sequences. Trends Biochem. Sci. 31, 563–571.
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 563-571
    • Hegde, R.S.1    Bernstein, H.D.2
  • 56
    • 84943411448 scopus 로고    scopus 로고
    • Addition of N-glycosylation sites on the globular head of the H5 hemagglutinin induces the escape of highly pathogenic avian influenza A H5N1 viruses from vaccine-induced immunity
    • Herve, P.L., Lorin, V., Jouvion, G., Da Costa, B. and Escriou, N. (2015) Addition of N-glycosylation sites on the globular head of the H5 hemagglutinin induces the escape of highly pathogenic avian influenza A H5N1 viruses from vaccine-induced immunity. Virology, 486, 134–145.
    • (2015) Virology , vol.486 , pp. 134-145
    • Herve, P.L.1    Lorin, V.2    Jouvion, G.3    Da Costa, B.4    Escriou, N.5
  • 57
    • 0029838640 scopus 로고    scopus 로고
    • ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway
    • Hiller, M.M., Finger, A., Schweiger, M. and Wolf, D.H. (1996) ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway. Science, 273, 1725–1728.
    • (1996) Science , vol.273 , pp. 1725-1728
    • Hiller, M.M.1    Finger, A.2    Schweiger, M.3    Wolf, D.H.4
  • 59
    • 84877341291 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress responses in plants
    • Howell, S.H. (2013) Endoplasmic reticulum stress responses in plants. Annu. Rev. Plant Biol. 64, 477–499.
    • (2013) Annu. Rev. Plant Biol. , vol.64 , pp. 477-499
    • Howell, S.H.1
  • 60
    • 0031055289 scopus 로고    scopus 로고
    • Coexpression of molecular chaperone BiP improves immunoglobulin solubility and IgG secretion from Trichoplusia ni insect cells
    • Hsu, T.A. and Betenbaugh, M.J. (1997) Coexpression of molecular chaperone BiP improves immunoglobulin solubility and IgG secretion from Trichoplusia ni insect cells. Biotechnol. Prog. 13, 96–104.
    • (1997) Biotechnol. Prog. , vol.13 , pp. 96-104
    • Hsu, T.A.1    Betenbaugh, M.J.2
  • 61
    • 85039048596 scopus 로고    scopus 로고
    • Estimates of global seasonal influenza-associated respiratory mortality: a modelling study
    • Iuliano, A.D., Roguski, K.M., Chang, H.H., Muscatello, D.J., Palekar, R., Tempia, S., Cohen, C. et al. (2017) Estimates of global seasonal influenza-associated respiratory mortality: a modelling study. Lancet, 391, 1285–1300.
    • (2017) Lancet , vol.391 , pp. 1285-1300
    • Iuliano, A.D.1    Roguski, K.M.2    Chang, H.H.3    Muscatello, D.J.4    Palekar, R.5    Tempia, S.6    Cohen, C.7
  • 62
    • 84877609579 scopus 로고    scopus 로고
    • Rational HIV immunogen design to target specific germline B cell receptors
    • Jardine, J., Julien, J.P., Menis, S., Ota, T., Kalyuzhniy, O., McGuire, A., Sok, D. et al. (2013) Rational HIV immunogen design to target specific germline B cell receptors. Science, 340, 711–716.
    • (2013) Science , vol.340 , pp. 711-716
    • Jardine, J.1    Julien, J.P.2    Menis, S.3    Ota, T.4    Kalyuzhniy, O.5    McGuire, A.6    Sok, D.7
  • 63
    • 0028858161 scopus 로고
    • Multiple proteolytic systems, including the proteasome, contribute to CFTR processing
    • Jensen, T.J., Loo, M.A., Pind, S., Williams, D.B., Goldberg, A.L. and Riordan, J.R. (1995) Multiple proteolytic systems, including the proteasome, contribute to CFTR processing. Cell, 83, 129–135.
    • (1995) Cell , vol.83 , pp. 129-135
    • Jensen, T.J.1    Loo, M.A.2    Pind, S.3    Williams, D.B.4    Goldberg, A.L.5    Riordan, J.R.6
  • 64
    • 40549118514 scopus 로고    scopus 로고
    • A plant-derived human monoclonal antibody induces an anticarbohydrate immune response in rabbits
    • Jin, C., Altmann, F., Strasser, R., Mach, L., Schahs, M., Kunert, R., Rademacher, T. et al. (2008) A plant-derived human monoclonal antibody induces an anticarbohydrate immune response in rabbits. Glycobiology, 18, 235–241.
    • (2008) Glycobiology , vol.18 , pp. 235-241
    • Jin, C.1    Altmann, F.2    Strasser, R.3    Mach, L.4    Schahs, M.5    Kunert, R.6    Rademacher, T.7
  • 65
    • 84874270957 scopus 로고    scopus 로고
    • Addition of glycosylation to influenza A virus hemagglutinin modulates antibody-mediated recognition of H1N1 2009 pandemic viruses
    • Job, E.R., Deng, Y.M., Barfod, K.K., Tate, M.D., Caldwell, N., Reddiex, S., Maurer-Stroh, S. et al. (2013) Addition of glycosylation to influenza A virus hemagglutinin modulates antibody-mediated recognition of H1N1 2009 pandemic viruses. J. Immunol. 190, 2169–2177.
    • (2013) J. Immunol. , vol.190 , pp. 2169-2177
    • Job, E.R.1    Deng, Y.M.2    Barfod, K.K.3    Tate, M.D.4    Caldwell, N.5    Reddiex, S.6    Maurer-Stroh, S.7
  • 66
  • 68
    • 84940583123 scopus 로고    scopus 로고
    • Modulating secretory pathway pH by proton channel co-expression can increase recombinant protein stability in plants
    • Jutras, P.V., D'Aoust, M.A., Couture, M.M., Vezina, L.P., Goulet, M.C., Michaud, D. and Sainsbury, F. (2015) Modulating secretory pathway pH by proton channel co-expression can increase recombinant protein stability in plants. Biotechnol. J. 10, 1478–1486.
    • (2015) Biotechnol. J. , vol.10 , pp. 1478-1486
    • Jutras, P.V.1    D'Aoust, M.A.2    Couture, M.M.3    Vezina, L.P.4    Goulet, M.C.5    Michaud, D.6    Sainsbury, F.7
  • 69
    • 85035340780 scopus 로고    scopus 로고
    • Are we prepared for emerging flaviviruses in Europe? Challenges for vaccination
    • Kaaijk, P. and Luytjes, W. (2017) Are we prepared for emerging flaviviruses in Europe? Challenges for vaccination. Hum. Vaccin. Immunother. 14, 337–344.
    • (2017) Hum. Vaccin. Immunother. , vol.14 , pp. 337-344
    • Kaaijk, P.1    Luytjes, W.2
  • 70
    • 84978634507 scopus 로고    scopus 로고
    • Arabidopsis thaliana plants expressing Rift Valley fever virus antigens: mice exhibit systemic immune responses as the result of oral administration of the transgenic plants
    • Kalbina, I., Lagerqvist, N., Moiane, B., Ahlm, C., Andersson, S., Strid, A. and Falk, K.I. (2016) Arabidopsis thaliana plants expressing Rift Valley fever virus antigens: mice exhibit systemic immune responses as the result of oral administration of the transgenic plants. Protein Expr. Purif. 127, 61–67.
    • (2016) Protein Expr. Purif. , vol.127 , pp. 61-67
    • Kalbina, I.1    Lagerqvist, N.2    Moiane, B.3    Ahlm, C.4    Andersson, S.5    Strid, A.6    Falk, K.I.7
  • 71
    • 84954167372 scopus 로고    scopus 로고
    • Glycosylation of plant produced human antibodies
    • Kallolimath, S. and Steinkellner, H. (2015) Glycosylation of plant produced human antibodies. Hum. Antibodies, 23, 45–48.
    • (2015) Hum. Antibodies , vol.23 , pp. 45-48
    • Kallolimath, S.1    Steinkellner, H.2
  • 73
    • 79957851156 scopus 로고    scopus 로고
    • Expression of dengue-3 premembrane and envelope polyprotein in lettuce chloroplasts
    • Kanagaraj, A.P., Verma, D. and Daniell, H. (2011) Expression of dengue-3 premembrane and envelope polyprotein in lettuce chloroplasts. Plant Mol. Biol. 76, 323–333.
    • (2011) Plant Mol. Biol. , vol.76 , pp. 323-333
    • Kanagaraj, A.P.1    Verma, D.2    Daniell, H.3
  • 76
    • 84881024740 scopus 로고    scopus 로고
    • Biological and biochemical characterization of HIV-1 Gag/dgp41 virus-like particles expressed in Nicotiana benthamiana
    • Kessans, S.A., Linhart, M.D., Matoba, N. and Mor, T. (2013) Biological and biochemical characterization of HIV-1 Gag/dgp41 virus-like particles expressed in Nicotiana benthamiana. Plant Biotechnol. J. 11, 681–690.
    • (2013) Plant Biotechnol. J. , vol.11 , pp. 681-690
    • Kessans, S.A.1    Linhart, M.D.2    Matoba, N.3    Mor, T.4
  • 77
    • 77957753828 scopus 로고    scopus 로고
    • Cholera toxin B subunit-domain III of dengue virus envelope glycoprotein E fusion protein production in transgenic plants
    • Kim, T.G., Kim, M.Y. and Yang, M.S. (2010) Cholera toxin B subunit-domain III of dengue virus envelope glycoprotein E fusion protein production in transgenic plants. Protein Expr. Purif. 74, 236–241.
    • (2010) Protein Expr. Purif. , vol.74 , pp. 236-241
    • Kim, T.G.1    Kim, M.Y.2    Yang, M.S.3
  • 78
    • 84862787104 scopus 로고    scopus 로고
    • Expression of a consensus dengue virus envelope protein domain III in transgenic callus of rice
    • Kim, M.Y., Yang, M.S. and Kim, T.G. (2012) Expression of a consensus dengue virus envelope protein domain III in transgenic callus of rice. Plant Cell. Tiss. Org. 109, 509–515.
    • (2012) Plant Cell. Tiss. Org. , vol.109 , pp. 509-515
    • Kim, M.Y.1    Yang, M.S.2    Kim, T.G.3
  • 79
    • 77957271989 scopus 로고    scopus 로고
    • Expression-system-dependent modulation of HIV-1 envelope glycoprotein antigenicity and immunogenicity
    • Kong, L., Sheppard, N.C., Stewart-Jones, G.B., Robson, C.L., Chen, H., Xu, X., Krashias, G. et al. (2010) Expression-system-dependent modulation of HIV-1 envelope glycoprotein antigenicity and immunogenicity. J. Mol. Biol. 403, 131–147.
    • (2010) J. Mol. Biol. , vol.403 , pp. 131-147
    • Kong, L.1    Sheppard, N.C.2    Stewart-Jones, G.B.3    Robson, C.L.4    Chen, H.5    Xu, X.6    Krashias, G.7
  • 80
    • 84880161438 scopus 로고    scopus 로고
    • Supersite of immune vulnerability on the glycosylated face of HIV-1 envelope glycoprotein gp120
    • Kong, L., Lee, J.H., Doores, K.J., Murin, C.D., Julien, J.P., McBride, R., Liu, Y. et al. (2013) Supersite of immune vulnerability on the glycosylated face of HIV-1 envelope glycoprotein gp120. Nat. Struct. Mol. Biol. 20, 796–803.
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 796-803
    • Kong, L.1    Lee, J.H.2    Doores, K.J.3    Murin, C.D.4    Julien, J.P.5    McBride, R.6    Liu, Y.7
  • 81
    • 0038725418 scopus 로고    scopus 로고
    • Folding of HIV-1 envelope glycoprotein involves extensive isomerization of disulfide bonds and conformation-dependent leader peptide cleavage
    • Land, A., Zonneveld, D. and Braakman, I. (2003) Folding of HIV-1 envelope glycoprotein involves extensive isomerization of disulfide bonds and conformation-dependent leader peptide cleavage. FASEB J. 17, 1058–1067.
    • (2003) FASEB J. , vol.17 , pp. 1058-1067
    • Land, A.1    Zonneveld, D.2    Braakman, I.3
  • 82
    • 78650981716 scopus 로고    scopus 로고
    • Preclinical and clinical development of plant-made virus-like particle vaccine against avian H5N1 influenza
    • Landry, N., Ward, B.J., Trepanier, S., Montomoli, E., Dargis, M., Lapini, G. and Vezina, L.P. (2010) Preclinical and clinical development of plant-made virus-like particle vaccine against avian H5N1 influenza. PLoS ONE, 5, e15559.
    • (2010) PLoS ONE , vol.5
    • Landry, N.1    Ward, B.J.2    Trepanier, S.3    Montomoli, E.4    Dargis, M.5    Lapini, G.6    Vezina, L.P.7
  • 83
    • 84908368993 scopus 로고    scopus 로고
    • Influenza virus-like particle vaccines made in Nicotiana benthamiana elicit durable, poly-functional and cross-reactive T cell responses to influenza HA antigens
    • Landry, N., Pillet, S., Favre, D., Poulin, J.F., Trepanier, S., Yassine-Diab, B. and Ward, B.J. (2014) Influenza virus-like particle vaccines made in Nicotiana benthamiana elicit durable, poly-functional and cross-reactive T cell responses to influenza HA antigens. Clin. Immunol. 154, 164–177.
    • (2014) Clin. Immunol. , vol.154 , pp. 164-177
    • Landry, N.1    Pillet, S.2    Favre, D.3    Poulin, J.F.4    Trepanier, S.5    Yassine-Diab, B.6    Ward, B.J.7
  • 84
    • 84939251174 scopus 로고    scopus 로고
    • Review/N-glycans: the making of a varied toolbox
    • Lannoo, N. and Van Damme, E.J. (2015) Review/N-glycans: the making of a varied toolbox. Plant Sci. 239, 67–83.
    • (2015) Plant Sci. , vol.239 , pp. 67-83
    • Lannoo, N.1    Van Damme, E.J.2
  • 85
  • 86
    • 84929504999 scopus 로고    scopus 로고
    • Biochemical composition of haemagglutinin-based influenza virus-like particle vaccine produced by transient expression in tobacco plants
    • Le Mauff, F., Mercier, G., Chan, P., Burel, C., Vaudry, D., Bardor, M., Vezina, L.P. et al. (2015) Biochemical composition of haemagglutinin-based influenza virus-like particle vaccine produced by transient expression in tobacco plants. Plant Biotechnol. J. 13, 717–725.
    • (2015) Plant Biotechnol. J. , vol.13 , pp. 717-725
    • Le Mauff, F.1    Mercier, G.2    Chan, P.3    Burel, C.4    Vaudry, D.5    Bardor, M.6    Vezina, L.P.7
  • 87
    • 0025292252 scopus 로고
    • Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type 1 recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells
    • Leonard, C.K., Spellman, M.W., Riddle, L., Harris, R.J., Thomas, J.N. and Gregory, T.J. (1990) Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type 1 recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells. J. Biol. Chem. 265, 10373–10382.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10373-10382
    • Leonard, C.K.1    Spellman, M.W.2    Riddle, L.3    Harris, R.J.4    Thomas, J.N.5    Gregory, T.J.6
  • 88
    • 0029792920 scopus 로고    scopus 로고
    • Effects of inefficient cleavage of the signal sequence of HIV-1 gp 120 on its association with calnexin, folding, and intracellular transport
    • Li, Y., Bergeron, J.J., Luo, L., Ou, W.J., Thomas, D.Y. and Kang, C.Y. (1996) Effects of inefficient cleavage of the signal sequence of HIV-1 gp 120 on its association with calnexin, folding, and intracellular transport. Proc. Natl Acad. Sci. U. S. A. 93, 9606–9611.
    • (1996) Proc. Natl Acad. Sci. U. S. A. , vol.93 , pp. 9606-9611
    • Li, Y.1    Bergeron, J.J.2    Luo, L.3    Ou, W.J.4    Thomas, D.Y.5    Kang, C.Y.6
  • 89
    • 0034608884 scopus 로고    scopus 로고
    • The HIV-1 Env protein signal sequence retards its cleavage and down-regulates the glycoprotein folding
    • Li, Y., Luo, L., Thomas, D.Y. and Kang, C.Y. (2000) The HIV-1 Env protein signal sequence retards its cleavage and down-regulates the glycoprotein folding. Virology, 272, 417–428.
    • (2000) Virology , vol.272 , pp. 417-428
    • Li, Y.1    Luo, L.2    Thomas, D.Y.3    Kang, C.Y.4
  • 90
    • 33748313109 scopus 로고    scopus 로고
    • Accumulation of recombinant SARS-CoV spike protein in plant cytosol and chloroplasts indicate potential for development of plant-derived oral vaccines
    • Li, H.Y., Ramalingam, S. and Chye, M.L. (2006) Accumulation of recombinant SARS-CoV spike protein in plant cytosol and chloroplasts indicate potential for development of plant-derived oral vaccines. Exp. Biol. Med. (Maywood) 231, 1346–1352.
    • (2006) Exp. Biol. Med. (Maywood) , vol.231 , pp. 1346-1352
    • Li, H.Y.1    Ramalingam, S.2    Chye, M.L.3
  • 91
    • 0023749075 scopus 로고
    • Degradation from the endoplasmic reticulum: disposing of newly synthesized proteins
    • Lippincott-Schwartz, J., Bonifacino, J.S., Yuan, L.C. and Klausner, R.D. (1988) Degradation from the endoplasmic reticulum: disposing of newly synthesized proteins. Cell, 54, 209–220.
    • (1988) Cell , vol.54 , pp. 209-220
    • Lippincott-Schwartz, J.1    Bonifacino, J.S.2    Yuan, L.C.3    Klausner, R.D.4
  • 92
    • 78049457576 scopus 로고    scopus 로고
    • Endoplasmic reticulum protein quality control and its relationship to environmental stress responses in plants
    • Liu, J.X. and Howell, S.H. (2010) Endoplasmic reticulum protein quality control and its relationship to environmental stress responses in plants. Plant Cell. 22, 2930–2942.
    • (2010) Plant Cell. , vol.22 , pp. 2930-2942
    • Liu, J.X.1    Howell, S.H.2
  • 93
  • 94
    • 84864306068 scopus 로고    scopus 로고
    • Induction of a protective immune response to rabies virus in sheep after oral immunization with transgenic maize, expressing the rabies virus glycoprotein
    • Loza-Rubio, E., Rojas-Anaya, E., Lopez, J., Olivera-Flores, M.T., Gomez-Lim, M. and Tapia-Perez, G. (2012) Induction of a protective immune response to rabies virus in sheep after oral immunization with transgenic maize, expressing the rabies virus glycoprotein. Vaccine, 30, 5551–5556.
    • (2012) Vaccine , vol.30 , pp. 5551-5556
    • Loza-Rubio, E.1    Rojas-Anaya, E.2    Lopez, J.3    Olivera-Flores, M.T.4    Gomez-Lim, M.5    Tapia-Perez, G.6
  • 95
    • 84890859441 scopus 로고    scopus 로고
    • Cryo-EM structure of a fully glycosylated soluble cleaved HIV-1 envelope trimer
    • Lyumkis, D., Julien, J.P., de Val, N., Cupo, A., Potter, C.S., Klasse, P.J., Burton, D.R. et al. (2013) Cryo-EM structure of a fully glycosylated soluble cleaved HIV-1 envelope trimer. Science, 342, 1484–1490.
    • (2013) Science , vol.342 , pp. 1484-1490
    • Lyumkis, D.1    Julien, J.P.2    de Val, N.3    Cupo, A.4    Potter, C.S.5    Klasse, P.J.6    Burton, D.R.7
  • 96
    • 84888130117 scopus 로고    scopus 로고
    • Realising the value of plant molecular pharming to benefit the poor in developing countries and emerging economies
    • Ma, J.K., Christou, P., Chikwamba, R., Haydon, H., Paul, M., Ferrer, M.P., Ramalingam, S. et al. (2013) Realising the value of plant molecular pharming to benefit the poor in developing countries and emerging economies. Plant Biotechnol. J. 11, 1029–1033.
    • (2013) Plant Biotechnol. J. , vol.11 , pp. 1029-1033
    • Ma, J.K.1    Christou, P.2    Chikwamba, R.3    Haydon, H.4    Paul, M.5    Ferrer, M.P.6    Ramalingam, S.7
  • 97
    • 84942427613 scopus 로고    scopus 로고
    • Intranasal vaccination with a plant-derived H5 HA vaccine protects mice and ferrets against highly pathogenic avian influenza virus challenge
    • Major, D., Chichester, J.A., Pathirana, R.D., Guilfoyle, K., Shoji, Y., Guzman, C.A., Yusibov, V. et al. (2015) Intranasal vaccination with a plant-derived H5 HA vaccine protects mice and ferrets against highly pathogenic avian influenza virus challenge. Hum. Vacc. Immunother. 11, 1235–1243.
    • (2015) Hum. Vacc. Immunother. , vol.11 , pp. 1235-1243
    • Major, D.1    Chichester, J.A.2    Pathirana, R.D.3    Guilfoyle, K.4    Shoji, Y.5    Guzman, C.A.6    Yusibov, V.7
  • 99
    • 47049100427 scopus 로고    scopus 로고
    • Nanoparticles target distinct dendritic cell populations according to their size
    • Manolova, V., Flace, A., Bauer, M., Schwarz, K., Saudan, P. and Bachmann, M.F. (2008) Nanoparticles target distinct dendritic cell populations according to their size. Eur. J. Immunol. 38, 1404–1413.
    • (2008) Eur. J. Immunol. , vol.38 , pp. 1404-1413
    • Manolova, V.1    Flace, A.2    Bauer, M.3    Schwarz, K.4    Saudan, P.5    Bachmann, M.F.6
  • 101
    • 77952239645 scopus 로고    scopus 로고
    • Exploring different strategies to express Dengue virus envelope protein in a plant system
    • Martinez, C.A., Topal, E., Giulietti, A.M., Talou, J.R. and Mason, H. (2010) Exploring different strategies to express Dengue virus envelope protein in a plant system. Biotechnol. Lett. 32, 867–875.
    • (2010) Biotechnol. Lett. , vol.32 , pp. 867-875
    • Martinez, C.A.1    Topal, E.2    Giulietti, A.M.3    Talou, J.R.4    Mason, H.5
  • 104
    • 84878626061 scopus 로고    scopus 로고
    • Engineering HIV envelope protein to activate germline B cell receptors of broadly neutralizing anti-CD4 binding site antibodies
    • McGuire, A.T., Hoot, S., Dreyer, A.M., Lippy, A., Stuart, A., Cohen, K.W., Jardine, J. et al. (2013) Engineering HIV envelope protein to activate germline B cell receptors of broadly neutralizing anti-CD4 binding site antibodies. J. Exp. Med. 210, 655–663.
    • (2013) J. Exp. Med. , vol.210 , pp. 655-663
    • McGuire, A.T.1    Hoot, S.2    Dreyer, A.M.3    Lippy, A.4    Stuart, A.5    Cohen, K.W.6    Jardine, J.7
  • 107
    • 33144486096 scopus 로고    scopus 로고
    • Nature of nonfunctional envelope proteins on the surface of human immunodeficiency virus type 1
    • Moore, P.L., Crooks, E.T., Porter, L., Zhu, P., Cayanan, C.S., Grise, H., Corcoran, P. et al. (2006) Nature of nonfunctional envelope proteins on the surface of human immunodeficiency virus type 1. J. Virol. 80, 2515–2528.
    • (2006) J. Virol. , vol.80 , pp. 2515-2528
    • Moore, P.L.1    Crooks, E.T.2    Porter, L.3    Zhu, P.4    Cayanan, C.S.5    Grise, H.6    Corcoran, P.7
  • 109
  • 110
    • 84873506978 scopus 로고    scopus 로고
    • Designing tomorrow's vaccines
    • Nabel, G.J. (2013) Designing tomorrow's vaccines. N. Engl. J. Med. 368, 551–560.
    • (2013) N. Engl. J. Med. , vol.368 , pp. 551-560
    • Nabel, G.J.1
  • 111
    • 0031035644 scopus 로고    scopus 로고
    • Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins
    • Oliver, J.D., van der Wal, F.J., Bulleid, N.J. and High, S. (1997) Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins. Science, 275, 86–88.
    • (1997) Science , vol.275 , pp. 86-88
    • Oliver, J.D.1    van der Wal, F.J.2    Bulleid, N.J.3    High, S.4
  • 112
    • 0032807338 scopus 로고    scopus 로고
    • ERp57 functions as a subunit of specific complexes formed with the ER lectins calreticulin and calnexin
    • Oliver, J.D., Roderick, H.L., Llewellyn, D.H. and High, S. (1999) ERp57 functions as a subunit of specific complexes formed with the ER lectins calreticulin and calnexin. Mol. Biol. Cell. 10, 2573–2582.
    • (1999) Mol. Biol. Cell. , vol.10 , pp. 2573-2582
    • Oliver, J.D.1    Roderick, H.L.2    Llewellyn, D.H.3    High, S.4
  • 113
    • 0025203223 scopus 로고
    • The human immunodeficiency virus type 1 envelope glycoprotein precursor acquires aberrant intermolecular disulfide bonds that may prevent normal proteolytic processing
    • Owens, R.J. and Compans, R.W. (1990) The human immunodeficiency virus type 1 envelope glycoprotein precursor acquires aberrant intermolecular disulfide bonds that may prevent normal proteolytic processing. Virology, 179, 827–833.
    • (1990) Virology , vol.179 , pp. 827-833
    • Owens, R.J.1    Compans, R.W.2
  • 114
    • 33845760011 scopus 로고    scopus 로고
    • Engineering of a sialic acid synthesis pathway in transgenic plants by expression of bacterial Neu5Ac-synthesizing enzymes
    • Paccalet, T., Bardor, M., Rihouey, C., Delmas, F., Chevalier, C., D'Aoust, M.A., Faye, L. et al. (2007) Engineering of a sialic acid synthesis pathway in transgenic plants by expression of bacterial Neu5Ac-synthesizing enzymes. Plant Biotechnol. J. 5, 16–25.
    • (2007) Plant Biotechnol. J. , vol.5 , pp. 16-25
    • Paccalet, T.1    Bardor, M.2    Rihouey, C.3    Delmas, F.4    Chevalier, C.5    D'Aoust, M.A.6    Faye, L.7
  • 115
    • 85025101545 scopus 로고    scopus 로고
    • Elicitation of Robust Tier 2 Neutralizing Antibody Responses in Nonhuman Primates by HIV Envelope Trimer Immunization Using Optimized Approaches
    • e1076.
    • Pauthner, M., Havenar-Daughton, C., Sok, D., Nkolola, J.P., Bastidas, R., Boopathy, A.V., Carnathan, D.G. et al. (2017) Elicitation of Robust Tier 2 Neutralizing Antibody Responses in Nonhuman Primates by HIV Envelope Trimer Immunization Using Optimized Approaches. Immunity, 46, 1073–1088. e1076.
    • (2017) Immunity , vol.46 , pp. 1073-1088
    • Pauthner, M.1    Havenar-Daughton, C.2    Sok, D.3    Nkolola, J.P.4    Bastidas, R.5    Boopathy, A.V.6    Carnathan, D.G.7
  • 116
  • 118
    • 84946615903 scopus 로고    scopus 로고
    • Plant-derived H7 VLP vaccine elicits protective immune response against H7N9 influenza virus in mice and ferrets
    • Pillet, S., Racine, T., Nfon, C., Di Lenardo, T.Z., Babiuk, S., Ward, B.J., Kobinger, G.P. et al. (2015) Plant-derived H7 VLP vaccine elicits protective immune response against H7N9 influenza virus in mice and ferrets. Vaccine, 33, 6282–6289.
    • (2015) Vaccine , vol.33 , pp. 6282-6289
    • Pillet, S.1    Racine, T.2    Nfon, C.3    Di Lenardo, T.Z.4    Babiuk, S.5    Ward, B.J.6    Kobinger, G.P.7
  • 119
    • 84973565832 scopus 로고    scopus 로고
    • A plant-derived quadrivalent virus like particle influenza vaccine induces cross-reactive antibody and T cell response in healthy adults
    • Pillet, S., Aubin, E., Trepanier, S., Bussiere, D., Dargis, M., Poulin, J.F., Yassine-Diab, B. et al. (2016) A plant-derived quadrivalent virus like particle influenza vaccine induces cross-reactive antibody and T cell response in healthy adults. Clin. Immunol. 168, 72–87.
    • (2016) Clin. Immunol. , vol.168 , pp. 72-87
    • Pillet, S.1    Aubin, E.2    Trepanier, S.3    Bussiere, D.4    Dargis, M.5    Poulin, J.F.6    Yassine-Diab, B.7
  • 122
    • 84965048029 scopus 로고    scopus 로고
    • Progress in developing virus-like particle influenza vaccines
    • Quan, F.S., Lee, Y.T., Kim, K.H., Kim, M.C. and Kang, S.M. (2016) Progress in developing virus-like particle influenza vaccines. Expert. Rev. Vaccines, 15, 1281–1293.
    • (2016) Expert. Rev. Vaccines , vol.15 , pp. 1281-1293
    • Quan, F.S.1    Lee, Y.T.2    Kim, K.H.3    Kim, M.C.4    Kang, S.M.5
  • 123
    • 84887307095 scopus 로고    scopus 로고
    • Cleavage strongly influences whether soluble HIV-1 envelope glycoprotein trimers adopt a native-like conformation
    • Ringe, R.P., Sanders, R.W., Yasmeen, A., Kim, H.J., Lee, J.H., Cupo, A., Korzun, J. et al. (2013) Cleavage strongly influences whether soluble HIV-1 envelope glycoprotein trimers adopt a native-like conformation. Proc. Natl Acad. Sci. U. S. A. 110, 18256–18261.
    • (2013) Proc. Natl Acad. Sci. U. S. A. , vol.110 , pp. 18256-18261
    • Ringe, R.P.1    Sanders, R.W.2    Yasmeen, A.3    Kim, H.J.4    Lee, J.H.5    Cupo, A.6    Korzun, J.7
  • 125
    • 84875343381 scopus 로고    scopus 로고
    • Rapid high-level production of functional HIV broadly neutralizing monoclonal antibodies in transient plant expression systems
    • Rosenberg, Y., Sack, M., Montefiori, D., Forthal, D., Mao, L., Hernandez-Abanto, S., Urban, L. et al. (2013) Rapid high-level production of functional HIV broadly neutralizing monoclonal antibodies in transient plant expression systems. PLoS ONE, 8, e58724.
    • (2013) PLoS ONE , vol.8
    • Rosenberg, Y.1    Sack, M.2    Montefiori, D.3    Forthal, D.4    Mao, L.5    Hernandez-Abanto, S.6    Urban, L.7
  • 126
    • 0030046574 scopus 로고    scopus 로고
    • In vitro folding of inclusion body proteins
    • Rudolph, R. and Lilie, H. (1996) In vitro folding of inclusion body proteins. FASEB J. 10, 49–56.
    • (1996) FASEB J. , vol.10 , pp. 49-56
    • Rudolph, R.1    Lilie, H.2
  • 127
    • 77956684691 scopus 로고    scopus 로고
    • Functional relationship between protein disulfide isomerase family members during the oxidative folding of human secretory proteins
    • Rutkevich, L.A., Cohen-Doyle, M.F., Brockmeier, U. and Williams, D.B. (2010) Functional relationship between protein disulfide isomerase family members during the oxidative folding of human secretory proteins. Mol. Biol. Cell. 21, 3093–3105.
    • (2010) Mol. Biol. Cell. , vol.21 , pp. 3093-3105
    • Rutkevich, L.A.1    Cohen-Doyle, M.F.2    Brockmeier, U.3    Williams, D.B.4
  • 128
    • 58149112262 scopus 로고    scopus 로고
    • Plant-produced vaccines: promise and reality
    • Rybicki, E.P. (2009) Plant-produced vaccines: promise and reality. Drug Discov. Today 14, 16–24.
    • (2009) Drug Discov. Today , vol.14 , pp. 16-24
    • Rybicki, E.P.1
  • 129
    • 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
  • 130
    • 84936865223 scopus 로고    scopus 로고
    • Plant based vaccines against viruses
    • Rybicki, E.P. (2014) Plant based vaccines against viruses. Virology Journal 11, 205.
    • (2014) Virology Journal , vol.11 , pp. 205
    • Rybicki, E.P.1
  • 131
    • 85045677925 scopus 로고    scopus 로고
    • Plant-made vaccines and reagents for the One Health initiative
    • Rybicki, E.P. (2017) Plant-made vaccines and reagents for the One Health initiative. Hum. Vaccin. Immunother. 13, 2912–2917.
    • (2017) Hum. Vaccin. Immunother. , vol.13 , pp. 2912-2917
    • Rybicki, E.P.1
  • 132
    • 84874073920 scopus 로고    scopus 로고
    • Developing country applications of molecular farming: case studies in South Africa and Argentina
    • Rybicki, E.P., Hitzeroth, I.I., Meyers, A., Dus Santos, M.J. and Wigdorovitz, A. (2013) Developing country applications of molecular farming: case studies in South Africa and Argentina. Curr. Pharm. Des. 19, 5612–5621.
    • (2013) Curr. Pharm. Des. , vol.19 , pp. 5612-5621
    • Rybicki, E.P.1    Hitzeroth, I.I.2    Meyers, A.3    Dus Santos, M.J.4    Wigdorovitz, A.5
  • 133
    • 34547819753 scopus 로고    scopus 로고
    • Production of dengue 2 envelope domain III in plant using TMV-based vector system
    • Saejung, W., Fujiyama, K., Takasaki, T., Ito, M., Hori, K., Malasit, P., Watanabe, Y. et al. (2007) Production of dengue 2 envelope domain III in plant using TMV-based vector system. Vaccine, 25, 6646–6654.
    • (2007) Vaccine , vol.25 , pp. 6646-6654
    • Saejung, W.1    Fujiyama, K.2    Takasaki, T.3    Ito, M.4    Hori, K.5    Malasit, P.6    Watanabe, Y.7
  • 134
    • 84886412961 scopus 로고    scopus 로고
    • Chaperone machines for protein folding, unfolding and disaggregation
    • Saibil, H. (2013) Chaperone machines for protein folding, unfolding and disaggregation. Nat. Rev. Mol. Cell. Biol. 14, 630–642.
    • (2013) Nat. Rev. Mol. Cell. Biol. , vol.14 , pp. 630-642
    • Saibil, H.1
  • 135
    • 85010843359 scopus 로고    scopus 로고
    • Native-like Env trimers as a platform for HIV-1 vaccine design
    • Sanders, R.W. and Moore, J.P. (2017) Native-like Env trimers as a platform for HIV-1 vaccine design. Immunol. Rev. 275, 161–182.
    • (2017) Immunol. Rev. , vol.275 , pp. 161-182
    • Sanders, R.W.1    Moore, J.P.2
  • 136
    • 0036637385 scopus 로고    scopus 로고
    • The mannose-dependent epitope for neutralizing antibody 2G12 on human immunodeficiency virus type 1 glycoprotein gp120
    • Sanders, R.W., Venturi, M., Schiffner, L., Kalyanaraman, R., Katinger, H., Lloyd, K.O., Kwong, P.D. et al. (2002) The mannose-dependent epitope for neutralizing antibody 2G12 on human immunodeficiency virus type 1 glycoprotein gp120. J. Virol. 76, 7293–7305.
    • (2002) J. Virol. , vol.76 , pp. 7293-7305
    • Sanders, R.W.1    Venturi, M.2    Schiffner, L.3    Kalyanaraman, R.4    Katinger, H.5    Lloyd, K.O.6    Kwong, P.D.7
  • 137
    • 84884678235 scopus 로고    scopus 로고
    • A next-generation cleaved, soluble HIV-1 Env trimer, BG505 SOSIP.664 gp140, expresses multiple epitopes for broadly neutralizing but not non-neutralizing antibodies
    • Sanders, R.W., Derking, R., Cupo, A., Julien, J.P., Yasmeen, A., de Val, N., Kim, H.J. et al. (2013) A next-generation cleaved, soluble HIV-1 Env trimer, BG505 SOSIP.664 gp140, expresses multiple epitopes for broadly neutralizing but not non-neutralizing antibodies. PLoS Pathog. 9, e1003618.
    • (2013) PLoS Pathog. , vol.9
    • Sanders, R.W.1    Derking, R.2    Cupo, A.3    Julien, J.P.4    Yasmeen, A.5    de Val, N.6    Kim, H.J.7
  • 138
    • 18244422922 scopus 로고    scopus 로고
    • The broadly neutralizing anti-human immunodeficiency virus type 1 antibody 2G12 recognizes a cluster of alpha1–>2 mannose residues on the outer face of gp120
    • Scanlan, C.N., Pantophlet, R., Wormald, M.R., Ollmann Saphire, E., Stanfield, R., Wilson, I.A., Katinger, H. et al. (2002) The broadly neutralizing anti-human immunodeficiency virus type 1 antibody 2G12 recognizes a cluster of alpha1–>2 mannose residues on the outer face of gp120. J. Virol. 76, 7306–7321.
    • (2002) J. Virol. , vol.76 , pp. 7306-7321
    • Scanlan, C.N.1    Pantophlet, R.2    Wormald, M.R.3    Ollmann Saphire, E.4    Stanfield, R.5    Wilson, I.A.6    Katinger, H.7
  • 140
    • 84883049428 scopus 로고    scopus 로고
    • The HIV-1 epidemic: low- to middle-income countries
    • Shao, Y. and Williamson, C. (2012) The HIV-1 epidemic: low- to middle-income countries. Cold Spring Harb. Perspect Med. 2, a007187.
    • (2012) Cold Spring Harb. Perspect Med. , vol.2 , pp. a007187
    • Shao, Y.1    Williamson, C.2
  • 141
    • 84928583366 scopus 로고    scopus 로고
    • Cleavage-independent HIV-1 Env trimers engineered as soluble native spike mimetics for vaccine design
    • Sharma, S.K., de Val, N., Bale, S., Guenaga, J., Tran, K., Feng, Y., Dubrovskaya, V. et al. (2015) Cleavage-independent HIV-1 Env trimers engineered as soluble native spike mimetics for vaccine design. Cell. Rep. 11, 539–550.
    • (2015) Cell. Rep. , vol.11 , pp. 539-550
    • Sharma, S.K.1    de Val, N.2    Bale, S.3    Guenaga, J.4    Tran, K.5    Feng, Y.6    Dubrovskaya, V.7
  • 143
    • 58549091833 scopus 로고    scopus 로고
    • Plant-derived hemagglutinin protects ferrets against challenge infection with the A/Indonesia/05/05 strain of avian influenza
    • Shoji, Y., Bi, H., Musiychuk, K., Rhee, A., Horsey, A., Roy, G., Green, B. et al. (2009a) Plant-derived hemagglutinin protects ferrets against challenge infection with the A/Indonesia/05/05 strain of avian influenza. Vaccine, 27, 1087–1092.
    • (2009) Vaccine , vol.27 , pp. 1087-1092
    • Shoji, Y.1    Bi, H.2    Musiychuk, K.3    Rhee, A.4    Horsey, A.5    Roy, G.6    Green, B.7
  • 144
    • 65549136839 scopus 로고    scopus 로고
    • Immunogenicity of hemagglutinin from A/Bar-headed Goose/Qinghai/1A/05 and A/Anhui/1/05 strains of H5N1 influenza viruses produced in Nicotiana benthamiana plants
    • Shoji, Y., Farrance, C.E., Bi, H., Shamloul, M., Green, B., Manceva, S., Rhee, A. et al. (2009b) Immunogenicity of hemagglutinin from A/Bar-headed Goose/Qinghai/1A/05 and A/Anhui/1/05 strains of H5N1 influenza viruses produced in Nicotiana benthamiana plants. Vaccine, 27, 3467–3470.
    • (2009) Vaccine , vol.27 , pp. 3467-3470
    • Shoji, Y.1    Farrance, C.E.2    Bi, H.3    Shamloul, M.4    Green, B.5    Manceva, S.6    Rhee, A.7
  • 145
    • 84863393057 scopus 로고    scopus 로고
    • Plant-based rapid production of recombinant subunit hemagglutinin vaccines targeting H1N1 and H5N1 influenza
    • Shoji, Y., Chichester, J.A., Jones, M., Manceva, S.D., Damon, E., Mett, V., Musiychuk, K. et al. (2011) Plant-based rapid production of recombinant subunit hemagglutinin vaccines targeting H1N1 and H5N1 influenza. Hum. Vaccin. 7(Suppl), 41–50.
    • (2011) Hum. Vaccin. , vol.7 , pp. 41-50
    • Shoji, Y.1    Chichester, J.A.2    Jones, M.3    Manceva, S.D.4    Damon, E.5    Mett, V.6    Musiychuk, K.7
  • 149
    • 84901236516 scopus 로고    scopus 로고
    • Promiscuous glycan site recognition by antibodies to the high-mannose patch of gp120 broadens neutralization of HIV
    • Sok, D., Doores, K.J., Briney, B., Le, K.M., Saye-Francisco, K.L., Ramos, A., Kulp, D.W. et al. (2014) Promiscuous glycan site recognition by antibodies to the high-mannose patch of gp120 broadens neutralization of HIV. Sci. Transl. Med. 6, 236ra263.
    • (2014) Sci. Transl. Med. , vol.6 , pp. 236ra263
    • Sok, D.1    Doores, K.J.2    Briney, B.3    Le, K.M.4    Saye-Francisco, K.L.5    Ramos, A.6    Kulp, D.W.7
  • 150
    • 84990856306 scopus 로고    scopus 로고
    • A Prominent Site of Antibody Vulnerability on HIV Envelope Incorporates a Motif Associated with CCR5 Binding and Its Camouflaging Glycans
    • Sok, D., Pauthner, M., Briney, B., Lee, J.H., Saye-Francisco, K.L., Hsueh, J., Ramos, A. et al. (2016) A Prominent Site of Antibody Vulnerability on HIV Envelope Incorporates a Motif Associated with CCR5 Binding and Its Camouflaging Glycans. Immunity, 45, 31–45.
    • (2016) Immunity , vol.45 , pp. 31-45
    • Sok, D.1    Pauthner, M.2    Briney, B.3    Lee, J.H.4    Saye-Francisco, K.L.5    Hsueh, J.6    Ramos, A.7
  • 151
    • 0027327659 scopus 로고
    • A protein translocation defect linked to ubiquitin conjugation at the endoplasmic reticulum
    • Sommer, T. and Jentsch, S. (1993) A protein translocation defect linked to ubiquitin conjugation at the endoplasmic reticulum. Nature, 365, 176–179.
    • (1993) Nature , vol.365 , pp. 176-179
    • Sommer, T.1    Jentsch, S.2
  • 152
    • 0033602713 scopus 로고    scopus 로고
    • Role of hemagglutinin cleavage for the pathogenicity of influenza virus
    • Steinhauer, D.A. (1999) Role of hemagglutinin cleavage for the pathogenicity of influenza virus. Virology, 258, 1–20.
    • (1999) Virology , vol.258 , pp. 1-20
    • Steinhauer, D.A.1
  • 153
    • 84935861496 scopus 로고    scopus 로고
    • N-glyco-engineering in plants: update on strategies and major achievements
    • Steinkellner, H. and Castilho, A. (2015) N-glyco-engineering in plants: update on strategies and major achievements. Methods Mol. Biol. 1321, 195–212.
    • (2015) Methods Mol. Biol. , vol.1321 , pp. 195-212
    • Steinkellner, H.1    Castilho, A.2
  • 154
    • 0026643396 scopus 로고
    • Influenza virus hemagglutinin with multibasic cleavage site is activated by furin, a subtilisin-like endoprotease
    • Stieneke-Grober, A., Vey, M., Angliker, H., Shaw, E., Thomas, G., Roberts, C., Klenk, H.D. et al. (1992) Influenza virus hemagglutinin with multibasic cleavage site is activated by furin, a subtilisin-like endoprotease. EMBO J. 11, 2407–2414.
    • (1992) EMBO J. , vol.11 , pp. 2407-2414
    • Stieneke-Grober, A.1    Vey, M.2    Angliker, H.3    Shaw, E.4    Thomas, G.5    Roberts, C.6    Klenk, H.D.7
  • 155
    • 84899729872 scopus 로고    scopus 로고
    • Plant molecular pharming for the treatment of chronic and infectious diseases
    • Stoger, E., Fischer, R., Moloney, M. and Ma, J.K. (2014) Plant molecular pharming for the treatment of chronic and infectious diseases. Annu. Rev. Plant Biol. 65, 743–768.
    • (2014) Annu. Rev. Plant Biol. , vol.65 , pp. 743-768
    • Stoger, E.1    Fischer, R.2    Moloney, M.3    Ma, J.K.4
  • 156
    • 85046727833 scopus 로고    scopus 로고
    • Protein Quality Control in the Endoplasmic Reticulum of Plants
    • Strasser, R. (2018) Protein Quality Control in the Endoplasmic Reticulum of Plants. Annu. Rev. Plant Biol. 69, 147–172.
    • (2018) Annu. Rev. Plant Biol. , vol.69 , pp. 147-172
    • Strasser, R.1
  • 157
    • 41749105290 scopus 로고    scopus 로고
    • Generation of glyco-engineered Nicotiana benthamiana for the production of monoclonal antibodies with a homogeneous human-like N-glycan structure
    • Strasser, R., Stadlmann, J., Schahs, M., Stiegler, G., Quendler, H., Mach, L., Glossl, J. et al. (2008) Generation of glyco-engineered Nicotiana benthamiana for the production of monoclonal antibodies with a homogeneous human-like N-glycan structure. Plant Biotechnol. J. 6, 392–402.
    • (2008) Plant Biotechnol. J. , vol.6 , pp. 392-402
    • Strasser, R.1    Stadlmann, J.2    Schahs, M.3    Stiegler, G.4    Quendler, H.5    Mach, L.6    Glossl, J.7
  • 158
    • 84903758537 scopus 로고    scopus 로고
    • Controlled glycosylation of plant-produced recombinant proteins
    • Strasser, R., Altmann, F. and Steinkellner, H. (2014) Controlled glycosylation of plant-produced recombinant proteins. Curr. Opin. Biotechnol. 30, 95–100.
    • (2014) Curr. Opin. Biotechnol. , vol.30 , pp. 95-100
    • Strasser, R.1    Altmann, F.2    Steinkellner, H.3
  • 159
    • 84942133215 scopus 로고    scopus 로고
    • Plant-produced candidate countermeasures against emerging and reemerging infections and bioterror agents
    • Streatfield, S.J., Kushnir, N. and Yusibov, V. (2015) Plant-produced candidate countermeasures against emerging and reemerging infections and bioterror agents. Plant Biotechnol. J. 13, 1136–1159.
    • (2015) Plant Biotechnol. J. , vol.13 , pp. 1136-1159
    • Streatfield, S.J.1    Kushnir, N.2    Yusibov, V.3
  • 160
    • 0026100208 scopus 로고
    • Enhanced secretion from insect cells of a foreign protein fused to the honeybee melittin signal peptide
    • Tessier, D.C., Thomas, D.Y., Khouri, H.E., Laliberte, F. and Vernet, T. (1991) Enhanced secretion from insect cells of a foreign protein fused to the honeybee melittin signal peptide. Gene, 98, 177–183.
    • (1991) Gene , vol.98 , pp. 177-183
    • Tessier, D.C.1    Thomas, D.Y.2    Khouri, H.E.3    Laliberte, F.4    Vernet, T.5
  • 161
    • 85041516091 scopus 로고    scopus 로고
    • Plant-produced subunit vaccine candidates against yellow fever induce virus neutralizing antibodies and confer protection against viral challenge in animal models
    • Tottey, S., Shoji, Y., Jones, R.M., Chichester, J.A., Green, B.J., Musiychuk, K., Si, H. et al. (2018) Plant-produced subunit vaccine candidates against yellow fever induce virus neutralizing antibodies and confer protection against viral challenge in animal models. Am. J. Trop. Med. Hyg. 98, 420–431.
    • (2018) Am. J. Trop. Med. Hyg. , vol.98 , pp. 420-431
    • Tottey, S.1    Shoji, Y.2    Jones, R.M.3    Chichester, J.A.4    Green, B.J.5    Musiychuk, K.6    Si, H.7
  • 162
    • 84894355475 scopus 로고    scopus 로고
    • Vaccine-elicited primate antibodies use a distinct approach to the HIV-1 primary receptor binding site informing vaccine redesign
    • Tran, K., Poulsen, C., Guenaga, J., de Val, N., Wilson, R., Sundling, C., Li, Y. et al. (2014) Vaccine-elicited primate antibodies use a distinct approach to the HIV-1 primary receptor binding site informing vaccine redesign. Proc. Natl Acad. Sci. U. S. A. 111, E738–E747.
    • (2014) Proc. Natl Acad. Sci. U. S. A. , vol.111 , pp. E738-E747
    • Tran, K.1    Poulsen, C.2    Guenaga, J.3    de Val, N.4    Wilson, R.5    Sundling, C.6    Li, Y.7
  • 163
    • 9044241681 scopus 로고    scopus 로고
    • Human monoclonal antibody 2G12 defines a distinctive neutralization epitope on the gp120 glycoprotein of human immunodeficiency virus type 1
    • Trkola, A., Purtscher, M., Muster, T., Ballaun, C., Buchacher, A., Sullivan, N., Srinivasan, K. et al. (1996) Human monoclonal antibody 2G12 defines a distinctive neutralization epitope on the gp120 glycoprotein of human immunodeficiency virus type 1. J. Virol. 70, 1100–1108.
    • (1996) J. Virol. , vol.70 , pp. 1100-1108
    • Trkola, A.1    Purtscher, M.2    Muster, T.3    Ballaun, C.4    Buchacher, A.5    Sullivan, N.6    Srinivasan, K.7
  • 165
    • 0029868289 scopus 로고    scopus 로고
    • Comparative cellular processing of the human immunodeficiency virus (HIV-1) envelope glycoprotein gp160 by the mammalian subtilisin/kexin-like convertases
    • Vollenweider, F., Benjannet, S., Decroly, E., Savaria, D., Lazure, C., Thomas, G., Chretien, M. et al. (1996) Comparative cellular processing of the human immunodeficiency virus (HIV-1) envelope glycoprotein gp160 by the mammalian subtilisin/kexin-like convertases. Biochem. J. 314(Pt 2), 521–532.
    • (1996) Biochem. J. , vol.314 , pp. 521-532
    • Vollenweider, F.1    Benjannet, S.2    Decroly, E.3    Savaria, D.4    Lazure, C.5    Thomas, G.6    Chretien, M.7
  • 166
    • 0025937289 scopus 로고
    • SSR alpha and associated calnexin are major calcium binding proteins of the endoplasmic reticulum membrane
    • Wada, I., Rindress, D., Cameron, P.H., Ou, W.J., Doherty, J.J. 2nd, Louvard, D., Bell, A.W. et al. (1991) SSR alpha and associated calnexin are major calcium binding proteins of the endoplasmic reticulum membrane. J. Biol. Chem. 266, 19599–19610.
    • (1991) J. Biol. Chem. , vol.266 , pp. 19599-19610
    • Wada, I.1    Rindress, D.2    Cameron, P.H.3    Ou, W.J.4    Doherty, J.J.5    Louvard, D.6    Bell, A.W.7
  • 167
    • 0028840915 scopus 로고
    • Degradation of CFTR by the ubiquitin-proteasome pathway
    • Ward, C.L., Omura, S. and Kopito, R.R. (1995) Degradation of CFTR by the ubiquitin-proteasome pathway. Cell, 83, 121–127.
    • (1995) Cell , vol.83 , pp. 121-127
    • Ward, C.L.1    Omura, S.2    Kopito, R.R.3
  • 168
    • 84908003879 scopus 로고    scopus 로고
    • Human antibody response to N-glycans present on plant-made influenza virus-like particle (VLP) vaccines
    • Ward, B.J., Landry, N., Trepanier, S., Mercier, G., Dargis, M., Couture, M., D'Aoust, M.A. et al. (2014) Human antibody response to N-glycans present on plant-made influenza virus-like particle (VLP) vaccines. Vaccine, 32, 6098–6106.
    • (2014) Vaccine , vol.32 , pp. 6098-6106
    • Ward, B.J.1    Landry, N.2    Trepanier, S.3    Mercier, G.4    Dargis, M.5    Couture, M.6    D'Aoust, M.A.7
  • 170
    • 77952969448 scopus 로고    scopus 로고
    • Cross-neutralization of 1918 and 2009 influenza viruses: role of glycans in viral evolution and vaccine design
    • Wei, C.J., Boyington, J.C., Dai, K., Houser, K.V., Pearce, M.B., Kong, W.P., Yang, Z.Y. et al. (2010) Cross-neutralization of 1918 and 2009 influenza viruses: role of glycans in viral evolution and vaccine design. Sci. Transl. Med. 2, 24ra21.
    • (2010) Sci. Transl. Med. , vol.2 , pp. 24ra21
    • Wei, C.J.1    Boyington, J.C.2    Dai, K.3    Houser, K.V.4    Pearce, M.B.5    Kong, W.P.6    Yang, Z.Y.7
  • 172
    • 84979053791 scopus 로고    scopus 로고
    • Co-expression of the protease furin in Nicotiana benthamiana leads to efficient processing of latent transforming growth factor-beta1 into a biologically active protein
    • Wilbers, R.H., Westerhof, L.B., van Raaij, D.R., van Adrichem, M., Prakasa, A.D., Lozano-Torres, J.L., Bakker, J. et al. (2016) Co-expression of the protease furin in Nicotiana benthamiana leads to efficient processing of latent transforming growth factor-beta1 into a biologically active protein. Plant Biotechnol. J. 14, 1695–1704.
    • (2016) Plant Biotechnol. J. , vol.14 , pp. 1695-1704
    • Wilbers, R.H.1    Westerhof, L.B.2    van Raaij, D.R.3    van Adrichem, M.4    Prakasa, A.D.5    Lozano-Torres, J.L.6    Bakker, J.7
  • 173
    • 84959224002 scopus 로고    scopus 로고
    • Zika virus outbreak in the Americas: the need for novel mosquito control methods
    • Yakob, L. and Walker, T. (2016) Zika virus outbreak in the Americas: the need for novel mosquito control methods. Lancet Glob. Health, 4, e148–e149.
    • (2016) Lancet Glob. Health , vol.4 , pp. e148-e149
    • Yakob, L.1    Walker, T.2
  • 174
    • 85027223330 scopus 로고    scopus 로고
    • Virus-like particles that display Zika virus envelope protein domain III induce potent neutralizing immune responses in mice
    • Yang, M., Lai, H., Sun, H. and Chen, Q. (2017a) Virus-like particles that display Zika virus envelope protein domain III induce potent neutralizing immune responses in mice. Sci. Rep. 7, 7679.
    • (2017) Sci. Rep. , vol.7 , pp. 7679
    • Yang, M.1    Lai, H.2    Sun, H.3    Chen, Q.4
  • 175
    • 85041077013 scopus 로고    scopus 로고
    • Plant-produced Zika virus envelope protein elicits neutralizing immune responses that correlate with protective immunity against Zika virus in mice
    • Yang, M., Sun, H., Lai, H., Hurtado, J. and Chen, Q. (2017b) Plant-produced Zika virus envelope protein elicits neutralizing immune responses that correlate with protective immunity against Zika virus in mice. Plant Biotechnol. J. 16, 572–580.
    • (2017) Plant Biotechnol. J. , vol.16 , pp. 572-580
    • Yang, M.1    Sun, H.2    Lai, H.3    Hurtado, J.4    Chen, Q.5
  • 176
    • 78349295260 scopus 로고    scopus 로고
    • Strategies for the plant-based expression of dengue subunit vaccines
    • Yap, Y.K. and Smith, D.R. (2010) Strategies for the plant-based expression of dengue subunit vaccines. Biotechnol. Appl. Biochem. 57, 47–53.
    • (2010) Biotechnol. Appl. Biochem. , vol.57 , pp. 47-53
    • Yap, Y.K.1    Smith, D.R.2
  • 177
    • 84880258930 scopus 로고    scopus 로고
    • Virus-induced humoral immunity: on how B cell responses are initiated
    • Zabel, F., Kundig, T.M. and Bachmann, M.F. (2013) Virus-induced humoral immunity: on how B cell responses are initiated. Curr. Opin. Virol. 3, 357–362.
    • (2013) Curr. Opin. Virol. , vol.3 , pp. 357-362
    • Zabel, F.1    Kundig, T.M.2    Bachmann, M.F.3
  • 178
    • 0032513212 scopus 로고    scopus 로고
    • Enhanced catalysis of ribonuclease B folding by the interaction of calnexin or calreticulin with ERp57
    • Zapun, A., Darby, N.J., Tessier, D.C., Michalak, M., Bergeron, J.J. and Thomas, D.Y. (1998) Enhanced catalysis of ribonuclease B folding by the interaction of calnexin or calreticulin with ERp57. J. Biol. Chem. 273, 6009–6012.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6009-6012
    • Zapun, A.1    Darby, N.J.2    Tessier, D.C.3    Michalak, M.4    Bergeron, J.J.5    Thomas, D.Y.6
  • 180
    • 3042561793 scopus 로고    scopus 로고
    • Generation of the transgenic potato expressing full-length spike protein of infectious bronchitis virus
    • Zhou, J.Y., Cheng, L.Q., Zheng, X.J., Wu, J.X., Shang, S.B., Wang, J.Y. and Chen, J.G. (2004) Generation of the transgenic potato expressing full-length spike protein of infectious bronchitis virus. J. Biotechnol. 111, 121–130.
    • (2004) J. Biotechnol. , vol.111 , pp. 121-130
    • Zhou, J.Y.1    Cheng, L.Q.2    Zheng, X.J.3    Wu, J.X.4    Shang, S.B.5    Wang, J.Y.6    Chen, J.G.7
  • 181
    • 84979649691 scopus 로고    scopus 로고
    • Taking forward a ‘One Health’ approach for turning the tide against the Middle East respiratory syndrome coronavirus and other zoonotic pathogens with epidemic potential
    • Zumla, A., Dar, O., Kock, R., Muturi, M., Ntoumi, F., Kaleebu, P., Eusebio, M. et al. (2016) Taking forward a ‘One Health’ approach for turning the tide against the Middle East respiratory syndrome coronavirus and other zoonotic pathogens with epidemic potential. Int. J. Infect. Dis. 47, 5–9.
    • (2016) Int. J. Infect. Dis. , vol.47 , pp. 5-9
    • Zumla, A.1    Dar, O.2    Kock, R.3    Muturi, M.4    Ntoumi, F.5    Kaleebu, P.6    Eusebio, M.7


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