메뉴 건너뛰기




Volumn 9, Issue 4, 2014, Pages 493-500

The human anti-HIV antibodies 2F5, 2G12, and PG9 differ in their susceptibility to proteolytic degradation: Down-regulation of endogenous serine and cysteine proteinase activities could improve antibody production in plant-based expression platforms

Author keywords

Antibodies; Biopharmaceutical; Nicotiana; Protein stability; Proteinase

Indexed keywords

AMINO ACIDS; DEGRADATION; DISEASES; PLANTS (BOTANY);

EID: 84897105776     PISSN: 18606768     EISSN: 18607314     Source Type: Journal    
DOI: 10.1002/biot.201300207     Document Type: Article
Times cited : (58)

References (37)
  • 1
    • 84877999567 scopus 로고    scopus 로고
    • Green factories for biopharmaceuticals.
    • Melnik, S., Stöger, E., Green factories for biopharmaceuticals. Curr. Med. Chem. 2013, 20, 1038-1046.
    • (2013) Curr. Med. Chem. , vol.20 , pp. 1038-1046
    • Melnik, S.1    Stöger, E.2
  • 2
    • 77953999126 scopus 로고    scopus 로고
    • Production of antibodies in plants: Status after twenty years.
    • de Muynck, B., Navarre, C., Boutry, M., Production of antibodies in plants: Status after twenty years. Plant Biotechnol. J. 2010, 8, 529-563.
    • (2010) Plant Biotechnol. J. , vol.8 , pp. 529-563
    • de Muynck, B.1    Navarre, C.2    Boutry, M.3
  • 3
    • 24944498904 scopus 로고    scopus 로고
    • Systemic Agrobacterium tumefaciens-mediated transfection of viral replicons for efficient transient expression in plants.
    • Marillonnet, S., Thoeringer, C., Kandzia, R., Klimyuk, V. et al., Systemic Agrobacterium tumefaciens-mediated transfection of viral replicons for efficient transient expression in plants. Nat. Biotechnol. 2005, 23, 718-723.
    • (2005) Nat. Biotechnol. , vol.23 , pp. 718-723
    • Marillonnet, S.1    Thoeringer, C.2    Kandzia, R.3    Klimyuk, V.4
  • 4
    • 77950383145 scopus 로고    scopus 로고
    • Rapid, high-yield production in plants of individualized idiotype vaccines for non-Hodgkin's lymphoma.
    • Bendandi, M., Marillonnet, S., Kandzia, R., Thieme, F. et al., Rapid, high-yield production in plants of individualized idiotype vaccines for non-Hodgkin's lymphoma. Ann. Oncol. 2010, 21, 2420-2427.
    • (2010) Ann. Oncol. , vol.21 , pp. 2420-2427
    • Bendandi, M.1    Marillonnet, S.2    Kandzia, R.3    Thieme, F.4
  • 5
    • 33747141725 scopus 로고    scopus 로고
    • Foreign protein degradation and instability in plants and plant tissue cultures.
    • Doran, P. M., Foreign protein degradation and instability in plants and plant tissue cultures. Trends Biotechnol. 2006, 24, 426-432.
    • (2006) Trends Biotechnol. , vol.24 , pp. 426-432
    • Doran, P.M.1
  • 6
    • 49349107658 scopus 로고    scopus 로고
    • Preventing unintended proteolysis in plant protein biofactories.
    • Benchabane, M., Goulet, C., Rivard, D., Faye, L. et al., Preventing unintended proteolysis in plant protein biofactories. Plant Biotechnol. J. 2008, 6, 633-648.
    • (2008) Plant Biotechnol. J. , vol.6 , pp. 633-648
    • Benchabane, M.1    Goulet, C.2    Rivard, D.3    Faye, L.4
  • 7
    • 33747144853 scopus 로고    scopus 로고
    • Cosecretion of protease inhibitor stabilizes antibodies produced by plant roots.
    • Komarnytsky, S., Borisjuk, N., Yakoby, N., Garvey, A. et al., Cosecretion of protease inhibitor stabilizes antibodies produced by plant roots. Plant Physiol. 2006, 141, 1185-1193.
    • (2006) Plant Physiol. , vol.141 , pp. 1185-1193
    • Komarnytsky, S.1    Borisjuk, N.2    Yakoby, N.3    Garvey, A.4
  • 8
    • 33645503258 scopus 로고    scopus 로고
    • An in-built proteinase inhibitor system for the protection of recombinant proteins recovered from transgenic plants.
    • Rivard, D., Anguenot, R., Brunelle, F., Le, V. Q. et al., An in-built proteinase inhibitor system for the protection of recombinant proteins recovered from transgenic plants. Plant Biotechnol. J. 2006, 4, 359-368.
    • (2006) Plant Biotechnol. J. , vol.4 , pp. 359-368
    • Rivard, D.1    Anguenot, R.2    Brunelle, F.3    Le, V.Q.4
  • 9
    • 50249165829 scopus 로고    scopus 로고
    • Improvement of recombinant hGM-CSF production by suppression of cysteine proteinase gene expression using RNA interference in a transgenic rice culture.
    • Kim, N.-S., Kim, T.-G., Kim, O.-H., Ko, E.-M. et al., Improvement of recombinant hGM-CSF production by suppression of cysteine proteinase gene expression using RNA interference in a transgenic rice culture. Plant Mol. Biol. 2008, 68, 263-275.
    • (2008) Plant Mol. Biol. , vol.68 , pp. 263-275
    • Kim, N.-S.1    Kim, T.-G.2    Kim, O.-H.3    Ko, E.-M.4
  • 10
    • 46049101277 scopus 로고    scopus 로고
    • Identification of peptidases in Nicotiana tabacum leaf intercellular fluid.
    • Delannoy, M., Alves, G., Vertommen, D., Ma, J. et al., Identification of peptidases in Nicotiana tabacum leaf intercellular fluid. Proteomics 2008, 8, 2285-2298.
    • (2008) Proteomics , vol.8 , pp. 2285-2298
    • Delannoy, M.1    Alves, G.2    Vertommen, D.3    Ma, J.4
  • 11
    • 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. et al., A protease activity-depleted environment for heterologous proteins migrating towards the leaf cell apoplast. Plant Biotechnol. J. 2012, 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
  • 12
    • 67349263591 scopus 로고    scopus 로고
    • Different subcellular localization and glycosylation for a functional antibody expressed in Nicotiana tabacum plants and suspension cells.
    • de Muynck, B., Navarre, C., Nizet, Y., Stadlmann, J. et al., Different subcellular localization and glycosylation for a functional antibody expressed in Nicotiana tabacum plants and suspension cells. Transgenic Res. 2009, 18, 467-482.
    • (2009) Transgenic Res. , vol.18 , pp. 467-482
    • de Muynck, B.1    Navarre, C.2    Nizet, Y.3    Stadlmann, J.4
  • 13
    • 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. et al., Human monoclonal antibody 2G12 defines a distinctive neutralization epitope on the gp120 glycoprotein of human immunodeficiency virus type 1. J. Virol. 1996, 70, 1100-1108.
    • (1996) J. Virol. , vol.70 , pp. 1100-1108
    • Trkola, A.1    Purtscher, M.2    Muster, T.3    Ballaun, C.4
  • 14
    • 0032167410 scopus 로고    scopus 로고
    • Molecular characterization of five neutralizing anti-HIV type 1 antibodies: Identification of nonconventional D segments in the human monoclonal antibodies 2G12 and 2F5.
    • Kunert, R., Rüker, F., Katinger, H., Molecular characterization of five neutralizing anti-HIV type 1 antibodies: Identification of nonconventional D segments in the human monoclonal antibodies 2G12 and 2F5. AIDS Res. Hum. Retroviruses 1998, 14, 1115-1128.
    • (1998) AIDS Res. Hum. Retroviruses , vol.14 , pp. 1115-1128
    • Kunert, R.1    Rüker, F.2    Katinger, H.3
  • 15
    • 70349887757 scopus 로고    scopus 로고
    • Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target.
    • Walker, L. M., Phogat, S. K., Chan-Hui, P. Y., Wagner, D. et al., Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target. Science 2009, 326, 285-289.
    • (2009) Science , vol.326 , pp. 285-289
    • Walker, L.M.1    Phogat, S.K.2    Chan-Hui, P.Y.3    Wagner, D.4
  • 16
    • 34249823666 scopus 로고    scopus 로고
    • Functional analysis of the broadly neutralizing human anti-HIV-1 antibody 2F5 produced in transgenic BY-2 suspension cultures.
    • Sack, M., Paetz, A., Kunert, R., Bomble, M. et al., Functional analysis of the broadly neutralizing human anti-HIV-1 antibody 2F5 produced in transgenic BY-2 suspension cultures. FASEB J. 2007, 21, 1655-1664.
    • (2007) FASEB J. , vol.21 , pp. 1655-1664
    • Sack, M.1    Paetz, A.2    Kunert, R.3    Bomble, M.4
  • 17
    • 34547568959 scopus 로고    scopus 로고
    • Production of a monoclonal antibody in plants with a humanized N-glycosylation pattern.
    • Schähs, M., Strasser, R., Stadlmann, J., Kunert, R. et al., Production of a monoclonal antibody in plants with a humanized N-glycosylation pattern. Plant Biotechnol. J. 2007, 5, 657-663.
    • (2007) Plant Biotechnol. J. , vol.5 , pp. 657-663
    • Schähs, M.1    Strasser, R.2    Stadlmann, J.3    Kunert, R.4
  • 18
    • 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., Schähs, M., Stiegler, G. et al., Generation of glyco-engineered Nicotiana benthamiana for the production of monoclonal antibodies with a homogeneous human-like N-glycan structure. Plant Biotechnol. J. 2008, 6, 392-402.
    • (2008) Plant Biotechnol. J. , vol.6 , pp. 392-402
    • Strasser, R.1    Stadlmann, J.2    Schähs, M.3    Stiegler, G.4
  • 19
    • 0028237920 scopus 로고
    • Maturation of human procathepsin B. Proenzyme activation and proteolytic processing of the precursor to the mature proteinase, in vitro, are primarily unimolecular processes.
    • Mach, L., Mort, J. S., Glössl, J., Maturation of human procathepsin B. Proenzyme activation and proteolytic processing of the precursor to the mature proteinase, in vitro, are primarily unimolecular processes. J. Biol. Chem. 1994, 269, 13030-13035.
    • (1994) J. Biol. Chem. , vol.269 , pp. 13030-13035
    • Mach, L.1    Mort, J.S.2    Glössl, J.3
  • 20
    • 84868119552 scopus 로고    scopus 로고
    • Structural basis for the recognition and cleavage of histone H3 by cathepsin L.
    • Adams-Cioaba, M. A., Krupa, J. C., Xu, C., Mort, J. S. et al., Structural basis for the recognition and cleavage of histone H3 by cathepsin L. Nat. Commun. 2011, 2, 197.
    • (2011) Nat. Commun. , vol.2 , pp. 197
    • Adams-Cioaba, M.A.1    Krupa, J.C.2    Xu, C.3    Mort, J.S.4
  • 21
    • 84879731123 scopus 로고    scopus 로고
    • Mechanistic and structural studies on legumain explain its zymogenicity, distinct activation pathways, and regulation.
    • Dall, E., Brandstetter, H., Mechanistic and structural studies on legumain explain its zymogenicity, distinct activation pathways, and regulation. Proc. Natl. Acad. Sci. USA 2013, 110, 10940-10945.
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 10940-10945
    • Dall, E.1    Brandstetter, H.2
  • 22
    • 0026664252 scopus 로고
    • Rat procathepsin B. Proteolytic processing to the mature form in vitro.
    • Rowan, A. D., Mason, P., Mach, L., Mort, J. S., Rat procathepsin B. Proteolytic processing to the mature form in vitro. J. Biol. Chem. 1992, 267, 15993-15999.
    • (1992) J. Biol. Chem. , vol.267 , pp. 15993-15999
    • Rowan, A.D.1    Mason, P.2    Mach, L.3    Mort, J.S.4
  • 23
    • 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., Altmann, F., Glycan profiles of the 27 N-glycosylation sites of the HIV envelope protein CN54gp140. Biol. Chem. 2012, 393, 719-730.
    • (2012) Biol. Chem. , vol.393 , pp. 719-730
    • Pabst, M.1    Chang, M.2    Stadlmann, J.3    Altmann, F.4
  • 24
    • 41649113980 scopus 로고    scopus 로고
    • Cost-effective production of a vaginal protein microbicide to prevent HIV transmission.
    • Ramessar, K., Rademacher, T., Sack, M., Stadlmann, J. et al., Cost-effective production of a vaginal protein microbicide to prevent HIV transmission. Proc. Natl. Acad. Sci. USA 2008, 105, 3727-3732.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 3727-3732
    • Ramessar, K.1    Rademacher, T.2    Sack, M.3    Stadlmann, J.4
  • 25
    • 84855165591 scopus 로고    scopus 로고
    • Antibody degradation in tobacco plants: A predominantly apoplastic process.
    • Hehle, V. K., Paul, M. J., Drake, P. M., Ma, J. K.-C. et al., Antibody degradation in tobacco plants: A predominantly apoplastic process. BMC Biotechnol. 2011, 11, 128.
    • (2011) BMC Biotechnol. , vol.11 , pp. 128
    • Hehle, V.K.1    Paul, M.J.2    Drake, P.M.3    Ma, J.K.-C.4
  • 26
    • 33747599863 scopus 로고    scopus 로고
    • A KDEL-tagged monoclonal antibody is efficiently retained in the endoplasmic reticulum in leaves, but is both partially secreted and sorted to protein storage vacuoles in seeds.
    • Petruccelli, S., Otegui, M. S., Lareu, F., Tran Dinh, O. et al., A KDEL-tagged monoclonal antibody is efficiently retained in the endoplasmic reticulum in leaves, but is both partially secreted and sorted to protein storage vacuoles in seeds. Plant Biotechnol. J. 2006, 4, 511-527.
    • (2006) Plant Biotechnol. J. , vol.4 , pp. 511-527
    • Petruccelli, S.1    Otegui, M.S.2    Lareu, F.3    Tran Dinh, O.4
  • 27
    • 0034599410 scopus 로고    scopus 로고
    • Papain digestion of different mouse IgG subclasses as studied by electrospray mass spectrometry.
    • Adamczyk, M., Gebler, J. C., Wu, J., Papain digestion of different mouse IgG subclasses as studied by electrospray mass spectrometry. J. Immunol. Methods 2000, 237, 95-104.
    • (2000) J. Immunol. Methods , vol.237 , pp. 95-104
    • Adamczyk, M.1    Gebler, J.C.2    Wu, J.3
  • 28
    • 0025214927 scopus 로고
    • Interactions of papaya proteinase IV with inhibitors.
    • Buttle, D. J., Ritonja, A., Dando, P. M., Abrahamson, M. et al., Interactions of papaya proteinase IV with inhibitors. FEBS Lett. 1990, 262, 58-60.
    • (1990) FEBS Lett. , vol.262 , pp. 58-60
    • Buttle, D.J.1    Ritonja, A.2    Dando, P.M.3    Abrahamson, M.4
  • 29
    • 34548040973 scopus 로고    scopus 로고
    • Analysis of post-translational modifications in recombinant monoclonal antibody IgG1 by reversed-phase liquid chromatography/mass spectrometry.
    • Yan, B., Valliere-Douglass, J., Brady, L., Steen, S. et al., Analysis of post-translational modifications in recombinant monoclonal antibody IgG1 by reversed-phase liquid chromatography/mass spectrometry. J. Chromatogr. A 2007, 1164, 153-161.
    • (2007) J. Chromatogr. A , vol.1164 , pp. 153-161
    • Yan, B.1    Valliere-Douglass, J.2    Brady, L.3    Steen, S.4
  • 30
    • 77956630367 scopus 로고    scopus 로고
    • Plant-produced trastuzumab inhibits the growth of HER2 positive cancer cells.
    • Grohs, B. M., Niu, Y., Veldhuis, L. J., Trabelsi, S. et al., Plant-produced trastuzumab inhibits the growth of HER2 positive cancer cells. J. Agric. Food Chem. 2010, 58, 10056-10063.
    • (2010) J. Agric. Food Chem. , vol.58 , pp. 10056-10063
    • Grohs, B.M.1    Niu, Y.2    Veldhuis, L.J.3    Trabelsi, S.4
  • 31
    • 78149470963 scopus 로고    scopus 로고
    • Optimisation of the purification process of a tumour-targeting antibody produced in N. benthamiana using vacuum-agroinfiltration.
    • Lombardi, R., Villani, M. E., Di Carli, M., Brunetti, P. et al., Optimisation of the purification process of a tumour-targeting antibody produced in N. benthamiana using vacuum-agroinfiltration. Transgenic Res. 2010, 19, 1083-1097.
    • (2010) Transgenic Res. , vol.19 , pp. 1083-1097
    • Lombardi, R.1    Villani, M.E.2    Di Carli, M.3    Brunetti, P.4
  • 32
    • 84865978982 scopus 로고    scopus 로고
    • Production of different glycosylation variants of the tumour-targeting mAb H10 in N. benthamiana: Influence on expression yield and antibody degradation.
    • Lombardi, R., Donini, M., Villani, M. E., Brunetti, P. et al., Production of different glycosylation variants of the tumour-targeting mAb H10 in N. benthamiana: Influence on expression yield and antibody degradation. Transgenic Res. 2012, 21, 1005-1021.
    • (2012) Transgenic Res. , vol.21 , pp. 1005-1021
    • Lombardi, R.1    Donini, M.2    Villani, M.E.3    Brunetti, P.4
  • 33
    • 57649121662 scopus 로고    scopus 로고
    • Plant pharming of a full-sized, tumour-targeting antibody using different expression strategies.
    • Villani, M. E., Morgun, B., Brunetti, P., Marusic, C. et al., Plant pharming of a full-sized, tumour-targeting antibody using different expression strategies. Plant Biotechnol. J. 2009, 7, 59-72.
    • (2009) Plant Biotechnol. J. , vol.7 , pp. 59-72
    • Villani, M.E.1    Morgun, B.2    Brunetti, P.3    Marusic, C.4
  • 34
    • 12444291017 scopus 로고    scopus 로고
    • Antibody domain exchange is an immunological solution to carbohydrate cluster recognition.
    • Calarese, D. A., Scanlan, C. N., Zwick, M. B., Deechongkit, S. et al., Antibody domain exchange is an immunological solution to carbohydrate cluster recognition. Science 2003, 300, 2065-2071.
    • (2003) Science , vol.300 , pp. 2065-2071
    • Calarese, D.A.1    Scanlan, C.N.2    Zwick, M.B.3    Deechongkit, S.4
  • 35
    • 77957189612 scopus 로고    scopus 로고
    • Antibody 2G12 recognizes di-mannose equivalently in domain- and nondomain-exchanged forms but only binds the HIV-1 glycan shield if domain exchanged.
    • Doores, K. J., Fulton, Z., Huber, M., Wilson, I. A. et al., Antibody 2G12 recognizes di-mannose equivalently in domain- and nondomain-exchanged forms but only binds the HIV-1 glycan shield if domain exchanged. J. Virol. 2010, 84, 10690-10699.
    • (2010) J. Virol. , vol.84 , pp. 10690-10699
    • Doores, K.J.1    Fulton, Z.2    Huber, M.3    Wilson, I.A.4
  • 36
    • 77954912140 scopus 로고    scopus 로고
    • Structure and function of broadly reactive antibody PG16 reveal an H3 subdomain that mediates potent neutralization of HIV-1.
    • Pejchal, R., Walker, L. M., Stanfield, R. L., Phogat, S. K. et al., Structure and function of broadly reactive antibody PG16 reveal an H3 subdomain that mediates potent neutralization of HIV-1. Proc. Natl. Acad. Sci. USA 2010, 107, 11483-11488.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 11483-11488
    • Pejchal, R.1    Walker, L.M.2    Stanfield, R.L.3    Phogat, S.K.4
  • 37
    • 0033829810 scopus 로고    scopus 로고
    • Effect of climate conditions and plant developmental stage on the stability of antibodies expressed in transgenic tobacco.
    • Stevens, L. H., Stoopen, G. M., Elbers, I. J. W., Molthoff, J. W. et al., Effect of climate conditions and plant developmental stage on the stability of antibodies expressed in transgenic tobacco. Plant Physiol. 2000, 124, 173-182.
    • (2000) Plant Physiol. , vol.124 , pp. 173-182
    • Stevens, L.H.1    Stoopen, G.M.2    Elbers, I.J.W.3    Molthoff, J.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.