메뉴 건너뛰기




Volumn 84, Issue 6, 2009, Pages 1087-1094

Enhancement of toxin- and virus-neutralizing capacity of single-domain antibody fragments by N-glycosylation

Author keywords

N glycosylation; Nanobody; Neutralization; Recombinant antibody; Yeast

Indexed keywords

ANTIBODY FRAGMENT; DEGLYCOSYLATION; FOOT-AND-MOUTH DISEASE VIRUS; FUSION PROTEINS; GLYCOSYLATED; N-GLYCOSYLATION; N-GLYCOSYLATION SITES; NANOBODY; NEUTRALIZATION; RECOMBINANT ANTIBODY; SACCHAROMYCES CEREVISIAE; SINGLE DOMAINS; SMALL SIZE;

EID: 70349680965     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-009-2029-1     Document Type: Article
Times cited : (32)

References (29)
  • 1
    • 0027489663 scopus 로고
    • Monoclonal immunoglobulin A antibodies directed against cholera toxin prevent the toxin-induced chloride secretory response and block toxin binding to intestinal epithelial cells in vitro
    • 1:CAS:528:DyaK2cXlt1altw%3D%3D
    • FM Apter WI Lencer RA Finkelstein JJ Mekalanos MR Neutra 1993 Monoclonal immunoglobulin A antibodies directed against cholera toxin prevent the toxin-induced chloride secretory response and block toxin binding to intestinal epithelial cells in vitro Infect Immun 61 5271 5278 1:CAS:528: DyaK2cXlt1altw%3D%3D
    • (1993) Infect Immun , vol.61 , pp. 5271-5278
    • Apter, F.M.1    Lencer, W.I.2    Finkelstein, R.A.3    Mekalanos, J.J.4    Neutra, M.R.5
  • 2
    • 0015795679 scopus 로고
    • Gangliosides and membrane receptors for cholera toxin
    • 10.1021/bi00742a032 1:CAS:528:DyaE3sXlt1ansbY%3D
    • P Cuatrecasas 1973 Gangliosides and membrane receptors for cholera toxin Biochemistry 12 3558 3566 10.1021/bi00742a032 1:CAS:528:DyaE3sXlt1ansbY%3D
    • (1973) Biochemistry , vol.12 , pp. 3558-3566
    • Cuatrecasas, P.1
  • 3
    • 0033961580 scopus 로고    scopus 로고
    • Isolation of antigen specific Llama V(HH) antibody fragments and their high level secretion by Saccharomyces cerevisiae
    • DOI 10.1016/S0168-1656(99)00228-X, PII S016816569900228X
    • LGJ Frenken RH van der Linden PW Hermans JW Bos RC Ruuls B de Geus CT Verrips 2000 Isolation of antigen specific llama VHH antibody fragments and their high level secretion by Saccharomyces cerevisiae J Biotechnol 78 11 21 10.1016/S0168-1656(99)00228-X 1:CAS:528:DC%2BD3cXpsFWqtA%3D%3D (Pubitemid 30084786)
    • (2000) Journal of Biotechnology , vol.78 , Issue.1 , pp. 11-21
    • Frenken, L.G.J.1    Van Der Linden, R.H.J.2    Hermans, P.W.J.J.3    Bos, J.W.4    Ruuls, R.C.5    De Geus, B.6    Verrips, C.T.7
  • 4
    • 0025367812 scopus 로고
    • Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: Implications for protein engineering
    • 10.1093/protein/3.5.433 1:CAS:528:DyaK3cXksFCmu78%3D
    • Y Gavel G von Heijne 1990 Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: implications for protein engineering Protein Eng 3 433 442 10.1093/protein/3.5.433 1:CAS:528: DyaK3cXksFCmu78%3D
    • (1990) Protein Eng , vol.3 , pp. 433-442
    • Gavel, Y.1    Von Heijne, G.2
  • 6
    • 36149001292 scopus 로고    scopus 로고
    • Glycosylation engineering in yeast: the advent of fully humanized yeast
    • DOI 10.1016/j.copbio.2007.09.001, PII S0958166907001139, Expression Technologies / Tissue and Cell Engineering
    • SR Hamilton TU Gerngross 2007 Glycosylation engineering in yeast: the advent of fully humanized yeast Curr Opin Biotechnol 18 387 392 10.1016/j.copbio.2007.09.001 1:CAS:528:DC%2BD2sXhtlGhu77F (Pubitemid 350116586)
    • (2007) Current Opinion in Biotechnology , vol.18 , Issue.5 , pp. 387-392
    • Hamilton, S.R.1    Gerngross, T.U.2
  • 7
    • 0034524838 scopus 로고    scopus 로고
    • Llama heavy-chain V regions consist of at least four distinct subfamilies revealing novel sequence features
    • DOI 10.1016/S0161-5890(00)00081-X, PII S016158900000081X
    • MM Harmsen RC Ruuls IJ Nijman TA Niewold LGJ Frenken B de Geus 2000 Llama heavy-chain V regions consist of at least four distinct subfamilies revealing novel sequence features Mol Immunol 37 579 590 10.1016/S0161-5890(00)00081-X 1:CAS:528:DC%2BD3MXitVymsA%3D%3D (Pubitemid 32052527)
    • (2000) Molecular Immunology , vol.37 , Issue.10 , pp. 579-590
    • Harmsen, M.M.1    Ruuls, R.C.2    Nijman, I.J.3    Niewold, T.A.4    Frenken, L.G.J.5    De Geus, B.6
  • 8
    • 0037213327 scopus 로고    scopus 로고
    • Stimulation of chymosin secretion by simultaneous expression with chymosin-binding llama single-domain antibody fragments in yeast
    • 10.1007/s00253-002-1136-z 1:CAS:528:DC%2BD38Xpt1Cju78%3D
    • MM Harmsen CB Smits B de Geus 2002 Stimulation of chymosin secretion by simultaneous expression with chymosin-binding llama single-domain antibody fragments in yeast Appl Microbiol Biotechnol 60 449 454 10.1007/s00253-002-1136- z 1:CAS:528:DC%2BD38Xpt1Cju78%3D
    • (2002) Appl Microbiol Biotechnol , vol.60 , pp. 449-454
    • Harmsen, M.M.1    Smits, C.B.2    De Geus, B.3
  • 9
    • 24144458917 scopus 로고    scopus 로고
    • Prolonged in vivo residence times of llama single-domain antibody fragments in pigs by binding to porcine immunoglobulins
    • DOI 10.1016/j.vaccine.2005.05.017, PII S0264410X05005372
    • MM Harmsen CB Van Solt HPD Fijten MC Van Setten 2005a Prolonged in vivo residence times of llama single-domain antibody fragments in pigs by binding to porcine immunoglobulins Vaccine 23 4926 4934 10.1016/j.vaccine.2005.05.017 1:CAS:528:DC%2BD2MXpvV2qsLc%3D (Pubitemid 41242869)
    • (2005) Vaccine , vol.23 , Issue.41 , pp. 4926-4934
    • Harmsen, M.M.1    Van Solt, C.B.2    Fijten, H.P.D.3    Van Setten, M.C.4
  • 10
    • 27644445089 scopus 로고    scopus 로고
    • Escherichia coli F4 fimbriae specific llama single-domain antibody fragments effectively inhibit bacterial adhesion in vitro but poorly protect against diarrhoea
    • DOI 10.1016/j.vetmic.2005.09.005, PII S0378113505003068
    • MM Harmsen CB van Solt A Hoogendoorn FG van Zijderveld TA Niewold J van der Meulen 2005b Escherichia coli F4 fimbriae specific llama single-domain antibody fragments effectively inhibit bacterial adhesion in vitro but poorly protect against diarrhoea Vet Microbiol 111 89 98 10.1016/j.vetmic.2005.09.005 1:CAS:528:DC%2BD2MXhtFyksLbF (Pubitemid 41578945)
    • (2005) Veterinary Microbiology , vol.111 , Issue.1-2 , pp. 89-98
    • Harmsen, M.M.1    Van Solt, C.B.2    Hoogendoorn, A.3    Van Zijderveld, F.G.4    Niewold, T.A.5    Van Der Meulen, J.6
  • 11
    • 35348819390 scopus 로고    scopus 로고
    • Properties, production, and applications of camelid single-domain antibody fragments
    • DOI 10.1007/s00253-007-1142-2
    • MM Harmsen HJ De Haard 2007 Properties, production, and applications of camelid single-domain antibody fragments Appl Microbiol Biotechnol 77 13 22 10.1007/s00253-007-1142-2 1:CAS:528:DC%2BD2sXhtFGgs7bO (Pubitemid 47573319)
    • (2007) Applied Microbiology and Biotechnology , vol.77 , Issue.1 , pp. 13-22
    • Harmsen, M.M.1    De Haard, H.J.2
  • 13
    • 0019448149 scopus 로고
    • Actions of cholera toxin and the prevention and treatment of cholera
    • DOI 10.1038/292413a0
    • J Holmgren 1981 Actions of cholera toxin and the prevention and treatment of cholera Nature 292 413 417 10.1038/292413a0 1:CAS:528:DyaL38XhsVWj (Pubitemid 11013851)
    • (1981) Nature , vol.292 , Issue.5822 , pp. 413-417
    • Holmgren, J.1
  • 14
    • 0032321747 scopus 로고    scopus 로고
    • Protein N-glycosylation: Molecular genetics and functional significance
    • 10.1177/10454411980090040301 1:CAS:528:DyaK1cXnslSqtbw%3D
    • MA Kukuruzinska K Lennon 1998 Protein N-glycosylation: molecular genetics and functional significance Crit Rev Oral Biol Med 9 415 448 10.1177/10454411980090040301 1:CAS:528:DyaK1cXnslSqtbw%3D
    • (1998) Crit Rev Oral Biol Med , vol.9 , pp. 415-448
    • Kukuruzinska, M.A.1    Lennon, K.2
  • 15
    • 1642369951 scopus 로고    scopus 로고
    • IMGT, the International ImMunoGeneTics Information System
    • 1:CAS:528:DC%2BD2cXos1Kntw%3D%3D http://imgt.cines.fr
    • MP Lefranc 2004 IMGT, The International ImMunoGeneTics Information System Methods Mol Biol 248 27 49 1:CAS:528:DC%2BD2cXos1Kntw%3D%3D http://imgt.cines.fr
    • (2004) Methods Mol Biol , vol.248 , pp. 27-49
    • Lefranc, M.P.1
  • 16
    • 33745490264 scopus 로고    scopus 로고
    • Functional and structural aspects of the interaction of foot-and-mouth disease virus with antibodies
    • F. Sobrino E. Domingo (eds). Horizon Norfolk
    • Mateu MG, Verdaguer N (2004) Functional and structural aspects of the interaction of foot-and-mouth disease virus with antibodies. In: Sobrino F, Domingo E (eds) Foot and mouth disease. Current perspectives. Horizon, Norfolk, pp 222-260
    • (2004) Foot and Mouth Disease. Current Perspectives , pp. 222-260
    • Mateu, M.G.1    Verdaguer, N.2
  • 17
    • 0001890686 scopus 로고    scopus 로고
    • Construction and screening of antibody display libraries
    • B.K. Kay J. Winter J. McCafferty (eds). Academic San Diego. 10.1016/B978-012402380-2/50008-3
    • McCafferty J, Johnson KS (1996) Construction and screening of antibody display libraries. In: Kay BK, Winter J, McCafferty J (eds) Phage display of peptides and proteins. Academic, San Diego, pp 79-111
    • (1996) Phage Display of Peptides and Proteins , pp. 79-111
    • McCafferty, J.1    Johnson, K.S.2
  • 18
    • 0035312546 scopus 로고    scopus 로고
    • Recognition of antigens by single-domain antibody fragments: The superfluous luxury of paired domains
    • DOI 10.1016/S0968-0004(01)01790-X, PII S096800040101790X
    • S Muyldermans C Cambillau L Wyns 2001 Recognition of antigens by single-domain antibody fragments: the superfluous luxury of paired domains Trends Biochem Sci 26 230 235 10.1016/S0968-0004(01)01790-X 1:CAS:528: DC%2BD3MXisF2nt7c%3D (Pubitemid 32289241)
    • (2001) Trends in Biochemical Sciences , vol.26 , Issue.4 , pp. 230-235
    • Muyldermans, S.1    Cambillau, C.2    Wyns, L.3
  • 19
    • 0035222608 scopus 로고    scopus 로고
    • The antiviral activity of antibodies in vitro and in vivo
    • DOI 10.1016/S0065-2776(01)77018-6
    • PW Parren DR Burton 2001 The antiviral activity of antibodies in vitro and in vivo Adv Immunol 77 195 262 10.1016/S0065-2776(01)77018-6 1:CAS:528:DC%2BD3MXivFCntro%3D (Pubitemid 33703707)
    • (2001) Advances in Immunology , vol.77 , pp. 195-262
    • Parren, P.W.H.I.1    Burton, D.R.2
  • 20
    • 54849403487 scopus 로고    scopus 로고
    • Single-domain antibodies as building blocks for novel therapeutics
    • 10.1016/j.coph.2008.07.006
    • D Saerens GH Ghassabeh S Muyldermans 2008 Single-domain antibodies as building blocks for novel therapeutics Curr Opin Pharmacol 8 1 9 10.1016/j.coph.2008.07.006
    • (2008) Curr Opin Pharmacol , vol.8 , pp. 1-9
    • Saerens, D.1    Ghassabeh, G.H.2    Muyldermans, S.3
  • 22
    • 25444435396 scopus 로고    scopus 로고
    • Glycoengineering: The effect of glycosylation on the properties of therapeutic proteins
    • DOI 10.1002/jps.20319
    • AM Sinclair S Elliott 2005 Glycoengineering: the effect of glycosylation on the properties of therapeutic proteins J Pharm Sci 94 1626 1635 10.1002/jps.20319 1:CAS:528:DC%2BD2MXnvVWnurg%3D (Pubitemid 41360859)
    • (2005) Journal of Pharmaceutical Sciences , vol.94 , Issue.8 , pp. 1626-1635
    • Sinclair, A.M.1    Elliott, S.2
  • 23
    • 0026598947 scopus 로고
    • Lactose binding to heat-labile enterotoxin revealed by X-ray crystallography
    • 10.1038/355561a0 1:CAS:528:DyaK38Xht1ejsr0%3D
    • TK Sixma SE Pronk KH Kalk BA van Zanten AM Berghuis WG Hol 1992 Lactose binding to heat-labile enterotoxin revealed by X-ray crystallography Nature 355 561 564 10.1038/355561a0 1:CAS:528:DyaK38Xht1ejsr0%3D
    • (1992) Nature , vol.355 , pp. 561-564
    • Sixma, T.K.1    Pronk, S.E.2    Kalk, K.H.3    Van Zanten, B.A.4    Berghuis, A.M.5    Hol, W.G.6
  • 24
    • 0026458260 scopus 로고
    • Structure and function of cholera toxin and the related Escherichia coli heat-labile enterotoxin
    • 1:CAS:528:DyaK3sXnsVygug%3D%3D
    • BD Spangler 1992 Structure and function of cholera toxin and the related Escherichia coli heat-labile enterotoxin Microbiol Rev 56 622 647 1:CAS:528:DyaK3sXnsVygug%3D%3D
    • (1992) Microbiol Rev , vol.56 , pp. 622-647
    • Spangler, B.D.1
  • 25
    • 0017656173 scopus 로고
    • Assay of Escherichia coli heat-labile enterotoxin with Vero cells
    • 1:STN:280:DyaE2s7os12ktg%3D%3D
    • JI Speirs S Stavric J Konowalchuk 1977 Assay of Escherichia coli heat-labile enterotoxin with Vero cells Infect Immun 16 617 622 1:STN:280:DyaE2s7os12ktg%3D%3D
    • (1977) Infect Immun , vol.16 , pp. 617-622
    • Speirs, J.I.1    Stavric, S.2    Konowalchuk, J.3
  • 26
    • 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
    • 10.1111/j.1467-7652.2008.00330.x 1:CAS:528:DC%2BD1cXlvFegsLw%3D
    • R Strasser J Stadlmann M Schahs G Stiegler H Quendler L Mach J Glossl K Weterings, 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 10.1111/j.1467-7652.2008.00330.x 1:CAS:528:DC%2BD1cXlvFegsLw%3D
    • (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    Weterings, K.8
  • 29
    • 0028169439 scopus 로고
    • Effect of altered C(H)2-associated carbohydrate structure on the functional properties and in vivo fate of chimeric mouse-human immunoglobulin G1
    • DOI 10.1084/jem.180.3.1087
    • A Wright SL Morrison 1994 Effect of altered CH2-associated carbohydrate structure on the functional properties and in vivo fate of chimeric mouse-human immunoglobulin G1 J Exp Med 180 1087 1096 10.1084/jem.180.3.1087 1:CAS:528:DyaK2cXlsFGhtr8%3D (Pubitemid 24256621)
    • (1994) Journal of Experimental Medicine , vol.180 , Issue.3 , pp. 1087-1096
    • Wright, A.1    Morrison, S.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.