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Volumn 8, Issue 6, 2016, Pages 1035-1044

Discovery of high affinity anti-ricin antibodies by B cell receptor sequencing and by yeast display of combinatorial VH:VL libraries from immunized animals

Author keywords

Antibody repertoire analysis; next generation sequencing; ricin A chain; yeast surface display

Indexed keywords

B LYMPHOCYTE RECEPTOR; RICIN ANTIBODY; SINGLE CHAIN FRAGMENT VARIABLE ANTIBODY; ANTIBODY; LYMPHOCYTE ANTIGEN RECEPTOR; MESSENGER RNA; NANOBODY; RICIN;

EID: 84976329717     PISSN: 19420862     EISSN: 19420870     Source Type: Journal    
DOI: 10.1080/19420862.2016.1190059     Document Type: Article
Times cited : (27)

References (44)
  • 1
    • 0028098025 scopus 로고
    • Ricin: structure, mode of action, and some current applications
    • 8119491
    • J.M.Lord, L.M.Roberts, J.D.Robertus. Ricin: structure, mode of action, and some current applications. J Fed Am Societies Exp Biol 1994; 8:201-8; PMID:8119491.
    • (1994) J Fed Am Societies Exp Biol , vol.8 , pp. 201-208
    • Lord, J.M.1    Roberts, L.M.2    Robertus, J.D.3
  • 2
    • 27744564219 scopus 로고    scopus 로고
    • Ricin Poisoning A Comprehensive Review
    • 16278363
    • J.Audi, M.Belson, M.Patel, J.Schier, J.Osterloh. Ricin Poisoning A Comprehensive Review. J Am Med Assoc 2005; 294:2342-51; PMID:16278363; doi 10.1001/jama.294.18.2342
    • (2005) J Am Med Assoc , vol.294 , pp. 2342-2351
    • Audi, J.1    Belson, M.2    Patel, M.3    Schier, J.4    Osterloh, J.5
  • 3
    • 0018780341 scopus 로고
    • Ricin-a potent homicidal poison
    • 421122
    • B.Knight. Ricin-a potent homicidal poison. Br Med J 1979; 1:350-1; PMID:421122
    • (1979) Br Med J , vol.1 , pp. 350-351
    • Knight, B.1
  • 4
    • 0037452278 scopus 로고    scopus 로고
    • UK doctors warned after ricin poison found in police raid
    • 12531838
    • S.Mayor. UK doctors warned after ricin poison found in police raid. Br Med J 2003; 326:126; PMID:12531838; doi 10.1136/bmj.326.7381.126
    • (2003) Br Med J , vol.326 , pp. 126
    • Mayor, S.1
  • 5
    • 2442626550 scopus 로고    scopus 로고
    • Immunological Characteristics Associated with the Protective Efficacy of Antibodies to Ricin
    • 15128810
    • M.Maddaloni, C.Cooke, R.Wilkinson, A.V.Stout, L.Eng, S.H.Pincus. Immunological Characteristics Associated with the Protective Efficacy of Antibodies to Ricin. J Immunol 2004; 172:6221-8; PMID:15128810; doi 10.4049/jimmunol.172.10.6221
    • (2004) J Immunol , vol.172 , pp. 6221-6228
    • Maddaloni, M.1    Cooke, C.2    Wilkinson, R.3    Stout, A.V.4    Eng, L.5    Pincus, S.H.6
  • 6
    • 33646905629 scopus 로고    scopus 로고
    • Immunoglobulin A antibodies against ricin A and B subunits protect epithelial cells from ricin intoxication
    • 16714576
    • N.J.Mantis, C.R.McGuinness, O.Sonuyi, G.Edwards, S.A.Farrant. Immunoglobulin A antibodies against ricin A and B subunits protect epithelial cells from ricin intoxication. Infect Immun 2006; 74:3455-62; PMID:16714576; doi 10.1128/iai.02088-05
    • (2006) Infect Immun , vol.74 , pp. 3455-3462
    • Mantis, N.J.1    McGuinness, C.R.2    Sonuyi, O.3    Edwards, G.4    Farrant, S.A.5
  • 7
    • 73449123743 scopus 로고    scopus 로고
    • A monoclonal immunoglobulin G antibody directed against an immunodominant linear epitope on the ricin A chain confers systemic and mucosal immunity to ricin
    • 16714576
    • L.M.Neal, J.O'Hara, R.N.Brey, N.J.Mantis. A monoclonal immunoglobulin G antibody directed against an immunodominant linear epitope on the ricin A chain confers systemic and mucosal immunity to ricin. Infect Immun 2010; 78:552-61; PMID:16714576; doi 10.1128/iai.02088-05
    • (2010) Infect Immun , vol.78 , pp. 552-561
    • Neal, L.M.1    O'Hara, J.2    Brey, R.N.3    Mantis, N.J.4
  • 9
    • 67849092221 scopus 로고    scopus 로고
    • Isolation of a human-like antibody fragment (scFv) that neutralizes ricin biological activity
    • 19563687
    • T.Pelat, M.Hust, M.Hale, M.-P.Lefranc, S.Dübel, P.Thullier. Isolation of a human-like antibody fragment (scFv) that neutralizes ricin biological activity. BMC Biotechnol 2009; 9:1-13; PMID:19563687; doi 10.1186/1472-6750-9-60
    • (2009) BMC Biotechnol , vol.9 , pp. 1-13
    • Pelat, T.1    Hust, M.2    Hale, M.3    Lefranc, M.-P.4    Dübel, S.5    Thullier, P.6
  • 10
    • 84893831480 scopus 로고    scopus 로고
    • The promise and challenge of high-throughput sequencing of the antibody repertoire
    • 24441474
    • G.Georgiou, G.C.Ippolito, J.Beausang, C.E.Busse, H.Wardemann, S.R.Quake. The promise and challenge of high-throughput sequencing of the antibody repertoire. Nat Biotechnol 2014; 32:158-68; PMID:24441474; doi 10.1038/nbt.2782
    • (2014) Nat Biotechnol , vol.32 , pp. 158-168
    • Georgiou, G.1    Ippolito, G.C.2    Beausang, J.3    Busse, C.E.4    Wardemann, H.5    Quake, S.R.6
  • 11
    • 79952399087 scopus 로고    scopus 로고
    • Beyond natural antibodies: the power of in vitro display technologies
    • 21390033
    • A.R.M.Bradbury, S.Sidhu, S.Dübel, J.McCafferty. Beyond natural antibodies: the power of in vitro display technologies. Nat Biotechnol 2011; 29:245-54; PMID:21390033; doi 10.1038/nbt.1791
    • (2011) Nat Biotechnol , vol.29 , pp. 245-254
    • Bradbury, A.R.M.1    Sidhu, S.2    Dübel, S.3    McCafferty, J.4
  • 12
    • 27144431943 scopus 로고    scopus 로고
    • Selecting and screening recombinant antibody libraries
    • 16151404
    • H.R.Hoogenboom. Selecting and screening recombinant antibody libraries. Nat Biotechnol 2005; 23:1105-16; PMID:16151404; doi 10.1038/nbt1126
    • (2005) Nat Biotechnol , vol.23 , pp. 1105-1116
    • Hoogenboom, H.R.1
  • 13
    • 0037406621 scopus 로고    scopus 로고
    • Isolation and expression of recombinant antibody fragments to the biological warfare pathogen Brucella melitensis
    • 12738372
    • A.Hayhurst, S.Happe, R.Mabry, Z.Koch, B.L.Iverson, G.Georgiou. Isolation and expression of recombinant antibody fragments to the biological warfare pathogen Brucella melitensis. J Immunol Methods 2003; 276:185-96; PMID:12738372; doi 10.1016/s0022-1759(03)00100-5
    • (2003) J Immunol Methods , vol.276 , pp. 185-196
    • Hayhurst, A.1    Happe, S.2    Mabry, R.3    Koch, Z.4    Iverson, B.L.5    Georgiou, G.6
  • 14
    • 13144261717 scopus 로고    scopus 로고
    • Efficient construction of a large nonimmune phage antibody library: the production of high-affinity human single-chain antibodies to protein antigens
    • 9600934
    • M.D.Sheets, P.Amersdorfer, R.Finnern, P.Sargent, E.Lindquist, R.Schier, G.Hemingsen, C.Wong, J.C.Gerhart, J.D.Marks. Efficient construction of a large nonimmune phage antibody library: the production of high-affinity human single-chain antibodies to protein antigens. Proc Natl Acad Sci U S A 1998; 95:6157-62; PMID:9600934; doi 10.1073/pnas.95.11.6157
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 6157-6162
    • Sheets, M.D.1    Amersdorfer, P.2    Finnern, R.3    Sargent, P.4    Lindquist, E.5    Schier, R.6    Hemingsen, G.7    Wong, C.8    Gerhart, J.C.9    Marks, J.D.10
  • 16
    • 0034635335 scopus 로고    scopus 로고
    • Fully synthetic human combinatorial antibody libraries (HuCAL) based on modular consensus frameworks and CDRs randomized with trinucleotides
    • 10656818
    • A.Knappik, L.Ge, A.Honegger, P.Pack, M.Fischer, G.Wellnhofer, A.Hoess, J.Wölle, A.Plückthun, B.Virnekäs. Fully synthetic human combinatorial antibody libraries (HuCAL) based on modular consensus frameworks and CDRs randomized with trinucleotides. J Mol Biol 2000; 296:57-86; PMID:10656818; doi 10.1006/jmbi.1999.3444
    • (2000) J Mol Biol , vol.296 , pp. 57-86
    • Knappik, A.1    Ge, L.2    Honegger, A.3    Pack, P.4    Fischer, M.5    Wellnhofer, G.6    Hoess, A.7    Wölle, J.8    Plückthun, A.9    Virnekäs, B.10
  • 19
    • 0037264969 scopus 로고    scopus 로고
    • Therapeutic Antibodies for Human Diseases at the Dawn of the Twenty-first Century
    • 12509759
    • O.H.Brekke, I.Sandlie. Therapeutic Antibodies for Human Diseases at the Dawn of the Twenty-first Century. Nat Rev Drug Discov 2003; 2:52-62; PMID:12509759; 10.1038/nrd984
    • (2003) Nat Rev Drug Discov , vol.2 , pp. 52-62
    • Brekke, O.H.1    Sandlie, I.2
  • 20
    • 0035793208 scopus 로고    scopus 로고
    • Stability engineering of antibody single-chain Fv fragments
    • 11162109
    • A.Wörn, A.Plückthun. Stability engineering of antibody single-chain Fv fragments. J Mol Biol 2001; 305:989-1010; PMID:11162109; doi 10.1006/jmbi.2000.4265
    • (2001) J Mol Biol , vol.305 , pp. 989-1010
    • Wörn, A.1    Plückthun, A.2
  • 21
    • 84896520964 scopus 로고    scopus 로고
    • High-throughput screening for developability during early-stage antibody discovery using self-interaction nanoparticle spectroscopy
    • 24492294
    • Y.Liu, I.Caffry, J.Wu, S.B.Geng, T.Jain, T.Sun, F.Reid, Y.Cao, P.Estep, Y.Yu, et al. High-throughput screening for developability during early-stage antibody discovery using self-interaction nanoparticle spectroscopy. MAbs 2014; 6:483-92; PMID:24492294; doi 10.4161/mabs.27431
    • (2014) MAbs , vol.6 , pp. 483-492
    • Liu, Y.1    Caffry, I.2    Wu, J.3    Geng, S.B.4    Jain, T.5    Sun, T.6    Reid, F.7    Cao, Y.8    Estep, P.9    Yu, Y.10
  • 22
    • 84885002758 scopus 로고    scopus 로고
    • Addressing polyspecificity of antibodies selected from an in vitro yeast presentation system: A FACS-based, high-throughput selection and analytical tool
    • 24046438
    • Y.Xu, W.Roach, T.Sun, T.Jain, B.Prinz, T.Y.Yu, J.Torrey, J.Thomas, P.Bobrowicz, M.Vásquez, et al. Addressing polyspecificity of antibodies selected from an in vitro yeast presentation system: A FACS-based, high-throughput selection and analytical tool. Protein Eng Des Sel 2013; 26:663-70; PMID:24046438; doi 10.1093/protein/gzt047
    • (2013) Protein Eng Des Sel , vol.26 , pp. 663-670
    • Xu, Y.1    Roach, W.2    Sun, T.3    Jain, T.4    Prinz, B.5    Yu, T.Y.6    Torrey, J.7    Thomas, J.8    Bobrowicz, P.9    Vásquez, M.10
  • 23
    • 84940274148 scopus 로고    scopus 로고
    • Increasing stability of antibody via antibody engineering: Stability engineering on an anti-hVEGF
    • 24916692
    • S.Wang, M.Liu, D.Zeng, W.Qiu, P.Ma, Y.Yu, H.Chang, Z.W.Sun. Increasing stability of antibody via antibody engineering: Stability engineering on an anti-hVEGF. Proteins Struct Funct Bioinforma 2014; 82:2620-30; PMID:24916692; doi 10.1002/prot.24626
    • (2014) Proteins Struct Funct Bioinforma , vol.82 , pp. 2620-2630
    • Wang, S.1    Liu, M.2    Zeng, D.3    Qiu, W.4    Ma, P.5    Yu, Y.6    Chang, H.7    Sun, Z.W.8
  • 24
    • 79957617682 scopus 로고    scopus 로고
    • High affinity, developability and functional size: The holy grail of combinatorial antibody library generation
    • 21540796
    • D.Ponsel, J.Neugebauer, K.Ladetzki-Baehs, K.Tissot. High affinity, developability and functional size: The holy grail of combinatorial antibody library generation. Molecules 2011; 16:3675-700; PMID:21540796; doi 10.3390/molecules16053675
    • (2011) Molecules , vol.16 , pp. 3675-3700
    • Ponsel, D.1    Neugebauer, J.2    Ladetzki-Baehs, K.3    Tissot, K.4
  • 25
    • 84877897559 scopus 로고    scopus 로고
    • A fully synthetic human Fab antibody library based on fixed VH/VL framework pairings with favorable biophysical properties
    • 23571156
    • T.Tiller, I.Schuster, D.Deppe, K.Siegers, R.Strohner, T.Herrmann, M.Berenguer, D.Poujol, J.Stehle, Y.Stark, et al. A fully synthetic human Fab antibody library based on fixed VH/VL framework pairings with favorable biophysical properties. MAbs 2013; 5:445-70; PMID:23571156; doi 10.4161/mabs.24218
    • (2013) MAbs , vol.5 , pp. 445-470
    • Tiller, T.1    Schuster, I.2    Deppe, D.3    Siegers, K.4    Strohner, R.5    Herrmann, T.6    Berenguer, M.7    Poujol, D.8    Stehle, J.9    Stark, Y.10
  • 26
    • 84867000753 scopus 로고    scopus 로고
    • Germline VH/VL pairing in antibodies
    • 22802295
    • N.Jayaram, P.Bhowmick, A.C.R.Martin. Germline VH/VL pairing in antibodies. Protein Eng Des Sel 2012; 25:523-9; PMID:22802295; doi 10.1093/protein/gzs043
    • (2012) Protein Eng Des Sel , vol.25 , pp. 523-529
    • Jayaram, N.1    Bhowmick, P.2    Martin, A.C.R.3
  • 28
    • 84892372545 scopus 로고    scopus 로고
    • Stability engineering of the human antibody repertoire
    • 24291820
    • R.Rouet, D.Lowe, D.Christ. Stability engineering of the human antibody repertoire. FEBS Lett 2014; 588:269-77; PMID:24291820; doi 10.1016/j.febslet.2013.11.029
    • (2014) FEBS Lett , vol.588 , pp. 269-277
    • Rouet, R.1    Lowe, D.2    Christ, D.3
  • 31
    • 84925284996 scopus 로고    scopus 로고
    • In-depth determination and analysis of the human paired heavy- and light-chain antibody repertoire
    • 25501908
    • B.J.DeKosky, T.Kojima, A.Rodin, W.Charab, G.C.Ippolito, A.D.Ellington, G.Georgiou. In-depth determination and analysis of the human paired heavy- and light-chain antibody repertoire. Nat Med 2015; 21:86-91; PMID:25501908; doi 10.1038/nm.3743
    • (2015) Nat Med , vol.21 , pp. 86-91
    • DeKosky, B.J.1    Kojima, T.2    Rodin, A.3    Charab, W.4    Ippolito, G.C.5    Ellington, A.D.6    Georgiou, G.7
  • 35
    • 84866717363 scopus 로고    scopus 로고
    • Rapid production of antigen-specific monoclonal antibodies from a variety of animals
    • 23017270
    • N.Kurosawa, M.Yoshioka, R.Fujimoto, F.Yamagishi, M.Isobe. Rapid production of antigen-specific monoclonal antibodies from a variety of animals. BMC Biol 2012; 10:1-14; PMID:23017270; doi 10.1186/1741-7007-10-80
    • (2012) BMC Biol , vol.10 , pp. 1-14
    • Kurosawa, N.1    Yoshioka, M.2    Fujimoto, R.3    Yamagishi, F.4    Isobe, M.5
  • 36
    • 84866996247 scopus 로고    scopus 로고
    • Antibody isolation from immunized animals: comparison of phage display and antibody discovery via V gene repertoire mining
    • 22988130
    • I.Saggy, Y.Wine, L.Shefet-Carasso, L.Nahary, G.Georgiou, I.Benhar. Antibody isolation from immunized animals: comparison of phage display and antibody discovery via V gene repertoire mining. Protein Eng Des Sel 2012; 25:539-49; PMID:22988130; doi 10.1093/protein/gzs060
    • (2012) Protein Eng Des Sel , vol.25 , pp. 539-549
    • Saggy, I.1    Wine, Y.2    Shefet-Carasso, L.3    Nahary, L.4    Georgiou, G.5    Benhar, I.6
  • 37
    • 34247176809 scopus 로고    scopus 로고
    • Isolating and engineering human antibodies using yeast surface display
    • 17406305
    • G.Chao, W.L.Lau, B.J.Hackel, S.L.Sazinsky, S.M.Lippow, K.D.Wittrup. Isolating and engineering human antibodies using yeast surface display. Nat Protoc 2006; 1:755-68; PMID:17406305; doi 10.1038/nprot.2006.94
    • (2006) Nat Protoc , vol.1 , pp. 755-768
    • Chao, G.1    Lau, W.L.2    Hackel, B.J.3    Sazinsky, S.L.4    Lippow, S.M.5    Wittrup, K.D.6
  • 38
    • 33947155314 scopus 로고    scopus 로고
    • Antigen selection from an HIV-1 immune antibody library displayed on yeast yields many novel antibodies compared to selection from the same library displayed on phage
    • 17242026
    • D.R.Bowley, A.F.Labrijn, M.B.Zwick, D.R.Burton. Antigen selection from an HIV-1 immune antibody library displayed on yeast yields many novel antibodies compared to selection from the same library displayed on phage. Protein Eng Des Sel 2007; 20:81-90; PMID:17242026; doi 10.1093/protein/gzl057
    • (2007) Protein Eng Des Sel , vol.20 , pp. 81-90
    • Bowley, D.R.1    Labrijn, A.F.2    Zwick, M.B.3    Burton, D.R.4
  • 40
    • 84887334370 scopus 로고    scopus 로고
    • IgG variable region and VH CDR3 diversity in unimmunized mice analyzed by massively parallel sequencing
    • 24211535
    • J.Lu, T.Panavas, K.Thys, J.Aerssens, M.Naso, J.Fisher, M.Rycyzyn, R.W.Sweet. IgG variable region and VH CDR3 diversity in unimmunized mice analyzed by massively parallel sequencing. Mol Immunol 2014; 57:274-83; PMID:24211535; doi 10.1016/j.molimm.2013.09.008
    • (2014) Mol Immunol , vol.57 , pp. 274-283
    • Lu, J.1    Panavas, T.2    Thys, K.3    Aerssens, J.4    Naso, M.5    Fisher, J.6    Rycyzyn, M.7    Sweet, R.W.8
  • 41
    • 84883858635 scopus 로고    scopus 로고
    • Comparing CDRH3 diversity captured from secondary lymphoid organs for the generation of recombinant human antibodies
    • 23924800
    • S.Venet, M.Kosco-Vilbois, N.Fischer. Comparing CDRH3 diversity captured from secondary lymphoid organs for the generation of recombinant human antibodies. MAbs 2013; 5:690-8; PMID:23924800; doi 10.4161/mabs.25592
    • (2013) MAbs , vol.5 , pp. 690-698
    • Venet, S.1    Kosco-Vilbois, M.2    Fischer, N.3
  • 42
    • 38449118706 scopus 로고    scopus 로고
    • Exploring the native human antibody repertoire to create antiviral therapeutics
    • 17990793
    • S.K.Dessain, S.P.Adekar, J.D.Berry. Exploring the native human antibody repertoire to create antiviral therapeutics. Curr Top Microbiol Immunol 2008; 317:155-83; PMID:17990793; doi 10.1007/978-3-540-72146-8_6
    • (2008) Curr Top Microbiol Immunol , vol.317 , pp. 155-183
    • Dessain, S.K.1    Adekar, S.P.2    Berry, J.D.3
  • 43
    • 77954656041 scopus 로고    scopus 로고
    • An improved yeast transformation method for the generation of very large human antibody libraries
    • 20130105
    • L.Benatuil, J.M.Perez, J.Belk, C.M.Hsieh. An improved yeast transformation method for the generation of very large human antibody libraries. Protein Eng Des Sel 2010; 23:155-9; PMID:20130105; doi 10.1093/protein/gzq002
    • (2010) Protein Eng Des Sel , vol.23 , pp. 155-159
    • Benatuil, L.1    Perez, J.M.2    Belk, J.3    Hsieh, C.M.4


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