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Original Article

Medical Applications of Single-Chain Antibodies

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Pages 195-217 | Received 22 Oct 1992, Published online: 10 Jul 2009

References

  • Silverstein A. M. The history of immunology. Fundamental Immunology, Second Edition, W. E. Paul. Raven Press, New York 1989; 21–38
  • Commemorative issue for the 100th anniversary of the discovery of antibodies (1890–1990). Molecular Immunology, R. S. Nezlin, 1991; 28: 1315–1412, 12
  • Porter R. R. The hydrolysis of rabbit γ-globulin and antibodies with crystalline papain. Biochem. J 1959; 73: 119–126
  • Edelman G. M. Dissociation of γ-globulin. J. Am. Chem. Soc 1959; 81: 3155–315
  • Fieischman J. B., Porter R. R., Press E. M. The arrangement of the peptide chains in γ-globulin. Biochem. J 1963; 88: 220–228
  • Immunoglobulin Genes, T. Honjo, F. W. Alt, T. H. Rabbits. Academic Press, New York 1989; 410
  • Kohler G., Milstein C. Continuous cultures of fused cells secreting antibody of predefined specificity. Nature 1975; 245: 495–497
  • Waldmann T. A. Monoclonal antibodies in diagnosis and therapy. Science 1991; 252: 1657–1662
  • Winter G., Milstein C. Man-made antibodies. Nature 1991; 349: 293–299
  • Givol D. The minimal antigen-binding fragment of antibodies—Fv fragment. Molecular Immunology 1991; 28: 1379–1386
  • Huston J. S., Levinson D., Mudgett-Hunter M., Tai M. -S., Novotny J., Margolies M. N., Ridge R. J., Bruccoleri R., Haber E., Crea R., Opperman H. Protein engineering of antibody binding sites: Recovery of specific activity in an anti-digoxin single-chain Fv analogue produced in Escherichia coli. Proc. Nat. Acad. Sci., USA 1988; 85: 5879–5883
  • Huston J. S., Mudgett-Hunter M., Haber E., Oppermann H. Protein engineering of single-chain Fv immunoconjugates. SIM News 1988; 38((4) (Suppl.))11
  • Huston J. S., Mudgett-Hunter M., Haber E., Oppermann H. Engineering immunoconjugates by gene fusion: Recovery of dual activity from a fusion protein comprising variable domains from antibody 26–10 and fragment B of protein A. Abstracts, 219. International Conference on Monoclonal Antibody Immunoconjugates in Cancer, San Diego, CA, 1989
  • Huston J. S., Mudgett-Hunter M., Tai M. -S., Haber E., Oppermann H. Confirmation of binding site fidelity in biosynthetic single-chain Fv and a single-chain Fv immunoconjugate. The Biochemist 1989; 11((2) (Suppl))22
  • McCartney J., Lederman L., Drier E., Wu G. -M., Cabral-Denison N., Huston J. S., Oppermann H. Biosynthetic antibody binding site (BABS) proteins: binding activities of MOPC 315 VH, Fv and single-chain Fv. ICSU Short Reports 1990; 10: 114
  • Shealy D., Nedelman M., Tai M. -S., Huston J. S., Berger H., Lister-James J., Dean R. T. Characterization and biodistribution of Tc-99m labeled single chain antibody Fv fragment. J. Nuclear Med 1990; 31((5) (Suppl.))776–777
  • Tai M. -S., Mudgett-Hunter M., Levinson D., Wu G. -M., Haber E., Oppermann H., Huston J. S. A bifunctional fusion protein containing Fc-binding fragment B of staphylococcal protein A amino terminal to antidigoxin single-chain Fv. Biochemistry 1990; 29: 8024–8030
  • Huston J. S., Tai M. S., McCartney J., Warren F., Mudgett-Hunter M., Oppermann H. Bifunctional single-chain Fv fusion proteins. Bispecific Antibodies and Targeted Cellular Cytotoxicity: Proceedings of the Second International Conference, J.-L. Romet-Lemonne, M. W. Fanger, D. M. Segal. Fondation Nationale de Transfusion Sanguine, Les UlisFrance, 1991: 201–206
  • McCartney J. E., Radcliffe R. D., Alvarez V. L., Rodwell J. D., Pang R. H. L., Warren F., Oppermann H. 1990, Unpublished results
  • Nedelman M. A., Shealy D., Boutin R., Brunt E., Weisman H. F., McCartney J. E., Warren F. D., Oppermann H., Pang R. H. L., Berger H. J. Rapid infarct imaging with a new Tc-99m antimyosin sFv fragment: Evaluation in acute myocardial infarction in dogs. J. Nuclear Med 1991; 32(Suppl.)1005
  • Huston J. S., Tai M. -S., Mudgett-Hunter M., McCartney J., Warren E., Haber E., Oppermann H. Protein engineering of single-chain Fv analogues and fusion proteins. Molecular Design and Modeling: Concepts and Applications, Part B, J. J. Langone. Methods in Enzymology, 1991; 203: 46–88
  • McCartney J., Lederman L., Drier E., Cabral-Denison N., Wu G. -M., Batorsky R., Huston J. S., Oppermann H. Biosynthetic antibody binding sites: Development of a single-chain Fv model based on anti-dinitrophenol IgA myeloma MOPC 315. Journal of Protein Chemistry 1991; 10: 669–683
  • McCartney J. E., Tai M. -S., Oppermann H., Jin D., Warren F. D., Weiner L. M., Bookman M. A., Stafford W. F., III, Houston L. L., Huston J. S. Refolding of single-chain Fv with C-terminal cysteine (sFv'): Formation of disulfide-bonded homodimers of anti-c-erbB-2 and anti-digoxin sFv'. Miami Short Reports 1993; 3: 91
  • Nedelman M. A., Shealy D. J., Boutin R., Brunt E., Seasholtz J. I., Allen I. E., Weisman H. E., McCartney J. E., Warren F. D., Oppermann H., Pang R. H. L., Berger H. J. Rapid infarct imaging with a technetium-99m antimyosin sFv fragment: Evaluation in a canine model of acute myocardial infarction. J. Nuclear Med 1993; 34: 234–241
  • Huston J. S., Tai M. -S., McCartney J., Keck P., Oppermann H. Antigen recognition and targeted delivery by the single-chain Fv. In: Advances in the Applications of Monoclonal Antibodies in Clinical Oncology. Proceedings of the 9th Hammersmith Meeting, A. A. Epenetos. Chapman & Hall, London 1993, In press
  • Huston J. S., Keck R., Tai M. -S., Jin D., McCartney J., Stafford W. E., III, Mudgett-Hunter M., Oppermann H., Haber E. Single-chain immunotechnology of Fv analogues and fusion proteins. Immunotechnology, J. Gosling, D. Reen. Portland Press, London 1993, In press
  • Bird R. E., Hardman K. D., Jacobson J. W., Johnson S., Kaufman B. M., Lee S. -M., Lee T., Pope S. H., Riordan G. S., Whitlow M. Single-chain antigen-binding proteins. Science 1988; 242: 423–426
  • Bedzyk W. D., Weidner K. M., Denzin L. K., Johnson L. S., Hardman K. D., Pantoliano M. W., Ansel E. D., Voss E. W., Jr. Immunological and structural characterization of a high affinity anti-fluorescein single-chain antibody. J. Biol. Chem 1990; 265: 18615–18620
  • Colcher D., Bird R., Roselli M., Hardman K. D., Johnson S., Pope S., Dodd S. W., Pantoliano M. W., Milenic D. E., Schlom J. In vivo tumor targeting of a recombinant single-chain antigen-binding protein. J. Nat. Cancer Inst 1990; 82: 1191–1197
  • Gibbs R. A., Posner B. A., Filpula D. R., Dodd S. W., Finkelman M. A. J., Lee T. K., Wroble M., Whitlow M., Benkovic S. J. Construction and characterization of a single-chain catalytic antibody. Proc. Nat. Acad. Sci., USA 1991; 88: 4001–4004
  • Milenic D. E., Yokota T., Filpula D. R., Finkelman M. A. J., Dodd S. W., Wood J. E., Whitlow M., Snoy R., Schlom J. Construction, binding properties, metabolism, and tumor targeting of a single-chain Fv derived from the pancarcinoma monoclonal antibody CC49. Cancer Research 1991; 51: 6363–6371
  • Pantoliano M. W., Bird R. D., Johnson S., Asel E. D., Dodd S. W., Wood J. E., Hardman K. D. Conformational stability, folding and ligand-binding affinity of single-chain Fv immunoglobulin fragments expressed in Escherichia coli. Biochemistry 1991; 30: 10117–10125
  • Yokota T., Milenic D. E., Whitlow M., Schlom J. Rapid tumor penetration of a single-chain Fv and comparison with other immunoglobulin forms. Cancer Res 1992; 52: 3402–3408
  • Johnson S., Bird R. E. Construction of single-chain Fv derivatives of monoclonal antibodies and their production in Escherichia coli. Methods in Enzymology 1991; 203: 88–98
  • Whitlow M., Filpula D. Single-chain Fv proteins and their fusion proteins. Methods: A Companion to Methods in Enzymology 1991; 2: 97–105
  • Batra J. K., Kasprzyk P. G., Bird R. E., Pastan I., King C. R. Recombinant anti-erbB2 immunotoxins containing Pseudomonas exotoxin. Proc. Nat. Acad. Sci., USA 1992; 89: 5867–5871
  • Chaudhary V. K., Queen C., Junghans R. R., Waldmann T. A., FitzGerald D. J., Pastan I. A recombinant immunotoxin consisting of two antibody variable domains fused to Pseudomonas exotoxin. Nature 1989; 339: 394–397
  • Chaudhary V K., Batra J. K., Gallo M. G., Willingham M. C., FitzGerald D. J., Pastan I. A rapid method of cloning functional variable-region antibody genes in Escherichia coli as single-chain immunotoxins. Proc. Nat. Acad. Sci., USA 1990; 87: 1066–1070
  • Batra J. K., Chaudhary V. K., FitzGerald D., Pastan I. TGFα-anti-Tac(Fv)-PE40: A bifunctional toxin cytotoxic for cells with EGF or IL2 receptors. Biochem. Biophys. Res. Comm 1990; 171: 1–6
  • Batra J. K., FitzGerald D., Gately M., Chaudhary V. K., Pastan I. Anti-Tac(Fv)-PE40, a single chain antibody Pseudomonas fusion protein directed at interleukin 2 receptor bearing cells. J. Biol. Chem 1990; 265: 15198–15202
  • Kreitman R. J., Chaudhary V. K., Waldmann T., Willingham M. C., FitzGerald D. I., Pastan I. The recombinant immunotoxin anti-Tac(Fv)-Pseudomonas exotoxin 40 is cytotoxic toward peripheral blood malignant cells from patients with adult T-cell leukemia. Proc. Nat. Acad. Sci., USA 1990; 87: 8291–8295
  • Chaudhary V K., Gallo M. G., FitzGerald D. J., Pastan I. A recombinant single-chain immunotoxin composed of anti-Tac variable regions and a truncated diphtheria toxin. Proc. Nat. Acad. Sci., USA 1990; 87: 9491–9494
  • Batra J. K., FitzGerald D. J., Chaudhary V. K., Pastan I. Single-chain immunotoxins directed at the human transferrin receptor containing Pseudomonas exotoxin A or diphtheria toxin: Anti-TFR(Fv)-PE40 and DT388-anti-TFR(Fv). Mol. Cell. Biol 1991; 11: 2200–2205
  • Buchner J., Brinkmann U., Pastan I. Renaturation of a single-chain immunotoxin facilitated by chaperones and protein disulfide isomerase. Bio/Technology 1992; 10: 682–685
  • Brinkmann U., Pai L. H., FitzGerald D. J., Willingham M., Pastan I. B3(Fv)-PE38KDEL, a single-chain immunotoxin that causes complete regression of a human carcinoma in mice. Proc. Nat. Acad. Sci., USA 1991; 88: 8616–8620
  • Seetharam S., Chaudhary V. K., FitzGerald D J., Pastan I. Increased cytotoxic activity of Pseudomonas exotoxin and two chimeric toxins ending in KDEL. J. Biol. Chem 1991; 266: 17376–17381
  • Brinkmann U., Buchner J., Pastan I. Independent folding of Pseudomonas exotoxin and single-chain immunotoxins: Influence of interdomain connections. Proc. Nat. Acad. Sci., USA 1992; 89: 3075–3079
  • Buchner J., Brinkmann U., Pastan I. Renaturation of a single-chain immunotoxin facilitated by chaperones and protein disulfide isomerase. Bio/Technology 1992; 10: 682–685
  • Buchner J., Pastan I., Brinkmann U. A method for increasing the yield of properly folded recombinant fusion proteins: Single-chain immunotoxins from renaturation of bacterial inclusion bodies. Anal. Biochem 1992; 205: 263–270
  • Glockshuber R., Malia M., Pfitzinger I., Plückthun A. A comparison of strategies to stabilize immunoglobulin Fv-fragments. Biochemistry 1990; 29: 1362–1367
  • Skerra A., Pfitzinger I., Plückthun A. The functional expression of antibody Fv fragments in Escherichia coll. Improved vectors and a generally applicable purification technique. Bio/Technology 1991; 9: 273–278
  • Glockshuber R., Schmidt T., Plückthun A. The disulfide bonds in antibody variable domains: Effects on stability, folding in vitro, and functional expression in. Escherichia coli. Biochemistry 1992; 31: 1270–1279
  • Pack P., Plückthun A. Miniantibodies: Use of amphipathic helices to produce functional, flexibly linked Fv fragments with high avidity in. Escherichia coli. Biochemistry 1992; 31: 1579–1534
  • McCafferty J., Griffiths A. D., Winter G., Chiswell D. J. Phage antibodies: filamentous phage displaying antibody variable domains. Nature 1990; 348: 552–554
  • Clackson T., Hoogenboom H. R., Griffiths A. D., Winter G. Making antibody fragments using phage display libraries. Nature 1991; 352: 624–628
  • Marks J. D., Hoogenboom H. R., Bonnert T. P., McCafferty J., Griffiths A. D., Winter G. Bypassing immunization: Human antibodies from V-gene libraries displayed on phage. J. Mol. Biol 1991; 222: 581–597
  • Marks J. D., Griffiths A. D., Malmqvist M., Clackson T. R., Bye J. B., Winter G. By-passing immunization: Building high affinity human antibodies by chain shuffling. Bio/Technology 1992; 10: 779–783
  • Marks J. D., Hoogenboom H. R., Griffiths A. D., Winter G. Molecular evolution of proteins on filamentous phage. J. Biol. Chem 1992; 267: 16007–16010
  • Iverson B. L., Iverson S. A., Roberts V. A., Getzoff E. D., Tainer J. A., Benkovic S. J., Lerner R. A. Metalloantibodies. Science 1990; 249: 659–662
  • Roberts V A., Iverson B. L., Iverson S. A., Benkovic S. J., Lerner R. A., Getzoff E. D., Tainer J. A. Antibody remodeling: A general solution to the design of a metal-coordination site in an antibody binding pocket. Proc. Nat. Acad. Sci., USA, 87: 6654–6658
  • Condra J. H., Sardana V. V., Tomassini J. E., Schlabach A. J., Davies M. -E., Lineberger D. W., Gotlib L., Colonno R. J. Bacterial expression of antibody fragments that block human rhinovirus infection of cultured cells. J. Biol. Chem 1990; 265: 2292–2295
  • Davis G. T., Bedzyk W D., Voss E. W., Jacobs T. W. Single-chain antibody (SCA) encoding genes: One-step construction and expression in eukaryotic cells. Bio/Technology 1991; 9: 165–169
  • Laroche Y., Demaeyer M., Stassen J. -M., Gansemans Y., Demarsin E., Matthyssens G., Collen D., Holvoet R. Characterization of a recombinant single-chain molecule comprising the variable domains of a monoclonal antibody specific for human fibrin fragment D-dimer. J. Biol. Chem 1991; 266: 16343–16349
  • Holvoet P., Laroche Y., Lijnen H. R., Van Cauwnberge R., Demarsin E., Brouwers E., Matthyssens G., Collen D. Characterization of a chimeric plasminogen activator consisting of a single-chain Fv fragment derived from a fibrin fragment D-dimer-specific antibody and a truncated single-chain urokinase. J. Biol. Chem 1991; 266: 19717–19724
  • Anand N. N., Mandal S., MacKenzie C. R., Sadowska J., Sigurskjold B., Young N. M., Bundle D. R., Narang S. A. Bacterial expression and secretion of various single-chain Fv genes encoding proteins specific for a Salmonella serotype B O-antigen. J. Biol. Chem 1991; 266: 21874–21879
  • Fuchs R., Breitling E., Dübel S., Seehaus T., Little M. Targeting recombinant antibodies to the surface of Escherichia coli: Fusion to a peptidoglycan associated lipoprotein. Bio/Technology 1991; 9: 1369–1372
  • Breitling E., Dübel S., Seehaus T., Klewinghaus I., Little M. A surface expression vector for antibody screening. Gene 1991; 104: 147–153
  • Dübel S., Breitling E., Seehaus T., Little M. Generation of a human IgM expression library in E. coli. Methods in Molecular and Cellular Biology 1992; 3: 47–52
  • Seehaus T., Breitling E., Dübel S., Klewinghaus I., Little M. A vector for the removal of deletion mutants from antibody libraries. Gene 1992; 114: 235–237
  • Takkinen K., Laukkanen M. -L., Sizmann D., Alfthan K., Immonen T., Vanne L., Kaartinen M., Knowles J. K. C., Teeri T. T. An active single-chain antibody containing a cellulase linker domain is secreted by. Escherichia coli. Prot. Eng 1991; 4: 837–841
  • Dreher M. L., Gherardi E., Skerra A., Milstein C. Colony assays for antibody fragments expressed in bacteria. J. Immunol. Methods 1991; 139: 197–205
  • Kohl J., Riiker F., Himmler G., Razazzi E., Katinger H. Cloning and expression of an HIV-1 specific single-chain Fv region fused to Escherichia coli alkaline phosphatase. Ann. N. Y. Acad. Sci., USA 1991; 646: 106–114
  • Weidner K. M., Voss E., Jr. Immunological characterization of Xenogenic anti-metatype antibodies. J. Biol. Chem 1991; 266: 2513–2519
  • Cheadle C., Hook L. E., Givol D., Ricca G. A. Cloning and expression of the variable regions of mouse myeloma protein MOPC315 in E. coli: Recovery of active Fv fragments. Molecular Immunology 1992; 29: 21–30
  • Bregegere F., Bedouelle H. Expression, export and purification of antibody fragments fused to the maltose binding protein of Escherichia coli. Comptes Rendus de l'Academie des Sciences. Series III - Sciences de la Vie 1992; 314: 527–532
  • Wels W., Harwerth I. -M., Zwickl M., Hardman N., Groner B., Hynes N. E. Construction, bacterial expression and characterization of a bifunctional single-chain antibody-phosphatase fusion protein targeted to the human erbB-2 receptor. Bio/Technology 1992; 10: 1128–1132
  • Wels W., Harwerth I. M., Hynes N. E., Groner B. Diminution of antibodies directed against tumor cell surface epitopes: A single chain Fv fusion molecules specifically recognizes the extracellular domain of the c-erbB-2 receptor. J. Steroid Biochem. Molec. Biol 1992; 43: 1–7
  • Wels W., Harwerth I. -M., Mueller M., Groner B., Hynes N. E. Selective inhibition of tumor cell growth by a recombinant single-chain antibody-toxin specific for the erbB-2 receptor. Cancer Res 1992; 52: 6310–6317
  • Mottez E., Jaulin C., Godeau F., Choppin J., Levy J. -P., Kourilsky P. A single-chain murine class I major transplantation antigen. Eur. J. Immunol 1991; 21: 467–471
  • Traunecker A., Lanzavecchia A., Karjalainen K. Bispecific single chain molecules (Janusins) target cytotoxic lymphocytes on HIV infected cells. EMBO J 1991; 10: 3655–3659
  • Novotny J., Ganju R. K., Smiley S. T., Hussey R. E., Luther M. A., Recny M. A., Siliciano R. F., Reinherz E. A soluble, single-chain T-cell receptor fragment endowed with antigen-combining properties. Proc. Nat. Acad. Sci., USA 1991; 88: 8646–8650
  • Hoo W. F. S., Lacy M. J., Denzin L. K., Voss E. W., Jr., Hardman K. D., Kranz D. M. Characterization of a single-chain T-cell receptor expressed in Escherichia coli. Proc. Nat. Acad. Sci. USA 1992; 89: 4759–4763
  • Ward E. S. Secretion of T cell receptor fragments from recombinant Escherichia coli cells. J. Mol. Biol 1992; 224: 885–890
  • Duchosal M. A., Eming S. A., Fischer P., Leturcq D., Barbas C. F., III, McConahey P. J., Caothien R. H., Thornton G. B., Dixon F. J., Burton D. R. Immunization of hu-PBL-SCID mice and the rescue of human monoclonal Fab fragments through combinatorial libraries. Nature 1992; 355: 258–262
  • Smith T. W., Butler V P., Jr., Haber E., Fozzard H., Marcus F. I., Bremner W. E., Schulman I. C., Phillips A. Treatment of life-threatening digitalis intoxication with digoxin-specific Fab antibody fragments: Experience in 26 cases. N. Engl. J. Med 1982; 307: 1357–1362
  • Lechat R., Mudgett-Hunter M., Margolies M. N., Haber E., Smith T. W. Reversal of lethal digoxin toxicity in guinea pigs using monoclonal antibodies and Fab fragments. J. Pharm. Expt. Therapeut 1984; 229: 210–213
  • Huston J. S., Bjork I., Tanford C. Properties of the Fd fragment from rabbit immunoglobulin G. Biochemistry 1972; 11: 4256–4262
  • Roberts S., Cheetham J., Rees A. R. Generation of an antibody with enhanced affinity and specificity for its antigen by protein engineering. Nature 1989; 328: 731–734
  • Dias J. A., Huston J. S., Reichert L. E., Jr. Differential effects of monovalent and bivalent antisera on the interaction of follicle stimulating hormone with its receptor. Endocrinol 1984; 114: 1259–1265
  • Painter R. G., Sage H. J., Tanford C. Contributions of heavy and light chains of rabbit immunoglobulin G to antibody activity. I. Binding studies on isolated heavy and light chains. Biochemistry 1972; 11: 1327–1337
  • Fischmann T. O., Bentley G. A., Bhat T. N., Boulot G., Mariuzza R. A., Phillips S. E. V., Tello D., Poljak R. J. Crystallographic refinement of the three-dimensional structure of the FabD1.3-lysozyme complex at 2.5 Å resolution. J. Biol. Chem 1991; 266: 12915–12920
  • Bernstein F. C., Brice M. D., Rodgers J. R., Kennard O., Shimanouchi T., Tasumi M. The protein data bank: a computer-based archival file for macromolecular structures. J. Mol. Biol 1977; 112: 535–542
  • Mudgett-Hunter M., Margolies M. N., Ju A., Haber E. High-affinity monoclonal antibodies to the cardiac glycoside, digoxin. J. Immunol 1982; 129: 1165–1172
  • Khaw B. -A., Mattis J. A., Melincoff G., Strauss H. W., Gold H. K., Haber E. Monoclonal antibody to cardiac myosin: Imaging of experimental myocardial infarction. Hybridoma 1984; 3: 11–23
  • Zalutsky M. R., Garg P. K., Johnson S. H., Utsunomiya H., Coleman R. E. Fluorine-18-antimyosin monoclonal antibody fragments: Preliminary investigations in a canine myocardial infarct model. J. Nucl. Med 1992; 33: 575–580
  • Cumber A. J., Ward E. S., Winter G., Parnell G. D., Wawrzynczak E. J. Comparative stabilities in vitro and in vivo of a recombinant mouse antibody FvCys fragment and a bisFvCys conjugate. J. Immunol 1992; 149: 120–126
  • King D. J., Mountain A., Adair J. R., Owens R. J., Harvey A., Weir N., Proudfoot K. A., Phipps A., Lawson A., Rhind S. K., Pedley B., Boden J., Boden R., Begent R. H. J., Yarranton G. T. Tumor localization of engineered antibody fragments. Antibody Immunoconj. Radiopharmaceut 1992; 5: 159–170
  • Huston J. S., Cohen C., Maratea D., Fields E., Tai M. -S., Cabral-Denison N., Juffras R., Rueger D. C., Ridge R. J., Oppermann H., Keck R., Baird L. G. Multisite association by recombinant proteins can enhance binding selectivity: Preferential removal of immune complexes from serum by immobilized truncated FB analogues of the B domain from staphylococcal protein A. Biophysical Journal 1992; 62: 87–91
  • Anthony J., Near R., Wong S. -L., Iida E., Ernst E., Wittekind M., Haber E., Ng S. -C. Production of stable anti-digoxin Fv in Escherichia coli. Mol. Immunol 1992; 29: 1237–1247
  • Gherardi E., Milstein C. Original and artificial antibodies. Nature 1992; 357: 201–202
  • Schott M. E., Milenic D. E., Yokota T., Whitlow M., Wood J. F., Fordyce W. A., Cheng R. C., Schlom I. Differential metabolic patterns of iodinated versus radiometal chelated anticarcinoma single-chain Fv molecules. Cancer Res 1992; 52: 6413–6417
  • Ayala M., Duenas M., Santos A., Vazquez J., Menendez A., Silva A., Gavilondo J. V. Bacterial single-chain antibody fragments, specific for carcinoembryonic antigen. BioTechniques 1992; 13: 790–799
  • Owen M., Gandecha A., Cockburn B., Whitelam G. Synthesis of a functional anti-phytochrome single-chain Fv protein in transgenic tobacco. Bio/Technology 1992; 10: 790–794
  • Gandecha A. R., Owen M. R. L., Cockburn B., Whitelam G. C. Production and secretion of a bifunctional staphylococcal protein A::antiphytochrome single-chain Fv fusion protein in Escherichia coli. Gene 1992; 122: 361–365
  • Malby R. L., Lawrence M., Tulip W. R., Harley V. R., Webster R. G., Hudson P. J., Colman P. M. Crystal structure of the complex between a single-chain antibody and neuraminidase: A basis for rational protein engineering. Miami Short Reports 1993; 3: 85
  • Hoogenboom H. R., Winter G. Human antibodies from synthetic repertoires of germline VH gene segments rearranged in vitro. J. Mol. Biol 1992; 227: 381–388
  • Wu X -C., Ng S. -C., Near R. J., Wong S. -L. Efficient production of a functional single-chain antidigoxin antibody via an engineered Bacillus subtilis expression-secretion system. Bio/Technology 1993; 11: 71–76
  • Knappik A., Krebber C., Plückthun A. The effect of folding catalysts on the in vivo folding process of different antibody fragments expressed in. Escherichia coli. Bio/Technology 1993; 11: 77–83
  • Friedman P. N., McAndrew S. J., Gawlak S. L., Chace D., Trail P. A., Brown J. R., Siegall C. G. BR96 sFv-PE40, a potent single-chain immunotoxin that selectively kills carcinoma cells. Cancer Research 1993; 53: 334–339
  • Brigido M. M., Polymenis M., Stollar B. D. Role of mouse VH10 and VL gene segments in the specific binding of antibody to Z-DNA, analyzed with recombinant single chain Fv molecules. J. Immunol 1993; 150: 469–479
  • Kurucz I., Jost C. R., George A. J.T., Andrew S. M., Segal D. M. A bacterially-expressed single chain Fv construct from the 2B4 T cell receptor. Proc. Nat. Acad. Sci., USA 1993; 90, In press
  • Mage M. G., Lee L., Ribaudo R. K., Corr M., Kozlowski S., McHugh L., Margulies D. H. A recombinant, soluble, single-chain class I major histocompatibility complex molecule with biological activity. Proc. Nat. Acad. Sci., USA 1992; 89: 10658–10662
  • Embleton M. J., Gorochov G., Jones P. T., Winter G. In-cell PCR from mRNA: amplifying and linking the rearranged immunoglobulin heavy and light chain V-genes within single cells. Nucleic Acids Res 1992; 20: 3831–3837

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