Single-chain Fv designs for protein, cell and gene therapeutics

Bibliography

• BIRD RE, HARDMAN KD, JACOBSON JW et al: Single- chain antigen-binding proteins. Science (1988) 242(4877)423–426.
   Google Scholar
• ••First article by Genex on sFy proteins.
   Google Scholar
• HUSTON JS, LEVINSON D, MUDGETT-HUNTER M et al: Protein engineering of antibody binding sites: recov-ery of specific activity in an anti-digoxin single-chain Fv analogue produced in Escherichia coif Proc. Natl. Acad. Sci. USA (1988) 85(16):5879–5883.
   PubMed Web of Science ®Google Scholar
• ••First article by CBM on sFy proteins.
   Google Scholar
• GEORGE AJT, EPENETOS AA: Advances in antibody en-gineering. Exp. Opin. Ther. Patents (1996) 6(5):441–456.
   Google Scholar
• HUDSON PJ: Recombinant antibody fragments. Curr. Opin. Biotechnol. (1998) 9(4):395–402.
   PubMedGoogle Scholar
• DALL'ACQUA W, CARTER P: Antibody engineering. Curr. Opin. Struct. Biol. (1998) 8(4):443–450.
   PubMedGoogle Scholar
• DE HAARD H, HENDERIKX P, HOOGENBOOM HR: Creat-ing and engineering human antibodies for immuno-therapy. Adv. Drug Deily. Rev. (1998) 31(1,2):5–31.
   Google Scholar
• KREITMAN RJ, PASTAN I: Immunotoxins for targeted cancer therapy. Adv. Drug Delhi. Rev. (1998) 31 (1,2):53–88.
   Google Scholar
• JONES SD, MARASCO WA: Antibodies for targeted genetherapy: extracellular gene targeting and intracellular expression. Adv. Drug Deliv. Rev. (1998) 31(1,2):153–170.
   Google Scholar
• FITZER-ATTAS CJ, ESHHAR Z: Tyrosine kinase chimeras for antigen-selective T-body therapy. Adv. Drug Deliv. Rev. (1998) 31(1,2):171–182.
   Google Scholar
• PLÜCKTHUN A, PACK P: New protein engineering ap-proaches to multivalent and bispecific antibody frag-ments. Immunotechnology (1997) 3 (2) :83–105.
   PubMedGoogle Scholar
• WANG D, BERVEN E, LI Q, UCKUN F, KERSEY JH: Optimi-zation of conditions for formation and analysis of anti-CD19 FVS191 single-chain Fv homodimer (scFv12. Bioconjugate Chem. (1997) 8(0:64–70.
   PubMedGoogle Scholar
• MeLLER KM, ARNDT KM, STRITTMATTER W, Plackthun A: The first constant domain (CH1 and CO of an antibody used as heterodimerization domain for bispecific miniantibodies. FEBS Lett. (1998) 422 (2) :259–264.
   PubMedGoogle Scholar
• LIBYH MT, GOOSSENS D, OUDIN S et al: A recombinanthuman scEv anti-Rh(D) antibody with multiple va-lences using a C-terminal fragment of C4-binding pro-tein. Blood (1997) 90(10:3978–3983.
   PubMedGoogle Scholar
• WHITLOW M, FILPULA D, ROLLENCE ML, FENG S-L, WOOD JF: Multivalent Fvs: characterization of single-chain Fv oligomers and preparation of a bispecific Fv. Protein Engin. (1994) 7 (8) :1017–1026.
   PubMedGoogle Scholar
• •This article characterises multivalent and heterodimeric Fv.
   Google Scholar
• ARNDT KM, WILLER KM, PLÜCKTHUN A: Factors influ-encing the dimer to monomer transition of an anti-body single-chain Fv fragment. Biochemistry (1998) 37 (37):12918–12926.
   PubMed Web of Science ®Google Scholar
• ADAMS GP, SCHIER R, MCCALL AM et al.: Prolonged invivo tumour retention of a human diabody targeting the extracellular domain of human HER2/neu. Br. J. Cancer (1998) 77(9):1405–1412.
   PubMed Web of Science ®Google Scholar
• •The value of bivalency for sFy proteins is demonstrated in an animal model.
   Google Scholar
• ZHU Z, ZAPATA G, SHALABY R, SNEDECOR B, CHEN H, CARTER P: High level secretion of a humanized bispe-cific diabody from Escherichia coli. Biotechnology (1996) 14 (2) :192–196.
   PubMedGoogle Scholar
• GHETIE M-A, PODAR EM, ILGEN A, GORDON BE, UHR JW, VITETTA ES: Homodimerization of tumor-specific monoclonal antibodies markedly increases their abil-ity to induce growth arrest or apoptosis of tumor cells. Proc. Natl. Acad. Sci. USA (1997) 94(14):7509–7514.
   PubMedGoogle Scholar
• WORN A, PLÜCKTHUN A: Mutual stabilization of VI, and VH in single-chain antibody fragments, investigated with mutants engineered for stability. Biochemistry (1998) 37(38):13120–13127.
   PubMedGoogle Scholar
• ALMOG O, BENHAR I, VASMATZIS G et al.: Crystal struc-ture of the disulfide-stabilized Fv fragment of antican-cer antibody B 1: conformational influence of an engineered disulfide bond. Proteins Struct. Func. Genet. (1998) 31(2):128–138.
   Google Scholar
• RAJAGOPAL V, PASTAN I, KREITMAN RJ: A form of anti-Tac(Fv) which is both single-chain and disulfide stabi-lized: comparison with its single-chain and disulfide-stabilized homologs. Protein Engin. (1997) 10 (12) :1453–1459.
   PubMedGoogle Scholar
• ZHU Z, PRESTA LG, ZAPATA G, CARTER P: Remodelingdomain interfaces to enhance heterodimer formation. Protein Sci. (1997) 6(4) :781–788.
   PubMedGoogle Scholar
• RAFFEN R, STEVENS PW, BOOGAARD C, SCHIFFER M, STEVENS FJ: Reengineering immunoglobulin domain interactions by introduction of charged residues. Pro-tein Engin. (1998) 11 (4) :303–309.
   PubMedGoogle Scholar
• CHOWDHURY PS, VASMATZIS G, BEERS R, LEE B, PASTAN I: Improved stability and yield of a Fv-toxin fusion pro-tein by computer design and protein engineering of the Fv. j Mol. Biol. (1998) 281 (5) :917–928.
   PubMedGoogle Scholar
• MARTINEAU P, JONES P, WINTER G: Expression of an antibody fragment at high levels in the bacterial cyto-plasm. J. Mol Biol. (1998) 280(0:117–127.
   PubMedGoogle Scholar
• ROBINSON CR, SAUER RT: Optimizing the stability of single-chain proteins by linker length and composi-tion mutagenesis. Proc. Natl. Acad. Sci. USA (1998) 95(105929–5934.
   Google Scholar
• WANG M, LEE LS, NEPOMICH A et al.: Single-chain Fv with manifold N-glycans as bifunctional scaffolds for immunomolecules. Protein Engin. (1998) 11 (12) :1277–1283.
   PubMedGoogle Scholar
• HAISMA HJ, SERNEE MF, HOOIJBERG E et al.: Construc-tion and characterization of a fusion protein of single-chain anti-CD20 antibody and human 6-glucuronidase for antibody-directed enzyme prodrug therapy. Blood (1998) 92(0:184–190.
   PubMedGoogle Scholar
• SHEETS MD, AMERSDORFER P, FINNERN R et al.: Efficient construction of a large nonimmune phage antibody li-brary: the production of high-affinity human single-chain antibodies to protein antigens. Proc. Natl. Acad. Sci. USA (1998) 95 (10:6157–6162.
   PubMedGoogle Scholar
• GRIFFITHS AD, DUNCAN AR: Strategies for selection of antibodies by phage display. Curr. Opin. Biotechnol (1998) 9(0:102–108.
   PubMedGoogle Scholar
• DAVIDSON S: Transplant antibodies vie for attention. Nature Biotechnol. (1998) 16(0:17.
   PubMedGoogle Scholar
• GLASER V: Conflicts brewing as phage display gets complex. Nature Biotechnol. (1997) 15 (6):506.
   PubMedGoogle Scholar
• DAUGHERTY PS, CHEN G, OLSEN MJ, IVERSON BL, GEOR-GIOU G: Antibody affinity maturation using bacterial surface display. Protein Engin. (1998) 11(9):825–832.
   PubMedGoogle Scholar
• HANES J, JERMUTUS L, WEBER-BORNHAUSER S, BOSS-HARD HR, PLÜCKTHUN A: Ribosome display efficiently selects and evolves high-affinity antibodies in vitro from immune libraries. Proc. Natl. Acad. ScL USA (1998) 95(24):14130–14135.
   PubMed Web of Science ®Google Scholar
• PELEGRIN M, MARIN M, NOEL D, PIECHACZYK M: Geneti-cally engineered antibodies in gene transfer and gene therapy. Human Gene Ther. (1998) 9 (15) :2165–2175.
   PubMedGoogle Scholar
• PROBA K, Worn A, HONEGGER A, Plückthun A: Antibody scEv fragments without disulfide bonds made by mo-lecular evolution. J. Mol Biol. (1998) 275(2):245–253.
   PubMedGoogle Scholar
• WORN A, PLÜCKTHUN A: An intrinsically stable anti-body scEv fragment can tolerate the loss of both disulfide bonds and fold correctly. FEBS Lett. (1998) 427(3) 357–361
   PubMedGoogle Scholar
• CHEN S-Y, YANG A-G, CHEN J-D et al.: Potent antitumor activity of a new class of tumour-specific killer cells. Nature (1997) 385(0:78–80.
   PubMedGoogle Scholar
• •A report which presents the potential applications of sFv-secreting cell therapeutics.
   Google Scholar
• NICOLET CM, BURKHOLDER JK, GAN J et al.: Expression of a tumor-reactive antibody-interleukin 2 fusion pro-tein after in vivo particle-mediated gene delivery. Can-cer Gene Ther. (1995) 2 (3) :161–170.
   PubMedGoogle Scholar
• BRINKMANN U, DI CARLO A, VASMATZIS G et al.: Stabili-zation of a recombinant Fv fragment by base-loop in-terconnection and VH-VL permutation. J. Mol (1997) 268(0:107–117.
   PubMedGoogle Scholar
• FILPULA D, LEE S, WANG M et al.: PEGylated sEv and gly-cosylated sFv. IBC's 8th Annual International Conference on Antibody Engineering: New Technology, Application & Commercialization. Coronado, CA, USA (1997).
   Google Scholar
• GLASER V: UCSF targets cancer ND. Nature Biotechnol. (1998) 16(0328.
   Google Scholar
• LOGTENBERG T: The phage antibody display toolbox: discovery of novel antigens and construction of antibody-based therapeutics. IBC's 9th Annual Interna-tional Conference on Antibody Engineering Coronado, CA, USA (1998).
   Google Scholar
• XIE M-H, YUAN J, ADAMS C, GURNEY A: Direct demon-stration of MuSK involvement in acetylcholine recep-tor clustering through identification of agonist scFv. Nature Biotechnol. (1997) 15(8):768–771.
   PubMedGoogle Scholar
• •A report which presents potential utilisation of sFy as agonists.
   Google Scholar
• GAO C, UN C-H, LO C-HL et al.: Making chemistry se-lectable by linking it to infectivity. Proc. Natl. Acad. Sci. USA (1997) 94(22):11777–11782.
   PubMedGoogle Scholar
• BOYLE JS, BRADY JL, LEW AM: Enhanced responses to a DNA vaccine encoding a fusion antigen that is directed to sites of immune induction. Nature (1998) 392 (6674):408–411.
   PubMedGoogle Scholar
• MAGLIANI W, POLONELLI L, CONTI S et al. Neonatal mouse immunity against group B streptococcal infec-tion by maternal vaccination with recombinant anti-idiotypes. Nature Med. (1998) 4(6):705–709.
   PubMedGoogle Scholar
• SHELVER WL, KEYLER DE, UN G etal.: Effects of recombi-nant drug-specific single chain antibody Fv fragment on [311]-desipramine distribution in rats. Biochem. Pharmacol. (1996) 51(4):531–537.
   Google Scholar
• FITCH JCK, ELEFTERIADES JA, RINDER HM et al.: Safety, pharmacokinetics, and immunogenicity of intrave-nous administration of H5G1.1-SCEV in humans. Blood (1996) 88(10):654A.
   Google Scholar
• HOLLIGER P, WING M, POUND JD, BOHLEN H, WINTERG: Retargeting serum immunoglobulin with bispecific diabodies. Nature Biotechnol. (1997) 15 (7):632–636.
   PubMed Web of Science ®Google Scholar
• •This report describes bifunctional diabodies with prolonged circulating life.
   Google Scholar
• HSU FJ, CASPAR CB, CZERWINSKI D et al Tumor-specific idiotype vaccines in the treatment of patients with B-cell lymphoma - long-term results of a clinical trial. Blood (1997) 89(9):3129–3135.
   PubMed Web of Science ®Google Scholar
• MCCORMICK A, KUMAGAI M, HANDLY K, TUSE' D, LEVY R: Rapid production of patient-specific vaccines for the treatment of non-Hodgkin's lymphoma. IBC's Post-Conference Workshop on Engineered Immunofusion Pro-teins. Coronado, CA, USA (1997).
   Google Scholar
• HENDERIKX P, KANDILOGIANNAKI M, PETRARCA C et al Human single-chain Fv antibodies to MUC1 core pep-tide selected from phage display libraries recognize unique epitopes and predominantly bind adenocarci-noma. Cancer Res. (1998) 58(19) 4324–4332
   PubMedGoogle Scholar