Fab chains as an efficient heterodimerization scaffold for the production of recombinant bispecific and trispecific antibody derivatives

Journal of Immunology

Volumn 165, Issue 12, 2000, Pages 7050-7057

  Schoonjans, R ^a   Willems, A ^a   Schoonooghe, S ^a   Fiers, W ^a   Grooten, J ^a   Mertens, N ^a  

^a Department of Molecular Biology ^*  (Belgium)

Author keywords

[No Author keywords available]

Indexed keywords

BISPECIFIC ANTIBODY; IMMUNOGLOBULIN F(AB) FRAGMENT; RECOMBINANT ANTIBODY; TRISPECIFIC ANTIBODY; UNCLASSIFIED DRUG;

ANIMAL CELL; ANTIBODY PRODUCTION; ANTIBODY SPECIFICITY; ARTICLE; BINDING SITE; CONTROLLED STUDY; DIMERIZATION; DRUG PENETRATION; DRUG RETENTION; FIBROSARCOMA; GENE EXPRESSION SYSTEM; HUMAN; HUMAN CELL; IMMUNOTHERAPY; KIDNEY CELL; MOLECULAR SIZE; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; TH1 CELL;

EID: 0034671764     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: 10.4049/jimmunol.165.12.7050     Document Type: Article

References (28)

1. 2 antibody containing thioetherlinked Fab'γ fragments
2. Hybrid hybridomas and their use in immunohistochemistry
3. A small bispecific antibody construct expressed as a functional single-chain molecule with high tumor cell cytotoxicity
4. Miniantibodies use of amphipathic helices to produce functional, flexibly linked dimeric Fv fragments with high avidity in Escherichia coli
5. An engineered bivalent single-chain antibody fragment that increases antigen binding activity
6. A dimeric bispecific miniantibody combines two specificities with avidity
7. Tumor localization of anti-CEA single-chain Fvs improved targeting by non-covalent dimers
8. 2, and Fab' anticarcinoembryonic antigen antibodies labeled with 99mTc the role of metabolism and kinetics
9. High level secretion of a humanized bispecific diabody from Escherichia coli
10. An efficient route to human bispecific IgG
11. Spontaneous assembly of bivalent single chain antibody fragments in Escherichia coli
12. Minibody a novel engineered anticarcinoembryonic antigen antibody fragment (single-chain Fv-CH3) which exhibits rapid, high-level targeting of xenografts
13. The first constant domain (C(H)1 and C(L)) of an antibody used as heterodimerization domain for bispecific miniantibodies
14. Quality control in the secretory pathway the role of calreticulin, calnexin and BiP in the retention of glycoproteins with C-terminal truncations
15. Analysis of mutation in human cells by using an Epstein-Barr virus shuttle system
16. Acquisition by the murine host of responsiveness toward various neoplastic cell lines, but not toward self, through adoptive transfer of a helper T-lymphocyte clone with antiself specificity
17. Bispecific antibody-mediated lysis of placental and germ cell alkaline phosphatase targeted solid tumors in immunocompetent mice
18. Radiolocalisation and imaging of stably HPLAP-transfected MO4 tumours with monoclonal antibodies and fragments
19. In vivo retargeting of T cell effector function by recombinant bispecific single chain Fv (anti-CD3 X anti-idiotype) induces longterm survival in the murine BCL1 lymphoma model
20. Efficient selection for highexpression transfectants with a novel eukaryotic vector
21. 2 fragments in COS-1 cells
22. Production and characterization of bispecific single-chain antibody fragments
23. Optimization of experimental variables influencing reporter gene expression in hepatoma cells following calcium phosphate transfection
24. Expression in non-lymphoid cells of mouse recombinant immunoglobulin directed against the tumour marker human placental alkaline phosphatase
25. Screening of sera and tumor extracts of cancer patients using a monoclonal antibody directed against human placental alkaline phosphatase
26. Coordination of immununoglobulin chain folding and immunoglobulin chain assembly is essential for the formation of functional IgG
27. Immunoglobulin heavy chain and binding protein complexes are dissociated in vivo by light chain addition
28. BiP and immunoglobulin light chain cooperate to control the folding of heavy chain and ensure the fidelity of immunoglobulin assembly