scholarly journals Selection of an Anti-CD20, Single-Chain Antibody by Phage ELISA on Fixed Cells

BioTechniques ◽  
1999 ◽  
Vol 26 (4) ◽  
pp. 697-702 ◽  
Author(s):  
Stefanie Schmidt ◽  
Michael Braunagel ◽  
Timo Kürschner ◽  
Melvyn Little
Keyword(s):  
Single Chain ◽  
Single Chain Antibody ◽  
Phage Elisa ◽  
Anti Cd20 ◽  
Selection Of

scholarly journals Construction of Anti-CD20 Single-Chain Antibody-CD28-CD137-TCRζ Recombinant Genetic Modified T Cells and its Treatment Effect on B Cell Lymphoma

2015 ◽  
Vol 21 ◽  
pp. 2110-2115 ◽  
Author(s):  
Fei Chen ◽  
Chuming Fan ◽  
Xuezhong Gu ◽  
Haixi Zhang ◽  
Qian Liu ◽  
...  
Keyword(s):  
T Cells ◽  
B Cell ◽  
Treatment Effect ◽  
Cell Lymphoma ◽  
B Cell Lymphoma ◽  
Single Chain ◽  
Single Chain Antibody ◽  
Anti Cd20

scholarly journals Phage display and kinetic selection of antibodies that specifically inhibit amyloid self-replication

2017 ◽  
Vol 114 (25) ◽  
pp. 6444-6449 ◽  
Author(s):  
Anna Munke ◽  
Jonas Persson ◽  
Tanja Weiffert ◽  
Erwin De Genst ◽  
Georg Meisl ◽  
...  
Keyword(s):  
Phage Display ◽  
Amyloid Fibrils ◽  
Amyloid Β ◽  
Amyloid Β Peptide ◽  
Nucleation Process ◽  
Single Chain ◽  
Secondary Nucleation ◽  
Single Chain Antibody ◽  
Phage Display Libraries ◽  
Selection Of

The aggregation of the amyloid β peptide (Aβ) into amyloid fibrils is a defining characteristic of Alzheimer’s disease. Because of the complexity of this aggregation process, effective therapeutic inhibitors will need to target the specific microscopic steps that lead to the production of neurotoxic species. We introduce a strategy for generating fibril-specific antibodies that selectively suppress fibril-dependent secondary nucleation of the 42-residue form of Aβ (Aβ42). We target this step because it has been shown to produce the majority of neurotoxic species during aggregation of Aβ42. Starting from large phage display libraries of single-chain antibody fragments (scFvs), the three-stage approach that we describe includes (i) selection of scFvs with high affinity for Aβ42 fibrils after removal of scFvs that bind Aβ42 in its monomeric form; (ii) ranking, by surface plasmon resonance affinity measurements, of the resulting candidate scFvs that bind to the Aβ42 fibrils; and (iii) kinetic screening and analysis to find the scFvs that inhibit selectively the fibril-catalyzed secondary nucleation process in Aβ42 aggregation. By applying this approach, we have identified four scFvs that inhibit specifically the fibril-dependent secondary nucleation process. Our method also makes it possible to discard antibodies that inhibit elongation, an important factor because the suppression of elongation does not target directly the production of toxic oligomers and may even lead to its increase. On the basis of our results, we suggest that the method described here could form the basis for rationally designed immunotherapy strategies to combat Alzheimer’s and related neurodegenerative diseases.

scholarly journals Selection of Linkers for a Catalytic Single-chain Antibody Using Phage Display Technology

1996 ◽  
Vol 271 (26) ◽  
pp. 15682-15686 ◽  
Author(s):  
Ying Tang ◽  
Ning Jiang ◽  
Cushrow Parakh ◽  
Donald Hilvert
Keyword(s):  
Phage Display ◽  
Single Chain ◽  
Single Chain Antibody ◽  
Phage Display Technology ◽  
Display Technology ◽  
Selection Of

scholarly journals Design and Selection of a Camelid Single-Chain Antibody Yeast Two-Hybrid Library Produced De Novo for the Cap Protein of Porcine Circovirus Type 2 (PCV2)

PLoS ONE ◽  
2013 ◽  
Vol 8 (3) ◽  
pp. e56222 ◽  
Author(s):  
Xiangjing Fu ◽  
Xiaolong Gao ◽  
Shengfang He ◽  
Di Huang ◽  
Peng Zhang ◽  
...  
Keyword(s):  
De Novo ◽  
Porcine Circovirus Type ◽  
Porcine Circovirus Type 2 ◽  
Porcine Circovirus ◽  
Single Chain ◽  
Yeast Two Hybrid ◽  
Single Chain Antibody ◽  
Two Hybrid ◽  
Selection Of

scholarly journals Comparison of a tetravalent single-chain antibody-streptavidin fusion protein and an antibody-streptavidin chemical conjugate for pretargeted anti-CD20 radioimmunotherapy of B-cell lymphomas

Blood ◽  
2006 ◽  
Vol 108 (1) ◽  
pp. 328-336 ◽  
Author(s):  
John M. Pagel ◽  
Yukang Lin ◽  
Nathan Hedin ◽  
Anastasia Pantelias ◽  
Donald Axworthy ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Athymic Mice ◽  
Single Chain ◽  
Single Chain Antibody ◽  
Normal Organ ◽  
Normal Tissues ◽  
Non Hodgkin Lymphoma ◽  
Chemical Conjugate ◽  
Anti Cd20 ◽  
Cd20 Antibodies

The efficacy of radioimmunotherapy (RIT) for patients with relapsed non-Hodgkin lymphoma (NHL) is limited by nonspecific delivery of radiation to normal tissues due to the long circulating half-life of radiolabeled anti-CD20 antibodies (Abs). Pretargeted RIT using a covalent conjugate of the 1F5 anti-CD20 Ab with streptavidin (SA) has been shown to augment the efficacy of RIT and decrease toxicity compared with a directly labeled 1F5 Ab. We have engineered a tetravalent singlechain 1F5 (scFv)4SA fusion protein and compared it to the 1F5-SA conjugate. Athymic mice bearing Ramos lymphoma xenografts received either the conjugate or fusion protein, followed 20 hours later by a biotin-N-acetyl-galactosamine clearing agent, followed 4 hours later by 111In-DOTA-biotin. After 24 hours, 11.4% ± 2.1% of the injected dose of radionuclide was present per gram of tumor (% ID/g) using 1F5 (scFv)4SA compared with 10.8% ± 2.5% ID/g with 1F5 Ab-SA. Superior tumor-to-normal organ ratios of radioactivity were consistently seen using the fusion protein compared with the chemical conjugate (eg, tumor-to-blood ratio > 65:1 after 48 hours with the fusion protein, but < 7:1 with the conjugate). More than 90% of lymphomabearing mice could be cured with minimal toxicity using either reagent followed by 1200 μCi (44.4 MBq) 90Y-DOTA-biotin. (Blood. 2006;108:328-336)

In vitro Cytolysis of B-Lymphoma Cells Mediated by an Anti-CD3/Anti-CD20 Bispecific Single-chain Antibody

2006 ◽  
Vol 22 (3) ◽  
pp. 384-390
Author(s):  
R YU ◽  
S LI ◽  
B WU ◽  
H LIU ◽  
L YE ◽  
...  
Keyword(s):  
Single Chain ◽  
Single Chain Antibody ◽  
Lymphoma Cells ◽  
B Lymphoma ◽  
B Lymphoma Cells ◽  
Anti Cd20

Selection of Human Metalloantibodies from a Combinatorial Phage Single-Chain Antibody Library

1999 ◽  
Vol 121 (27) ◽  
pp. 6517-6518 ◽  
Author(s):  
Changshou Gao ◽  
Oliver Brümmer ◽  
Shenlan Mao ◽  
Kim D. Janda
Keyword(s):  
Antibody Library ◽  
Single Chain ◽  
Single Chain Antibody ◽  
Selection Of

Selection of Single Chain Antibody Fragments for Targeting Prostate Specific Membrane Antigen: A Comparison Between Cell-based and Antigen-based Approach

2016 ◽  
Vol 23 (4) ◽  
pp. 336-342 ◽  
Author(s):  
Javad Rezaei ◽  
Masoumeh RajabiBazl ◽  
Walead Ebrahimizadeh ◽  
Gholamreza Rafiei Dehbidi ◽  
Hossien Hosseini
Keyword(s):  
Antibody Fragments ◽  
Prostate Specific Membrane Antigen ◽  
Single Chain ◽  
Single Chain Antibody ◽  
Antigen A ◽  
Specific Membrane ◽  
Selection Of
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