Development and Preclinical Testing of a High-Affinity Single-Chain Antibody against (+)-Methamphetamine

2009 ◽  
Vol 2009 ◽  
pp. 108-109
Author(s):  
R. Frances
Keyword(s):  
Single Chain ◽  
Single Chain Antibody ◽  
Preclinical Testing ◽  
High Affinity

scholarly journals Preclinical Testing of a High Affinity Single Chain Antibody against (+)‐Methamphetamine (METH)

2007 ◽  
Vol 21 (6) ◽  
Author(s):  
Eric Charles Peterson ◽  
Elizabeth M Laurenzna ◽  
Howard P Hendrickson ◽  
S Michael Owens
Keyword(s):  
Single Chain ◽  
Single Chain Antibody ◽  
Preclinical Testing ◽  
High Affinity

scholarly journals Development and Preclinical Testing of a High-Affinity Single-Chain Antibody against (+)-Methamphetamine

2008 ◽  
Vol 325 (1) ◽  
pp. 124-133 ◽  
Author(s):  
Eric C. Peterson ◽  
Elizabeth M. Laurenzana ◽  
William T. Atchley ◽  
Howard P. Hendrickson ◽  
S. Michael Owens
Keyword(s):  
Single Chain ◽  
Single Chain Antibody ◽  
Preclinical Testing ◽  
High Affinity

scholarly journals Antibodies that potently inhibit or enhance SARS-CoV-2 spike protein-ACE2 interaction isolated from synthetic single-chain antibody libraries

2020 ◽  
Author(s):  
Matthew D. Beasley ◽  
Sanja Aracic ◽  
Fiona M. Gracey ◽  
Ruban Kannan ◽  
Avisa Masarati ◽  
...  
Keyword(s):  
Vaccine Development ◽  
Spike Protein ◽  
Receptor Binding Domain ◽  
Single Chain ◽  
Single Chain Antibody ◽  
High Affinity ◽  
Scfv Library ◽  
Antibody Libraries ◽  
Prophylactic Use

AbstractAntibodies with high affinity against the receptor binding domain (RBD) of the SARS-CoV-2 S1 ectodomain were identified from screens using the Retained Display™ (ReD) platform employing a 1 × 1011 clone single-chain antibody (scFv) library. Numerous unique scFv clones capable of inhibiting binding of the viral S1 ectodomain to the ACE2 receptor in vitro were characterized. To maximize avidity, selected clones were reformatted as bivalent diabodies and monoclonal antibodies (mAb). The highest affinity mAb completely neutralized live SARS-CoV-2 virus in cell culture for four days at a concentration of 6.7 nM, suggesting potential therapeutic and/or prophylactic use. Furthermore, scFvs were identified that greatly increased the interaction of the viral S1 trimer with the ACE2 receptor, with potential implications for vaccine development.

scholarly journals PEGylation of a High-Affinity Anti-(+)Methamphetamine Single Chain Antibody Fragment Extends Functional Half-Life by Reducing Clearance

2016 ◽  
Vol 33 (12) ◽  
pp. 2954-2966 ◽  
Author(s):  
Emily E. Reichard ◽  
Nisha Nanaware-Kharade ◽  
Guillermo A. Gonzalez ◽  
Shraddha Thakkar ◽  
S. Michael Owens ◽  
...  
Keyword(s):  
Half Life ◽  
Antibody Fragment ◽  
Single Chain ◽  
Single Chain Antibody ◽  
High Affinity ◽  
Single Chain Antibody Fragment

Phage-displayed recombinant single-chain antibody fragments with high affinity for cholesteryl ester transfer protein (CETP): cDNA cloning, characterization and CETP quantification

2004 ◽  
Vol 42 (3) ◽  
Author(s):  
Andreas Ritsch ◽  
Christoph Ebenbichler ◽  
Elisabeth Naschberger ◽  
Wilfried Schgoer ◽  
Ursula Stanzl ◽  
...  
Keyword(s):  
Cholesteryl Ester ◽  
Cholesteryl Ester Transfer Protein ◽  
Density Lipoprotein ◽  
Phage Display Library ◽  
Antibody Fragments ◽  
Single Chain ◽  
Single Chain Antibody ◽  
Recombinant Phage ◽  
Transfer Protein ◽  
High Affinity

AbstractCholesteryl ester transfer protein (CETP) greatly affects the metabolism of all lipoprotein classes including low-density lipoprotein (LDL) and high-density lipoprotein (HDL), bothknown to constitute powerful risk factors for coronary artery disease (CAD). We now report the successful first cloning and characterization of single-chain antibody fragments specific for CETP. A recombinant phage display library was generated using spleen mRNA isolated from BALB/c mice that had been immunized with highly purified CETP. Screening of the library yielded two single-chain antibody fragments with high affinity for CETP, termed 1CL8 and 1CL10, displaying respective K

scholarly journals Generation of High-Affinity Chicken Single-Chain Fv Antibody Fragments for Measurement of the Pseudonitzschia pungens Toxin Domoic Acid

2006 ◽  
Vol 72 (5) ◽  
pp. 3343-3349 ◽  
Author(s):  
William J. J. Finlay ◽  
Iain Shaw ◽  
Joanna P. Reilly ◽  
Marian Kane
Keyword(s):  
Domoic Acid ◽  
Recombinant Antibody ◽  
Variable Region ◽  
Antibody Fragments ◽  
Enzyme Linked Immunosorbent Assay ◽  
Single Chain ◽  
Single Chain Antibody ◽  
High Affinity ◽  
Single Chain Fv ◽  
Recombinant Antibody Fragments

ABSTRACT Antibody-based assay systems are now accepted by regulatory authorities for detection of the toxins produced by phytoplankton that accumulate in shellfish tissues. However, the generation of suitable antibodies for sensitive assay development remains a major challenge. We have examined the potential of using the chicken immune system to generate high-affinity, high-specificity recombinant antibody fragments against phytotoxins. Following immunization of the chicken with domoic acid-bovine serum albumin, a single-chain antibody variable region (scFv) gene library was generated from single VH and VL genes isolated from the immune cells in the spleen and bone marrow. scFvs reacting with domoic acid were isolated by phage display and affinity matured by light chain shuffling, resulting in an approximate 10-fold increase in sensitivity. The isolated scFvs were effectively expressed in Escherichia coli and readily purified by affinity chromatography. They were then used to develop a convenient and sensitive indirect competitive enzyme-linked immunosorbent assay for domoic acid, with a 50% effective dose of 156 ng/ml, which could be used reliably with shellfish extracts. This study demonstrates that chickens provide a valuable model system for the simplified, rapid generation of high-affinity recombinant antibody fragments with specificity for small toxin molecules.

scholarly journals Immunological and structural characterization of a high affinity anti-fluorescein single-chain antibody.

1990 ◽  
Vol 265 (30) ◽  
pp. 18615-18620 ◽  
Author(s):  
W D Bedzyk ◽  
K M Weidner ◽  
L K Denzin ◽  
L S Johnson ◽  
K D Hardman ◽  
...  
Keyword(s):  
Structural Characterization ◽  
Single Chain ◽  
Single Chain Antibody ◽  
High Affinity

scholarly journals Trimolecular Complex Formation of IgE, FcεRI, and a Recombinant Nonanaphylactic Single-Chain Antibody Fragment with High Affinity for IgE

2009 ◽  
Vol 182 (8) ◽  
pp. 4817-4829 ◽  
Author(s):  
Christian Lupinek ◽  
Kenneth H. Roux ◽  
Sylvia Laffer ◽  
Ingrid Rauter ◽  
Kavita Reginald ◽  
...  
Keyword(s):  
Complex Formation ◽  
Antibody Fragment ◽  
Single Chain ◽  
Single Chain Antibody ◽  
High Affinity ◽  
Trimolecular Complex ◽  
Single Chain Antibody Fragment
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