Interactions of High Affinity Anti (6-4) Photoproduct Antibody Fragments with Damaged DNA

1999 ◽  
Vol 18 (6-7) ◽  
pp. 1321-1322 ◽  
Author(s):  
Eiko Ohtsuka ◽  
Hiroyuki Kobayashi ◽  
Hiroshi Morioka ◽  
Kousuke Sato ◽  
Yasuo Komatsu ◽  
...  
Keyword(s):  
Antibody Fragments ◽  
High Affinity ◽  
Damaged Dna

scholarly journals High Affinity Human Antibody Fragments to Dengue Virus Non-Structural Protein 3

2010 ◽  
Vol 4 (11) ◽  
pp. e881 ◽  
Author(s):  
Nicole J. Moreland ◽  
Moon Y. F. Tay ◽  
Elfin Lim ◽  
Prasad N. Paradkar ◽  
Danny N. P. Doan ◽  
...  
Keyword(s):  
Dengue Virus ◽  
Antibody Fragments ◽  
Human Antibody ◽  
Structural Protein ◽  
High Affinity

scholarly journals High-Affinity Recombinant Antibody Fragments (Fabs) Can Be Applied in Peptide Enrichment Immuno-MRM Assays

2014 ◽  
Vol 13 (4) ◽  
pp. 2187-2196 ◽  
Author(s):  
Jeffrey R. Whiteaker ◽  
Lei Zhao ◽  
Christian Frisch ◽  
Francisco Ylera ◽  
Stefan Harth ◽  
...  
Keyword(s):  
Recombinant Antibody ◽  
Antibody Fragments ◽  
High Affinity ◽  
Recombinant Antibody Fragments ◽  
Peptide Enrichment

scholarly journals Single-Stranded DNA Aptamers against Pathogens and Toxins: Identification and Biosensing Applications

2015 ◽  
Vol 2015 ◽  
pp. 1-31 ◽  
Author(s):  
Ka Lok Hong ◽  
Letha J. Sooter
Keyword(s):  
Nucleic Acid ◽  
Molecular Recognition ◽  
Nucleic Acids ◽  
Antibody Fragments ◽  
Small Peptides ◽  
Basic Principles ◽  
Single Stranded Dna ◽  
High Affinity ◽  
Ssdna Aptamer ◽  
Recognition Elements

Molecular recognition elements (MREs) can be short sequences of single-stranded DNA, RNA, small peptides, or antibody fragments. They can bind to user-defined targets with high affinity and specificity. There has been an increasing interest in the identification and application of nucleic acid molecular recognition elements, commonly known as aptamers, since they were first described in 1990 by the Gold and Szostak laboratories. A large number of target specific nucleic acids MREs and their applications are currently in the literature. This review first describes the general methodologies used in identifying single-stranded DNA (ssDNA) aptamers. It then summarizes advancements in the identification and biosensing application of ssDNA aptamers specific for bacteria, viruses, their associated molecules, and selected chemical toxins. Lastly, an overview of the basic principles of ssDNA aptamer-based biosensors is discussed.

scholarly journals Characterization and structure determination of a llama-derived nanobody targeting the J-base binding protein 1

2018 ◽  
Vol 74 (11) ◽  
pp. 690-695 ◽  
Author(s):  
Bart van Beusekom ◽  
Tatjana Heidebrecht ◽  
Athanassios Adamopoulos ◽  
Alexander Fish ◽  
Els Pardon ◽  
...  
Keyword(s):  
Binding Protein ◽  
Antibody Fragments ◽  
Molecular Replacement ◽  
Asymmetric Unit ◽  
Single Domain Antibody ◽  
High Affinity ◽  
Domain Antibody ◽  
Ligand Free ◽  
Complementarity Determining Regions

J-base binding protein 1 (JBP1) contributes to the biosynthesis and maintenance of base J (β-D-glucosylhydroxymethyluracil), a modification of thymidine confined to some protozoa. Camelid (llama) single-domain antibody fragments (nanobodies) targeting JBP1 were produced for use as crystallization chaperones. Surface plasmon resonance screening identified Nb6 as a strong binder, recognizing JBP1 with a 1:1 stoichiometry and high affinity (K d = 30 nM). Crystallization trials of JBP1 in complex with Nb6 yielded crystals that diffracted to 1.47 Å resolution. However, the dimensions of the asymmetric unit and molecular replacement with a nanobody structure clearly showed that the crystals of the expected complex with JBP1 were of the nanobody alone. Nb6 crystallizes in space group P31 with two molecules in the asymmetric unit; its crystal structure was refined to a final resolution of 1.64 Å. Ensemble refinement suggests that in the ligand-free state one of the complementarity-determining regions (CDRs) is flexible, while the other two adopt well defined conformations.

Expression of high-affinity human antibody fragments in bacteria

2012 ◽  
Vol 7 (2) ◽  
pp. 364-373 ◽  
Author(s):  
Romain Rouet ◽  
David Lowe ◽  
Kip Dudgeon ◽  
Brendan Roome ◽  
Peter Schofield ◽  
...  
Keyword(s):  
Antibody Fragments ◽  
Human Antibody ◽  
High Affinity

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 Passive Protection against Anthrax by Using a High-Affinity Antitoxin Antibody Fragment Lacking an Fc Region

2005 ◽  
Vol 73 (12) ◽  
pp. 8362-8368 ◽  
Author(s):  
Robert Mabry ◽  
Mridula Rani ◽  
Robert Geiger ◽  
Gene B. Hubbard ◽  
Ricardo Carrion ◽  
...  
Keyword(s):  
Viral Infections ◽  
Protective Antigen ◽  
Critical Role ◽  
Passive Immunization ◽  
Antibody Fragment ◽  
Antibody Fragments ◽  
Manufacturing Cost ◽  
High Affinity ◽  
Complement Dependent Cytotoxicity ◽  
Unique Approach

ABSTRACT Passive immunization has been successfully employed for protection against bacterial and viral infections for over 100 years. Immunoglobulin Fc regions play a critical role in the clearance of bacterial pathogens by mediating antibody-dependent and complement-dependent cytotoxicity. Here we show that antibody fragments engineered to recognize the protective antigen component of the B. anthracis exotoxin with high affinity and conjugated to polyethylene glycol (PEG) for prolonged circulation half-life confer significant protection against inhalation anthrax despite their lack of Fc regions. The speed and lower manufacturing cost of bacterially expressed PEGylated antibody fragments could provide decisive advantages for anthrax prophylaxis. Importantly, our results suggest that PEGylated antibody fragments may represent a unique approach for mounting a rapid therapeutic response to emerging pathogen infections.

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