scholarly journals Monoclonal antibodies with subnanomolar affinity to tenofovir for monitoring adherence to antiretroviral therapies: from hapten synthesis to prototype development

2020 ◽  
Vol 8 (45) ◽  
pp. 10439-10449 ◽  
Author(s):  
Simone Cavalera ◽  
Consuelo Agulló ◽  
Josep V. Mercader ◽  
Fabio Di Nardo ◽  
Matteo Chiarello ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Hiv Infection ◽  
Lateral Flow ◽  
Prototype Development ◽  
High Affinity ◽  
Antiretroviral Therapies ◽  
Hapten Synthesis

High-affinity antibodies were generated to develop enzymatic and lateral flow immunoassays for monitoring tenofovir, a drug commonly used for treating HIV infection and used as a biomarker of adherence to the therapy.

Generation of High Affinity Monoclonal Antibodies for the Prevention of HIV Infection

2009 ◽  
Vol 3 (2) ◽  
pp. 88-95 ◽  
Author(s):  
Nobuo Sakaguchi ◽  
Teppei Toda ◽  
Teruo Nakaya ◽  
Masataka Kitabatake ◽  
Kazuhiko Maeda ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Hiv Infection ◽  
High Affinity ◽  
Prevention Of Hiv

Conformation as the Therapeutic Target for Neurodegenerative Diseases

2017 ◽  
Vol 14 (4) ◽  
pp. 393-402 ◽  
Author(s):  
Rajaraman Krishnan ◽  
Franz Hefti ◽  
Haim Tsubery ◽  
Michal Lulu ◽  
Ming Proschitsky ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Neurodegenerative Diseases ◽  
Protein Misfolding ◽  
Specific Binding ◽  
Drug Candidate ◽  
High Affinity ◽  
Novel Approach ◽  
Multiple Protein ◽  
Clinical Benefits ◽  
Effective Drugs

Therapeutic strategies that target pathways of protein misfolding and the toxicity of intermediates along these pathways are mainly at discovery and early development stages, with the exception of monoclonal antibodies that have mainly failed to produce convincing clinical benefits in late stage trials. The clinical failures represent potentially critical lessons for future neurodegenerative disease drug development. More effective drugs may be achieved by pursuing the following two strategies. First, conformational targeting of aggregates of misfolded proteins, rather than less specific binding that includes monomer subunits, which vastly outnumber the toxic targets. Second, since neurodegenerative diseases frequently include more than one potential protein pathology, generic targeting of aggregates by shape might also be a crucial feature of a drug candidate. Incorporating both of these critical features into a viable drug candidate along with high affinity binding has not been achieved with small molecule approaches or with antibody fragments. Monoclonal antibodies developed so far are not broadly acting through conformational recognition. Using GAIM (General Amyloid Interaction Motif) represents a novel approach that incorporates high affinity conformational recognition for multiple protein assemblies, as well as recognition of an array of assemblies along the misfolding pathway between oligomers and fibers. A GAIM-Ig fusion, NPT088, is nearing clinical testing.

scholarly journals Inhibition of receptor binding and neutralization of bioactivity by anti-erythropoietin monoclonal antibodies

Blood ◽  
1990 ◽  
Vol 75 (4) ◽  
pp. 874-880 ◽  
Author(s):  
AD D'Andrea ◽  
PJ Szklut ◽  
HF Lodish ◽  
EM Alderman
Keyword(s):  
Monoclonal Antibodies ◽  
Receptor Binding ◽  
Sodium Dodecyl ◽  
Dependent Manner ◽  
Epo Receptor ◽  
High Affinity ◽  
Group I ◽  
Dependent Cell ◽  
Group Ii ◽  
Murine Erythroleukemia

Abstract We have generated four high affinity monoclonal antibodies (MoAbs) to recombinant human erythropoietin (EPO). All four MoAbs immunoprecipitate radioiodinated native EPO, and the concentrations of MoAbs required for maximum binding range from 10 nmol/L to 100 nmol/L. Two MoAbs, designated Group I MoAbs, bind to an epitope within the N- terminal 20 amino acids of EPO and also immunoprecipitate sodium dodecyl sulfate (SDS)-denatured EPO. Two other MoAbs (Group II MoAbs) do not immunoprecipitate SDS-denatured EPO and do not bind to any of the eight endo C fragments of EPO. We first used murine erythroleukemia (MEL) cells to test the MoAbs for inhibition of EPO-receptor binding. MEL cells, although unresponsive to EPO, express 760 high affinity receptors for EPO per cell (Kd = 0.24 nmol/L). To assay our MoAbs, MEL cells were grown as monolayers on fibronectin-coated Petri dishes and incubated at 4 degrees C with radioiodinated EPO. Group I MoAbs do not inhibit binding of radioiodinated EPO to the MEL EPO-receptor, but Group II MoAbs do inhibit binding in a dose-dependent manner. We next examined the neutralization of EPO bioactivity by our MoAbs, using EPO- dependent cell line. Only Group II MoAbs inhibit a newly developed EPO- dependent cell growth, demonstrating that inhibition of EPO-receptor binding correlates with neutralization of EPO bioactivity.

scholarly journals Rapid cloning of high-affinity human monoclonal antibodies against influenza virus

Nature ◽  
2008 ◽  
Vol 453 (7195) ◽  
pp. 667-671 ◽  
Author(s):  
Jens Wrammert ◽  
Kenneth Smith ◽  
Joe Miller ◽  
William A. Langley ◽  
Kenneth Kokko ◽  
...  
Keyword(s):  
Influenza Virus ◽  
Monoclonal Antibodies ◽  
Human Monoclonal Antibodies ◽  
High Affinity

A repertoire of high-affinity monoclonal antibodies specific to S. typhi: as potential candidate for improved typhoid diagnostic

2015 ◽  
Vol 62 (3) ◽  
pp. 325-340 ◽  
Author(s):  
Chandresh Sharma ◽  
Anurag Sankhyan ◽  
Tarang Sharma ◽  
Naeem Khan ◽  
Susmita Chaudhuri ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Potential Candidate ◽  
High Affinity

scholarly journals Preparation of Hybridomas Producing Monoclonal Antibodies against Aflatoxin B1 as a Tool to Control Hepatocellular Carcinoma

2019 ◽  
Vol 13 ◽  
pp. 1-12
Author(s):  
Manal M.E. Ahmed ◽  
Rafik Soliman ◽  
Jakeen Eljakee ◽  
Ahmed El-Sanousi ◽  
Haitham Amer ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Aflatoxin B1 ◽  
Quantitative Measurement ◽  
Myeloma Cell ◽  
Selective Medium ◽  
Immunization Schedule ◽  
Spleen Cells ◽  
Myeloma Cell Line ◽  
High Affinity ◽  
Multiple Uses

Hybridomas that secreted antibodies against aflatoxin B1 for multiple uses were prepared using a unique immunization schedule. Aflatoxin B1-BSA conjugate was used for immunization of Balb/c mice. Spleen cells were harvested from the hyper immunized mice to be fused with myeloma cell line (P3NS1) using polyethylene glycol 3000, 50% concentration as a fusogenic agent. The produced hybridomas were selected using HAT selective medium that was replaced by complete HT medium. From the 10thday after fusion, wells that contain colonies of hybridomas covering 30% or greater of the wells surface were screened for production of monoclonal antibodies against aflatoxin B1 using ELISA. 21 hybridomas were found to be reactive to aflatoxin B1. All were found to belong to IgG2aisotype except one was found to belong to IgM isotype. The prepared monoclonal antibodies and their application to immunoassays represents a useful and rapid quantitative measurement with high affinity and low detection limits in order to purify environmentally occurring levels of this carcinogen specially in areas at high risk for liver cancer.

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