Fragments d’anticorps à domaine unique

Chames, Patrick; Baty, Daniel

doi:10.1051/medsci/200925121159

Cited by 5 publications

(2 citation statements)

References 22 publications

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“…For example, the manufacturing processes in the production capacity of therapeutic antibodies in eukaryotic systems will cause a high cost [ 1 ]. Moreover, the large size of monoclonal antibodies may disturb efficient tissue accessibility and penetration [ 2 ]. Such problems could be solved by obtaining smaller antigen-binding antibody fragments [ 3 ].…”

Section: Introductionmentioning

confidence: 99%

Construction of a synthetic phage-displayed Nanobody library with CDR3 regions randomized by trinucleotide cassettes for diagnostic applications

Yan

et al. 2014

J Transl Med

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BackgroundNanobodies (Nbs) have proved their great value as therapeutic molecules and clinical diagnostic tools. Although the routine procedure to obtain Nbs is to immunize camels with antigens, it is unavailable to immunize a camel when the antigens are highly toxic, pathogenic or nonimmunogenic. A synthetic phage display library is an alternative to generate Nbs against such targets, besides all the other ones.MethodsWe constructed a large and diverse synthetic phage display Nanobody (Nb) library based on the conserved camel single-domain antibody fragment (VHH) framework of cAbBCII10. Diversity was introduced in the complementarity-determining region 3 (CDR3) by means of randomization of synthetic oligonucleotides. Then human prealbumin (PA) and neutrophil gelatinase-associated lipocalin (NGAL) were used to select specific Nbs from this library. Furthermore, a sandwich enzyme-linked immunosorbent assay (ELISA) was developed to detect PA based on horseradish peroxidase (HRP)-conjugated anti-PA Nb isolated from this study and another biotinylated anti-PA Nb obtained from an immune library, in our previous study.ResultsA large and diverse synthetic phage display Nb library with CDR3 regions randomized by trinucleotide cassettes was constructed. The library size was 1.65 × 109 CFU/mL and the correct insertion ratio was nearly 100%. A Nb against human PA and against NGAL was successfully isolated from the synthetic library. The obtained anti-PA Nb was effectively used to develop a sandwich ELISA for PA detection and it demonstrated a working range from 50 to 1000 ng/mL, with a limit of detection (LOD) of 27.1 ng/mL.ConclusionThis proposed novel synthetic library was a good source for obtaining some antigen-specific Nbs. This approach could provide crucial support to an immune library and a naïve library in the acquisition of specific Nbs, potentially functioning as a great resource for medical diagnostic applications. In addition, we have successfully developed a novel sandwich ELISA to detect PA, which could provide great assistance for clinical PA detection.

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Section: Introductionmentioning

confidence: 99%

Construction of a synthetic phage-displayed Nanobody library with CDR3 regions randomized by trinucleotide cassettes for diagnostic applications

Yan

et al. 2014

J Transl Med

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“…Bispecific antibodies act through an amplified cytotoxic signal from tumor localized activated effector T cells, making this an attractive approach for killing quiescent cancer stem cells, cancers overexpressing drug pumps, and cancer cells with low levels of surface antigens [7] . For AML, a bispecific antibody that targets the CD33 antigen, has previously been evaluated [8] .…”

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confidence: 99%

Targeting Human C‐Type Lectin‐like Molecule‐1 (CLL1) with a Bispecific Antibody for Immunotherapy of Acute Myeloid Leukemia

Zhou

Deshmukh

et al. 2014

Angew Chem Int Ed

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Acute myeloid leukemia (AML), the most common acute adult leukemia and the second most common pediatric leukemia, still has a poor prognosis. Human C-type lectin-like molecule-1 (CLL1) is a recently identified myeloid lineage restricted cell surface marker, which is overexpressed in over 90% of AML patient myeloid blasts and in leukemic stem cells. Here, we describe the synthesis of a novel bispecific antibody, αCLL1-αCD3, using the genetically encoded unnatural amino acid, p-acetylphenylalanine. The resulting αCLL1-αCD3 recruits cytotoxic T cells to CLL1 positive cells, and demonstrates potent and selective cytotoxicity against several human AML cell lines and primary AML patient-derived cells in vitro. Moreover, αCLL1-αCD3 treatment completely eliminates established tumors in an U937 AML cell line xenograft model. These results validate the clinical potential of CLL1 as an AML specific antigen for the generation of a novel immunotherapeutic for AML.

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Structure tridimensionnelle du récepteur de l’adénosine A_2Alié à son agoniste naturel l’adénosine

Lebon

Tate

2011

Med Sci (Paris)

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Fragments d’anticorps à domaine unique

Cited by 5 publications

References 22 publications

Construction of a synthetic phage-displayed Nanobody library with CDR3 regions randomized by trinucleotide cassettes for diagnostic applications

Construction of a synthetic phage-displayed Nanobody library with CDR3 regions randomized by trinucleotide cassettes for diagnostic applications

Targeting Human C‐Type Lectin‐like Molecule‐1 (CLL1) with a Bispecific Antibody for Immunotherapy of Acute Myeloid Leukemia

Structure tridimensionnelle du récepteur de l’adénosine A_2Alié à son agoniste naturel l’adénosine

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Fragments d’anticorps à domaine unique

Cited by 5 publications

References 22 publications

Construction of a synthetic phage-displayed Nanobody library with CDR3 regions randomized by trinucleotide cassettes for diagnostic applications

Construction of a synthetic phage-displayed Nanobody library with CDR3 regions randomized by trinucleotide cassettes for diagnostic applications

Targeting Human C‐Type Lectin‐like Molecule‐1 (CLL1) with a Bispecific Antibody for Immunotherapy of Acute Myeloid Leukemia

Structure tridimensionnelle du récepteur de l’adénosine A2Alié à son agoniste naturel l’adénosine

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Structure tridimensionnelle du récepteur de l’adénosine A_2Alié à son agoniste naturel l’adénosine